https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Jasper+Small 2026-09-14T17:53:48Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=Lactate_Dehydrogenase&diff=1082732 2010-05-05T06:24:51Z

<p>Jasper Small: New page: 200px {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE=== ==Lactate Dehydrogenas...</p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> [[Image:LDH_reaction.jpeg|355px|Catalytic function of LDH (1)]]<br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets&lt;ref name=&quot;2nd&quot;&gt;http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf &lt;/ref&gt;. The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NADH must bind to the enzyme first followed by lactate. Several residues are involved in the binding of NADH, including &lt;scene name='Jasper_Lactate_Final/250_final/1'&gt;Lys 250&lt;/scene&gt; and &lt;scene name='Jasper_Lactate_Final/85_final/1'&gt;Tyr 85&lt;/scene&gt;. Once the NADH is bound to the enzyme, it is then possible for lactate to bind. Lactate binds to the enzyme between the nicotinamide ring and &lt;scene name='Jasper_Lactate_Final/His_195_final/1'&gt;His 195&lt;/scene&gt;. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two tertiary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate .Finally pyruvate dissociates from the enzyme followed by NAD+&lt;ref name=&quot;1st&quot;&gt; http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm&lt;/ref&gt;.<br /> <br /> [[Image:2nd.png|355px|(1)]]<br /> <br /> ==Kinetics==<br /> Kinetic studies of lactate dehydrogenase with oxalate and oxamate (structural analogues of lactate and pyruvate)have proven the mechanism stated above. The rate limiting step in this reaction is the rate of dissociation of NAD+ and NADH. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is very favorable.<br /> <br /> [[Image:Kin.jpg|355px|(1)]]<br /> <br /> ==Regulation==<br /> <br /> As the mechanism is one of equilibrium, There appears to be no regulation specifically designed for lactate dehydrogenase, instead it is dependent on the activation of anaerobic reparation and the presence of pyruvate and NADH, or lactate and NAD+. <br /> <br /> <br /> <br /> ==Reference==<br /> <br /> *1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> *2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf<br /> *3- http://resources.metapress.com/pdf-preview.axd?code=ulnhp23038060m21&amp;size=largest<br /> *4- http://www.u676.org/Documents/Chretien-ClinChimActa-95.pdf<br /> *5- http://www.jbc.org/content/243/17/4526.full.pdf+html</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065233 2010-04-05T12:53:07Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> [[Image:LDH_reaction.jpeg|355px|Catalytic function of LDH (1)]]<br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets&lt;ref name=&quot;2nd&quot;&gt;http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf &lt;/ref&gt;. The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NADH must bind to the enzyme first followed by lactate. Several residues are involved in the binding of NADH, including &lt;scene name='Jasper_Lactate_Final/250_final/1'&gt;Lys 250&lt;/scene&gt; and &lt;scene name='Jasper_Lactate_Final/85_final/1'&gt;Tyr 85&lt;/scene&gt;. Once the NADH is bound to the enzyme, it is then possible for lactate to bind. Lactate binds to the enzyme between the nicotinamide ring and &lt;scene name='Jasper_Lactate_Final/His_195_final/1'&gt;His 195&lt;/scene&gt;. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two tertiary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate .Finally pyruvate dissociates from the enzyme followed by NAD+&lt;ref name=&quot;1st&quot;&gt; http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm&lt;/ref&gt;.<br /> <br /> [[Image:2nd.png|355px|(1)]]<br /> <br /> ==Kinetics==<br /> Kinetic studies of lactate dehydrogenase with oxalate and oxamate (structural analogues of lactate and pyruvate)have proven the mechanism stated above. The rate limiting step in this reaction is the rate of dissociation of NAD+ and NADH. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is very favorable.<br /> <br /> [[Image:Kin.jpg|355px|(1)]]<br /> <br /> ==Regulation==<br /> <br /> As the mechanism is one of equilibrium, There appears to be no regulation specifically designed for lactate dehydrogenase, instead it is dependent on the activation of anaerobic reparation and the presence of pyruvate and NADH, or lactate and NAD+. <br /> <br /> <br /> <br /> ==Reference==<br /> <br /> *1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> *2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf<br /> *3- http://resources.metapress.com/pdf-preview.axd?code=ulnhp23038060m21&amp;size=largest<br /> *4- http://www.u676.org/Documents/Chretien-ClinChimActa-95.pdf<br /> *5- http://www.jbc.org/content/243/17/4526.full.pdf+html</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065232 2010-04-05T12:51:02Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> [[Image:LDH_reaction.jpeg|355px|Catalytic function of LDH (1)]]<br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets&lt;ref name=&quot;2nd&quot;&gt;http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf &lt;/ref&gt;. The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NADH must bind to the enzyme first followed by lactate. Several residues are involved in the binding of NADH, including &lt;scene name='Jasper_Lactate_Final/250_final/1'&gt;Lys 250&lt;/scene&gt; and &lt;scene name='Jasper_Lactate_Final/85_final/1'&gt;Tyr 85&lt;/scene&gt;. Once the NADH is bound to the enzyme, it is then possible for lactate to bind. Lactate binds to the enzyme between the nicotinamide ring and &lt;scene name='Jasper_Lactate_Final/His_195_final/1'&gt;His 195&lt;/scene&gt;. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two tertiary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate .Finally pyruvate dissociates from the enzyme followed by NAD+&lt;ref name=&quot;1st&quot;&gt; http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm&lt;/ref&gt;.<br /> <br /> [[Image:2nd.png|355px|(1)]]<br /> <br /> ==Kinetics==<br /> Kinetic studies of lactate dehydrogenase with oxalate and oxamate (structural analogues of lactate and pyruvate)have proven the mechanism stated above. The rate limiting step in this reaction is the rate of dissociation of NAD+ and NADH. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is very favorable.<br /> <br /> [[Image:Kin.jpg|355px|(1)]]<br /> <br /> ==Regulation==<br /> <br /> As the mechanism is one of equilibrium, There appears to be no regulation specifically designed for lactate dehydrogenase, instead it is dependent on the activation of anaerobic reparation and the presence of pyruvate and NADH, or lactate and NAD+. <br /> <br /> <br /> <br /> ==Reference==<br /> <br /> *1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> *2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf<br /> *3</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065231 2010-04-05T12:49:17Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> [[Image:LDH_reaction.jpeg|355px|Catalytic function of LDH (1)]]<br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets.(2) The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NADH must bind to the enzyme first followed by lactate. Several residues are involved in the binding of NADH, including &lt;scene name='Jasper_Lactate_Final/250_final/1'&gt;Lys 250&lt;/scene&gt; and &lt;scene name='Jasper_Lactate_Final/85_final/1'&gt;Tyr 85&lt;/scene&gt;. Once the NADH is bound to the enzyme, it is then possible for lactate to bind. Lactate binds to the enzyme between the nicotinamide ring and &lt;scene name='Jasper_Lactate_Final/His_195_final/1'&gt;His 195&lt;/scene&gt;. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two tertiary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate .Finally pyruvate dissociates from the enzyme followed by NAD+&lt;ref name=&quot;1st&quot;&gt; http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm&lt;/ref&gt;.<br /> <br /> [[Image:2nd.png|355px|(1)]]<br /> <br /> ==Kinetics==<br /> Kinetic studies of lactate dehydrogenase with oxalate and oxamate (structural analogues of lactate and pyruvate)have proven the mechanism stated above. The rate limiting step in this reaction is the rate of dissociation of NAD+ and NADH. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is very favorable.<br /> <br /> [[Image:Kin.jpg|355px|(1)]]<br /> <br /> ==Regulation==<br /> <br /> As the mechanism is one of equilibrium, There appears to be no regulation specifically designed for lactate dehydrogenase, instead it is dependent on the activation of anaerobic reparation and the presence of pyruvate and NADH, or lactate and NAD+. <br /> <br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065230 2010-04-05T12:44:59Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> [[Image:LDH_reaction.jpeg|355px|Catalytic function of LDH (1)]]<br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets.(2) The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NADH must bind to the enzyme first followed by lactate. Several residues are involved in the binding of NADH, including &lt;scene name='Jasper_Lactate_Final/250_final/1'&gt;Lys 250&lt;/scene&gt; and &lt;scene name='Jasper_Lactate_Final/85_final/1'&gt;Tyr 85&lt;/scene&gt;. Once the NADH is bound to the enzyme, it is then possible for lactate to bind. Lactate binds to the enzyme between the nicotinamide ring and &lt;scene name='Jasper_Lactate_Final/His_195_final/1'&gt;His 195&lt;/scene&gt;. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two tertiary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate .Finally pyruvate dissociates from the enzyme followed by NAD+.<br /> <br /> [[Image:2nd.png|355px|(1)]]<br /> <br /> ==Kinetics==<br /> Kinetic studies of lactate dehydrogenase with oxalate and oxamate (structural analogues of lactate and pyruvate)have proven the mechanism stated above. The rate limiting step in this reaction is the rate of dissociation of NAD+ and NADH. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is very favorable.<br /> <br /> [[Image:Kin.jpg|355px|(1)]]<br /> <br /> ==Regulation==<br /> <br /> As the mechanism is one of equilibrium, There appears to be no regulation specifically designed for lactate dehydrogenase, instead it is dependent on the activation of anaerobic reparation and the presence of pyruvate and NADH, or lactate and NAD+. <br /> <br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065229 2010-04-05T12:35:32Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> [[Image:LDH_reaction.jpeg|355px|Catalytic function of LDH (1)]]<br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets.(2) The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NADH must bind to the enzyme first followed by lactate. Several residues are involved in the binding of NADH, including &lt;scene name='Jasper_Lactate_Final/250_final/1'&gt;Lys 250&lt;/scene&gt; and &lt;scene name='Jasper_Lactate_Final/85_final/1'&gt;Tyr 85&lt;/scene&gt;. Once the NADH is bound to the enzyme, it is then possible for lactate to bind. Lactate binds to the enzyme between the nicotinamide ring and &lt;scene name='Jasper_Lactate_Final/His_195_final/1'&gt;His 195&lt;/scene&gt;. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two tertiary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate .Finally pyruvate dissociates from the enzyme followed by NAD+.<br /> <br /> [[Image:2nd.png|355px|(1)]]<br /> <br /> ==Kinetics==<br /> Kinetic studies of lactate dehydrogenase with oxalate and oxamate (structural analogues of lactate and pyruvate)have proven the mechanism stated above. The rate limiting step in this reaction is the rate of dissociation of NAD+ and NADH. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is very favorable.<br /> <br /> [[Image:Kin.jpg|355px|(1)]]<br /> <br /> <br /> <br /> <br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065228 2010-04-05T12:34:19Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> [[Image:LDH_reaction.jpeg|355px|Catalytic function of LDH (1)]]<br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets.(2) The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NADH must bind to the enzyme first followed by lactate. Several residues are involved in the binding of NADH, including &lt;scene name='Jasper_Lactate_Final/250_final/1'&gt;Lys 250&lt;/scene&gt; and &lt;scene name='Jasper_Lactate_Final/85_final/1'&gt;Tyr 85&lt;/scene&gt;. Once the NADH is bound to the enzyme, it is then possible for lactate to bind. Lactate binds to the enzyme between the nicotinamide ring and &lt;scene name='Jasper_Lactate_Final/His_195_final/1'&gt;His 195&lt;/scene&gt;. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two tertiary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NAD+.<br /> [[Image:2nd.png|355px|(1)]]<br /> <br /> ==Kinetics==<br /> Kinetic studies of lactate dehydrogenase with oxalate and oxamate (structural analogues of lactate and pyruvate)have proven the mechanism stated above. The rate limiting step in this reaction is the rate of dissociation of NAD+ and NADH. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is very favorable.<br /> [[Image:Kin.jpg|355px|(1)]]<br /> <br /> <br /> <br /> <br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065227 2010-04-05T12:33:48Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> [[Image:LDH_reaction.jpeg|355px|Catalytic function of LDH (1)]]<br /> <br /> <br /> <br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets.(2) The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NADH must bind to the enzyme first followed by lactate. Several residues are involved in the binding of NADH, including &lt;scene name='Jasper_Lactate_Final/250_final/1'&gt;Lys 250&lt;/scene&gt; and &lt;scene name='Jasper_Lactate_Final/85_final/1'&gt;Tyr 85&lt;/scene&gt;. Once the NADH is bound to the enzyme, it is then possible for lactate to bind. Lactate binds to the enzyme between the nicotinamide ring and &lt;scene name='Jasper_Lactate_Final/His_195_final/1'&gt;His 195&lt;/scene&gt;. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two tertiary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NAD+.<br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> <br /> <br /> <br /> <br /> <br /> <br /> ==Kinetics==<br /> Kinetic studies of lactate dehydrogenase with oxalate and oxamate (structural analogues of lactate and pyruvate)have proven the mechanism stated above. The rate limiting step in this reaction is the rate of dissociation of NAD+ and NADH. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is very favorable.<br /> [[Image:Kin.jpg|left|thumb|355px|(1)]]<br /> <br /> <br /> <br /> <br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065226 2010-04-05T12:33:12Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> <br /> <br /> <br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets.(2) The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NADH must bind to the enzyme first followed by lactate. Several residues are involved in the binding of NADH, including &lt;scene name='Jasper_Lactate_Final/250_final/1'&gt;Lys 250&lt;/scene&gt; and &lt;scene name='Jasper_Lactate_Final/85_final/1'&gt;Tyr 85&lt;/scene&gt;. Once the NADH is bound to the enzyme, it is then possible for lactate to bind. Lactate binds to the enzyme between the nicotinamide ring and &lt;scene name='Jasper_Lactate_Final/His_195_final/1'&gt;His 195&lt;/scene&gt;. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two tertiary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NAD+.<br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> <br /> <br /> <br /> <br /> <br /> <br /> ==Kinetics==<br /> Kinetic studies of lactate dehydrogenase with oxalate and oxamate (structural analogues of lactate and pyruvate)have proven the mechanism stated above. The rate limiting step in this reaction is the rate of dissociation of NAD+ and NADH. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is very favorable.<br /> [[Image:Kin.jpg|left|thumb|355px|(1)]]<br /> <br /> <br /> <br /> <br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065225 2010-04-05T12:32:08Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> <br /> <br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> <br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets.(2) The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NADH must bind to the enzyme first followed by lactate. Several residues are involved in the binding of NADH, including &lt;scene name='Jasper_Lactate_Final/250_final/1'&gt;Lys 250&lt;/scene&gt; and &lt;scene name='Jasper_Lactate_Final/85_final/1'&gt;Tyr 85&lt;/scene&gt;. Once the NADH is bound to the enzyme, it is then possible for lactate to bind. Lactate binds to the enzyme between the nicotinamide ring and &lt;scene name='Jasper_Lactate_Final/His_195_final/1'&gt;His 195&lt;/scene&gt;. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two tertiary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NAD+.<br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> <br /> <br /> <br /> ==Kinetics==<br /> Kinetic studies of lactate dehydrogenase with oxalate and oxamate (structural analogues of lactate and pyruvate)have proven the mechanism stated above. The rate limiting step in this reaction is the rate of dissociation of NAD+ and NADH. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is very favorable.<br /> [[Image:Kin.jpg|left|thumb|355px|(1)]]<br /> <br /> <br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065224 2010-04-05T12:31:42Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> <br /> <br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> <br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets.(2) The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NADH must bind to the enzyme first followed by lactate. Several residues are involved in the binding of NADH, including &lt;scene name='Jasper_Lactate_Final/250_final/1'&gt;Lys 250&lt;/scene&gt; and &lt;scene name='Jasper_Lactate_Final/85_final/1'&gt;Tyr 85&lt;/scene&gt;. Once the NADH is bound to the enzyme, it is then possible for lactate to bind. Lactate binds to the enzyme between the nicotinamide ring and &lt;scene name='Jasper_Lactate_Final/His_195_final/1'&gt;His 195&lt;/scene&gt;. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two tertiary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NAD+.<br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> <br /> ==Kinetics==<br /> Kinetic studies of lactate dehydrogenase with oxalate and oxamate (structural analogues of lactate and pyruvate)have proven the mechanism stated above. The rate limiting step in this reaction is the rate of dissociation of NAD+ and NADH. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is very favorable.<br /> [[Image:Kin.jpg|left|thumb|355px|(1)]]<br /> <br /> <br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065223 2010-04-05T12:31:00Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> <br /> <br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> <br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets.(2) The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NADH must bind to the enzyme first followed by lactate. Several residues are involved in the binding of NADH, including &lt;scene name='Jasper_Lactate_Final/250_final/1'&gt;Lys 250&lt;/scene&gt; and &lt;scene name='Jasper_Lactate_Final/85_final/1'&gt;Tyr 85&lt;/scene&gt;. Once the NADH is bound to the enzyme, it is then possible for lactate to bind. Lactate binds to the enzyme between the nicotinamide ring and &lt;scene name='Jasper_Lactate_Final/His_195_final/1'&gt;His 195&lt;/scene&gt;. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two tertiary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NAD+.<br /> <br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> <br /> ==Kinetics==<br /> Kinetic studies of lactate dehydrogenase with oxalate and oxamate (structural analogues of lactate and pyruvate)have proven the mechanism stated above. The rate limiting step in this reaction is the rate of dissociation of NAD+ and NADH. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is very favorable.<br /> <br /> <br /> <br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065222 2010-04-05T12:30:13Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> <br /> <br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> <br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets.(2) The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> ==Catalysis==<br /> Kinetic studies of lactate dehydrogenase with oxalate and oxamate (structural analogues of lactate and pyruvate)have proven the mechanism stated above. The rate limiting step in this reaction is the rate of dissociation of NAD+ and NADH. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is very favorable.<br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NADH must bind to the enzyme first followed by lactate. Several residues are involved in the binding of NADH, including &lt;scene name='Jasper_Lactate_Final/250_final/1'&gt;Lys 250&lt;/scene&gt; and &lt;scene name='Jasper_Lactate_Final/85_final/1'&gt;Tyr 85&lt;/scene&gt;. Once the NADH is bound to the enzyme, it is then possible for lactate to bind. Lactate binds to the enzyme between the nicotinamide ring and &lt;scene name='Jasper_Lactate_Final/His_195_final/1'&gt;His 195&lt;/scene&gt;. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two tertiary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NAD+.<br /> <br /> ==Kinetics==<br /> asdf<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> <br /> <br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065221 2010-04-05T12:29:45Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> <br /> <br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> <br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets.(2) The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> ==Catalysis==<br /> Kinetic studies of lactate dehydrogenase with oxalate and oxamate (structural analogues of lactate and pyruvate)have proven the mechanism stated above. The rate limiting step in this reaction is the rate of dissociation of NAD+ and NADH. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is very favorable.<br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NADH must bind to the enzyme first followed by lactate. Several residues are involved in the binding of NADH, including &lt;scene name='Jasper_Lactate_Final/250_final/1'&gt;Lys 250&lt;/scene&gt; and &lt;scene name='Jasper_Lactate_Final/85_final/1'&gt;Tyr 85&lt;/scene&gt;. Once the NADH is bound to the enzyme, it is then possible for lactate to bind. Lactate binds to the enzyme between the nicotinamide ring and &lt;scene name='Jasper_Lactate_Final/His_195_final/1'&gt;His 195&lt;/scene&gt;. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two tertiary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NAD+.<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> <br /> <br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065220 2010-04-05T12:26:45Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> <br /> <br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> <br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets.(2) The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> ==Kinetics==<br /> Kinetic studies of lactate dehydrogenase with oxalate and oxamate (structural analogues of lactate and pyruvate)have proven the mechanism stated above. The rate limiting step in this reaction is the rate of dissociation of NAD+ and NADH. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is very favorable.<br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NADH must bind to the enzyme first followed by lactate. Several residues are involved in the binding of NADH, including &lt;scene name='Jasper_Lactate_Final/250_final/1'&gt;Lys 250&lt;/scene&gt; and &lt;scene name='Jasper_Lactate_Final/85_final/1'&gt;Tyr 85&lt;/scene&gt;. Once the NADH is bound to the enzyme, it is then possible for lactate to bind. Lactate binds to the enzyme between the nicotinamide ring and &lt;scene name='Jasper_Lactate_Final/His_195_final/1'&gt;His 195&lt;/scene&gt;. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two tertiary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NAD+.<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> <br /> <br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065219 2010-04-05T12:26:28Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> <br /> <br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> <br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets.(2) The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> ==Kinetics==<br /> Kinetic studies of lactate dehydrogenase with oxalate and oxamate (structural analogues of lactate and pyruvate)have proven the mechanism stated above. The rate limiting step in this reaction is the rate of dissociation of NAD+ and NADH. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is very favorable(1).<br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NADH must bind to the enzyme first followed by lactate. Several residues are involved in the binding of NADH, including &lt;scene name='Jasper_Lactate_Final/250_final/1'&gt;Lys 250&lt;/scene&gt; and &lt;scene name='Jasper_Lactate_Final/85_final/1'&gt;Tyr 85&lt;/scene&gt;. Once the NADH is bound to the enzyme, it is then possible for lactate to bind. Lactate binds to the enzyme between the nicotinamide ring and &lt;scene name='Jasper_Lactate_Final/His_195_final/1'&gt;His 195&lt;/scene&gt;. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two tertiary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NAD+.<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> <br /> <br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065218 2010-04-05T12:25:39Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> <br /> <br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> <br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets.(2) The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NADH must bind to the enzyme first followed by lactate. Several residues are involved in the binding of NADH, including &lt;scene name='Jasper_Lactate_Final/250_final/1'&gt;Lys 250&lt;/scene&gt; and &lt;scene name='Jasper_Lactate_Final/85_final/1'&gt;Tyr 85&lt;/scene&gt;. Once the NADH is bound to the enzyme, it is then possible for lactate to bind. Lactate binds to the enzyme between the nicotinamide ring and &lt;scene name='Jasper_Lactate_Final/His_195_final/1'&gt;His 195&lt;/scene&gt;. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two tertiary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NAD+.<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> <br /> ==Kinetics==<br /> Kinetic studies of lactate dehydrogenase with oxalate and oxamate (structural analogues of lactate and pyruvate)have proven the mechanism stated above. The rate limiting step in this reaction is the rate of dissociation of NAD+ and NADH. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is very favorable(1).<br /> <br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065217 2010-04-05T12:25:21Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> <br /> <br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> <br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets.(2) The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NADH must bind to the enzyme first followed by lactate. Several residues are involved in the binding of NADH, including &lt;scene name='Jasper_Lactate_Final/250_final/1'&gt;Lys 250&lt;/scene&gt; and &lt;scene name='Jasper_Lactate_Final/85_final/1'&gt;Tyr 85&lt;/scene&gt;. Once the NADH is bound to the enzyme, it is then possible for lactate to bind. Lactate binds to the enzyme between the nicotinamide ring and &lt;scene name='Jasper_Lactate_Final/His_195_final/1'&gt;His 195&lt;/scene&gt;. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two tertiary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NAD+.<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> <br /> ==Kinetics==<br /> Kinetic studies of lactate dehydrogenase with oxalate and oxamate (structural analogues of lactate and pyruvate)have proven the mechanism stated above. The rate limiting step in this reaction is the rate of dissociation of NAD+ and NADH. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is very favorable(1).<br /> [[Image:kin.jpg|left|thumb|355px|(1)]]<br /> <br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065216 2010-04-05T12:24:14Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> <br /> <br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> <br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets.(2) The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NADH must bind to the enzyme first followed by lactate. Several residues are involved in the binding of NADH, including &lt;scene name='Jasper_Lactate_Final/250_final/1'&gt;Lys 250&lt;/scene&gt; and &lt;scene name='Jasper_Lactate_Final/85_final/1'&gt;Tyr 85&lt;/scene&gt;. Once the NADH is bound to the enzyme, it is then possible for lactate to bind. Lactate binds to the enzyme between the nicotinamide ring and &lt;scene name='Jasper_Lactate_Final/His_195_final/1'&gt;His 195&lt;/scene&gt;. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two tertiary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NAD+.<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> <br /> ==Kinetics==<br /> Kinetic studies of lactate dehydrogenase with oxalate and oxamate (structural analogues of lactate and pyruvate)have proven the mechanism stated above. The rate limiting step in this reaction is the rate of dissociation of NAD+ and NADH. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable(1).<br /> <br /> [[Image:kin.jpg|left|thumb|355px|(1)]]<br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=File:Kin.jpg&diff=1065215 2010-04-05T12:23:15Z

<p>Jasper Small: </p> <hr /> <div></div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065214 2010-04-05T12:22:50Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> <br /> <br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> <br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets.(2) The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NADH must bind to the enzyme first followed by lactate. Several residues are involved in the binding of NADH, including &lt;scene name='Jasper_Lactate_Final/250_final/1'&gt;Lys 250&lt;/scene&gt; and &lt;scene name='Jasper_Lactate_Final/85_final/1'&gt;Tyr 85&lt;/scene&gt;. Once the NADH is bound to the enzyme, it is then possible for lactate to bind. Lactate binds to the enzyme between the nicotinamide ring and &lt;scene name='Jasper_Lactate_Final/His_195_final/1'&gt;His 195&lt;/scene&gt;. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two tertiary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NAD+.<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> <br /> ==Kinetics==<br /> Kinetic studies of lactate dehydrogenase with oxalate and oxamate (structural analogues of lactate and pyruvate)have proven the mechanism stated above. The rate limiting step in this reaction is the rate of dissociation of NAD+ and NADH. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable(1).<br /> [[Image:kin.jpg|thumb|(1)]]<br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065213 2010-04-05T12:01:30Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> <br /> <br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> <br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets.(2) The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NADH must bind to the enzyme first followed by lactate. Several residues are involved in the binding of NADH, including &lt;scene name='Jasper_Lactate_Final/250_final/1'&gt;Lys 250&lt;/scene&gt; and &lt;scene name='Jasper_Lactate_Final/85_final/1'&gt;Tyr 85&lt;/scene&gt;. Once the NADH is bound to the enzyme, it is then possible for lactate to bind. Lactate binds to the enzyme between the nicotinamide ring and &lt;scene name='Jasper_Lactate_Final/His_195_final/1'&gt;His 195&lt;/scene&gt;. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two tertiary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NAD+. The rate limiting step in this reaction is the rate of dissociation of NAD+. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable(1).<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065212 2010-04-05T11:59:07Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> <br /> <br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> <br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets.(2) The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NADH must bind to the enzyme first followed by lactate. Several residues are involved in the binding of NADH, including &lt;scene name='Jasper_Lactate_Final/250_final/1'&gt;Lys 250&lt;/scene&gt; and Tyr 85. Once the NADH is bound to the enzyme, it is then possible for lactate to bind. Lactate binds to the enzyme between the nicotinamide ring and &lt;scene name='Jasper_Lactate_Final/His_195_final/1'&gt;His 195&lt;/scene&gt;. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two tertiary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NAD+. The rate limiting step in this reaction is the rate of dissociation of NAD+. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable(1).<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065211 2010-04-05T11:56:34Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> <br /> <br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> <br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets.(2) The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NADH must bind to the enzyme first followed by lactate. Several residues are involved in the binding of NADH, including Lys 250 and Tyr 85. Once the NADH is bound to the enzyme, it is then possible for lactate to bind. Lactate binds to the enzyme between the nicotinamide ring and &lt;scene name='Jasper_Lactate_Final/His_195_final/1'&gt;His 195&lt;/scene&gt;. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two tertiary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NAD+. The rate limiting step in this reaction is the rate of dissociation of NAD+. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable(1).<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065209 2010-04-05T11:48:27Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> <br /> <br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> <br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets.(2) The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NADH must bind to the enzyme first followed by lactate. Several residues are involved in the binding of NADH, including Lys 250 and Tyr 85. Once the NADH is bound to the enzyme, it is then possible for lactate to bind. Lactate binds to the enzyme between the nicotinamide ring and &lt;scene name='Jasper_Small_Lactate_Sandbox_1/His_195/1'&gt;HIS 195&lt;/scene&gt;. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two tertiary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NAD+. The rate limiting step in this reaction is the rate of dissociation of NAD+. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable(1).<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065208 2010-04-05T11:44:42Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> <br /> <br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> <br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets.(2) The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NAD+ must bind to the enzyme first followed by lactate. Several residues are involved in the binding of NAD+, including Lys 250 and Tyr 85. Once the NAD+ is bound to the enzyme, it is then possible for lactate to bind. Lactate binds to the enzyme between the nicotinamide ring and &lt;scene name='Jasper_Small_Lactate_Sandbox_1/His_195/1'&gt;HIS 195&lt;/scene&gt;. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two tertiary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NADH. The rate limiting step in this reaction is the rate of dissociation of NADH. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable(1).<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> Important Sites:<br /> *<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_109/1'&gt;ARG 109&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Asp_168/1'&gt;ASP 168&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_171/1'&gt;ARG 171&lt;/scene&gt;<br /> <br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065207 2010-04-05T11:31:03Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> <br /> <br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> <br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH as shown here is comprised of 40% alpha helices and 23% beta sheets.(2) The SCOP data classifies this form of lactate dehydrogenase as mixed beta-alpha-beta, with mainly parallel beta sheets. <br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NAD+ must bind to the enzyme first followed by lactate. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two teranary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NADH. The rate limiting step in this reaction is the rate of dissociation of NADH. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable(1).<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> Important Sites:<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/His_195/1'&gt;HIS 195&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_109/1'&gt;ARG 109&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Asp_168/1'&gt;ASP 168&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_171/1'&gt;ARG 171&lt;/scene&gt;<br /> <br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065206 2010-04-05T11:25:13Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> <br /> <br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> <br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The &lt;scene name='Jasper_Lactate_Final/Secondary/1'&gt;secondary structure&lt;/scene&gt; of LDH is comprised of 40% alpha helices and 23% beta sheets.(2)<br /> SCOP<br /> 1I10- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> 1I0Z- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NAD+ must bind to the enzyme first followed by lactate. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two teranary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NADH. The rate limiting step in this reaction is the rate of dissociation of NADH. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable(1).<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> Important Sites:<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/His_195/1'&gt;HIS 195&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_109/1'&gt;ARG 109&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Asp_168/1'&gt;ASP 168&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_171/1'&gt;ARG 171&lt;/scene&gt;<br /> <br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1065205 2010-04-05T11:19:57Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> <br /> <br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> <br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The secondary structure of LDH is comprised of 40% alpha helices and 23% beta sheets.(2)<br /> SCOP<br /> 1I10- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> 1I0Z- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NAD+ must bind to the enzyme first followed by lactate. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two teranary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NADH. The rate limiting step in this reaction is the rate of dissociation of NADH. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable(1).<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> Important Sites:<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/His_195/1'&gt;HIS 195&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_109/1'&gt;ARG 109&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Asp_168/1'&gt;ASP 168&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_171/1'&gt;ARG 171&lt;/scene&gt;<br /> <br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Small_Lactate_Sandbox_1&diff=1065204 2010-04-05T11:16:02Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'&gt;Lactate Dehydrogenase (LDH)&lt;/scene&gt; is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> <br /> <br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> <br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The secondary structure of LDH is comprised of 40% alpha helices and 23% beta sheets.(2)<br /> SCOP<br /> 1I10- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> 1I0Z- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NAD+ must bind to the enzyme first followed by lactate. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two teranary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NADH. The rate limiting step in this reaction is the rate of dissociation of NADH. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable(1).<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> Important Sites:<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/His_195/1'&gt;HIS 195&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_109/1'&gt;ARG 109&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Asp_168/1'&gt;ASP 168&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_171/1'&gt;ARG 171&lt;/scene&gt;<br /> <br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Small_Lactate_Sandbox_1&diff=1065203 2010-04-05T11:04:03Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> Lactate Dehydrogenase (LDH) is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> <br /> <br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> <br /> <br /> ==Structure==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> The secondary structure of LDH is comprised of 40% alpha helices and 23% beta sheets.(2)<br /> SCOP<br /> 1I10- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> 1I0Z- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NAD+ must bind to the enzyme first followed by lactate. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two teranary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NADH. The rate limiting step in this reaction is the rate of dissociation of NADH. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable(1).<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> Important Sites:<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/His_195/1'&gt;HIS 195&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_109/1'&gt;ARG 109&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Asp_168/1'&gt;ASP 168&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_171/1'&gt;ARG 171&lt;/scene&gt;<br /> <br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Small_Lactate_Sandbox_1&diff=1065202 2010-04-05T11:03:04Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> Lactate Dehydrogenase (LDH) is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+. <br /> <br /> <br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> <br /> <br /> ==Forms==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NAD+ must bind to the enzyme first followed by lactate. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two teranary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NADH. The rate limiting step in this reaction is the rate of dissociation of NADH. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable(1).<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> Important Sites:<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/His_195/1'&gt;HIS 195&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_109/1'&gt;ARG 109&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Asp_168/1'&gt;ASP 168&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_171/1'&gt;ARG 171&lt;/scene&gt;<br /> <br /> ==Structure==<br /> <br /> The secondary structure of LDH is comprised of 40% alpha helices and 23% beta sheets.(2)<br /> <br /> SCOP<br /> 1I10- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> 1I0Z- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Small_Lactate_Sandbox_1&diff=1065201 2010-04-05T10:43:58Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> Lactate Dehydrogenase (LDH) is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in homolactic fermentation. Homolactic fermentation is the anaerobic conversion of pyruvate into lactate acid, and the conversion of NADH back into NAD+. This is important as NAD+ is consumed and NADH is created in glycolysis, when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate. <br /> <br /> ==Function==<br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> LDH preforms an important metabolic function in the body. The enzyme catalyzes both the conversion of pyruvate to lactose as well as the conversion of lactose to pyruvate. The conversion of pyruvate to lactose occurs in the muscles of the body when oxygen is absent. The lactate acid is then moved back to the liver where LDH catalyzes the Cori cycle which converts the lactose back into pyruvate. The reaction is also important as it is coupled with the interconversion of NADH and NAD+.<br /> <br /> ==Forms==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NAD+ must bind to the enzyme first followed by lactate. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two teranary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NADH. The rate limiting step in this reaction is the rate of dissociation of NADH. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable(1).<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> Important Sites:<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/His_195/1'&gt;HIS 195&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_109/1'&gt;ARG 109&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Asp_168/1'&gt;ASP 168&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_171/1'&gt;ARG 171&lt;/scene&gt;<br /> <br /> ==Structure==<br /> <br /> The secondary structure of LDH is comprised of 40% alpha helices and 23% beta sheets.(2)<br /> <br /> SCOP<br /> 1I10- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> 1I0Z- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Small_Lactate_Sandbox_1&diff=1065191 2010-04-05T00:14:51Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> Lactate Dehydrogenase (LDH) is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver.<br /> <br /> ==Function==<br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> LDH preforms an important metabolic function in the body. The enzyme catalyzes both the conversion of pyruvate to lactose as well as the conversion of lactose to pyruvate. The conversion of pyruvate to lactose occurs in the muscles of the body when oxygen is absent. The lactate acid is then moved back to the liver where LDH catalyzes the Cori cycle which converts the lactose back into pyruvate. The reaction is also important as it is coupled with the interconversion of NADH and NAD+.<br /> <br /> ==Forms==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NAD+ must bind to the enzyme first followed by lactate. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two teranary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NADH. The rate limiting step in this reaction is the rate of dissociation of NADH. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable(1).<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> Important Sites:<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/His_195/1'&gt;HIS 195&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_109/1'&gt;ARG 109&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Asp_168/1'&gt;ASP 168&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_171/1'&gt;ARG 171&lt;/scene&gt;<br /> <br /> ==Structure==<br /> <br /> The secondary structure of LDH is comprised of 40% alpha helices and 23% beta sheets.(2)<br /> <br /> SCOP<br /> 1I10- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> 1I0Z- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1051260 2010-03-03T09:31:16Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> Lactate Dehydrogenase (LDH) is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver.<br /> <br /> ==Function==<br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> LDH preforms an important metabolic function in the body. The enzyme catalyzes both the conversion of pyruvate to lactose as well as the conversion of lactose to pyruvate. The conversion of pyruvate to lactose occurs in the muscles of the body when oxygen is absent. The lactate acid is then moved back to the liver where LDH catalyzes the Cori cycle which converts the lactose back into pyruvate. The reaction is also important as it is coupled with the interconversion of NADH and NAD+.<br /> <br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NAD+ must bind to the enzyme first followed by lactate. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two teranary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NADH. The rate limiting step in this reaction is the rate of dissociation of NADH. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable(1).<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> Important Sites:<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/His_195/1'&gt;HIS 195&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_109/1'&gt;ARG 109&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Asp_168/1'&gt;ASP 168&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_171/1'&gt;ARG 171&lt;/scene&gt;<br /> <br /> ==Structure==<br /> <br /> LDH is comprized of 40% alpha helixes and 23% beta sheets.(2)<br /> <br /> SCOP<br /> 1I10- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> 1I0Z- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> <br /> ===Forms===<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1051259 2010-03-03T09:30:03Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> Lactate Dehydrogenase (LDH) is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver.<br /> <br /> ==Function==<br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> LDH preforms an important metabolic function in the body. The enzyme catalyzes both the conversion of pyruvate to lactose as well as the conversion of lactose to pyruvate. The conversion of pyruvate to lactose occurs in the muscles of the body when oxygen is absent. The lactate acid is then moved back to the liver where LDH catalyzes the Cori cycle which converts the lactose back into pyruvate. The reaction is also important as it is coupled with the interconversion of NADH and NAD+.<br /> <br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NAD+ must bind to the enzyme first followed by lactate. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two teranary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NADH. The rate limiting step in this reaction is the rate of dissociation of NADH. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable(1).<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> Important Sites:<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/His_195/1'&gt;HIS 195&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_109/1'&gt;ARG 109&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Asp_168/1'&gt;ASP 168&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_171/1'&gt;ARG 171&lt;/scene&gt;<br /> <br /> ==Structure==<br /> <br /> LDH is comprized of 40% alpha helixes and 23% beta sheets.(2)<br /> <br /> SCOP<br /> 1I10- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> 1I0Z- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> <br /> =Forms=<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Lactate_Final&diff=1051258 2010-03-03T09:28:32Z

<p>Jasper Small: New page: 200px {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE=== ==Lactate Dehydrogenas...</p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> Lactate Dehydrogenase (LDH) is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver.<br /> <br /> ==Function==<br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> LDH preforms an important metabolic function in the body. The enzyme catalyzes both the conversion of pyruvate to lactose as well as the conversion of lactose to pyruvate. The conversion of pyruvate to lactose occurs in the muscles of the body when oxygen is absent. The lactate acid is then moved back to the liver where LDH catalyzes the Cori cycle which converts the lactose back into pyruvate. The reaction is also important as it is coupled with the interconversion of NADH and NAD+.<br /> <br /> ==Forms==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NAD+ must bind to the enzyme first followed by lactate. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two teranary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NADH. The rate limiting step in this reaction is the rate of dissociation of NADH. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable(1).<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> Important Sites:<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/His_195/1'&gt;HIS 195&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_109/1'&gt;ARG 109&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Asp_168/1'&gt;ASP 168&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_171/1'&gt;ARG 171&lt;/scene&gt;<br /> <br /> ==Structure==<br /> <br /> LDH is comprized of 40% alpha helixes and 23% beta sheets.(2)<br /> <br /> SCOP<br /> 1I10- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> 1I0Z- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Small_Lactate_Sandbox_1&diff=1051257 2010-03-03T09:26:41Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> Lactate Dehydrogenase (LDH) is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver.<br /> <br /> ==Function==<br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> LDH preforms an important metabolic function in the body. The enzyme catalyzes both the conversion of pyruvate to lactose as well as the conversion of lactose to pyruvate. The conversion of pyruvate to lactose occurs in the muscles of the body when oxygen is absent. The lactate acid is then moved back to the liver where LDH catalyzes the Cori cycle which converts the lactose back into pyruvate. The reaction is also important as it is coupled with the interconversion of NADH and NAD+.<br /> <br /> ==Forms==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> *(4H) Heart<br /> *(3H1M) Reticuloendothelial<br /> *(2H2M) Lungs<br /> *(1H3M) Kidneys<br /> *(4M) Muscle and Liver<br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NAD+ must bind to the enzyme first followed by lactate. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two teranary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NADH. The rate limiting step in this reaction is the rate of dissociation of NADH. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable(1).<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> Important Sites:<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/His_195/1'&gt;HIS 195&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_109/1'&gt;ARG 109&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Asp_168/1'&gt;ASP 168&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_171/1'&gt;ARG 171&lt;/scene&gt;<br /> <br /> ==Structure==<br /> <br /> LDH is comprized of 40% alpha helixes and 23% beta sheets.(2)<br /> <br /> SCOP<br /> 1I10- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> 1I0Z- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Small_Lactate_Sandbox_1&diff=1051256 2010-03-03T09:24:09Z

<p>Jasper Small: </p> <hr /> <div>[[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> Lactate Dehydrogenase (LDH) is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver.<br /> <br /> ==Function==<br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> LDH preforms an important metabolic function in the body. The enzyme catalyzes both the conversion of pyruvate to lactose as well as the conversion of lactose to pyruvate. The conversion of pyruvate to lactose occurs in the muscles of the body when oxygen is absent. The lactate acid is then moved back to the liver where LDH catalyzes the Cori cycle which converts the lactose back into pyruvate. The reaction is also important as it is coupled with the interconversion of NADH and NAD+.<br /> <br /> ==Forms==<br /> <br /> LDH is a quaternary protein formed of the combination of two subunits, M and H (Muscle and Heart) into a structure of four of the subunits. The various combinations found in the human body are:<br /> * LDH-1 (4H) - in the heart<br /> * LDH-2 (3H1M) - in the reticuloendothelial system<br /> * LDH-3 (2H2M) - in the lungs<br /> * LDH-4 (1H3M) - in the kidneys<br /> * LDH-5 (4M) - in the liver and striated muscle<br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NAD+ must bind to the enzyme first followed by lactate. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two teranary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NADH. The rate limiting step in this reaction is the rate of dissociation of NADH. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable(1).<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> Important Sites:<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/His_195/1'&gt;HIS 195&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_109/1'&gt;ARG 109&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Asp_168/1'&gt;ASP 168&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_171/1'&gt;ARG 171&lt;/scene&gt;<br /> <br /> ==Structure==<br /> <br /> LDH is comprized of 40% alpha helixes and 23% beta sheets.(2)<br /> <br /> SCOP<br /> 1I10- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> 1I0Z- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Small_Lactate_Sandbox_1&diff=1051255 2010-03-03T09:20:17Z

<p>Jasper Small: </p> <hr /> <div><br /> [[Image:1i10.png|left|200px]]<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> Lactate Dehydrogenase (LDH) is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver.<br /> <br /> ==Function==<br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> LDH preforms an important metabolic function in the body. The enzyme catalyzes both the conversion of pyruvate to lactose as well as the conversion of lactose to pyruvate. The conversion of pyruvate to lactose occurs in the muscles of the body when oxygen is absent. The lactate acid is then moved back to the liver where LDH catalyzes the Cori cycle which converts the lactose back into pyruvate. The reaction is also important as it is coupled with the interconversion of NADH and NAD+.<br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NAD+ must bind to the enzyme first followed by lactate. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two teranary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NADH. The rate limiting step in this reaction is the rate of dissociation of NADH. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable(1).<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> Important Sites:<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/His_195/1'&gt;HIS 195&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_109/1'&gt;ARG 109&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Asp_168/1'&gt;ASP 168&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_171/1'&gt;ARG 171&lt;/scene&gt;<br /> <br /> ==Structure==<br /> <br /> LDH is comprized of 40% alpha helixes and 23% beta sheets.(2)<br /> <br /> SCOP<br /> 1I10- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> 1I0Z- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> <br /> ==Reference==<br /> <br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Small_Lactate_Sandbox_1&diff=1051254 2010-03-03T09:19:30Z

<p>Jasper Small: </p> <hr /> <div>{{Seed}}<br /> [[Image:1i10.png|left|200px]]<br /> <br /> &lt;!--<br /> The line below this paragraph, containing &quot;STRUCTURE_1i10&quot;, creates the &quot;Structure Box&quot; on the page.<br /> You may change the PDB parameter (which sets the PDB file loaded into the applet) <br /> or the SCENE parameter (which sets the initial scene displayed when the page is loaded),<br /> or leave the SCENE parameter empty for the default display.<br /> --&gt;<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> Lactate Dehydrogenase (LDH) is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver.<br /> <br /> ==Function==<br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH (1)]]<br /> LDH preforms an important metabolic function in the body. The enzyme catalyzes both the conversion of pyruvate to lactose as well as the conversion of lactose to pyruvate. The conversion of pyruvate to lactose occurs in the muscles of the body when oxygen is absent. The lactate acid is then moved back to the liver where LDH catalyzes the Cori cycle which converts the lactose back into pyruvate. The reaction is also important as it is coupled with the interconversion of NADH and NAD+.<br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NAD+ must bind to the enzyme first followed by lactate. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two teranary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NADH. The rate limiting step in this reaction is the rate of dissociation of NADH. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable(1).<br /> <br /> [[Image:2nd.png|left|thumb|355px|(1)]]<br /> Important Sites:<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/His_195/1'&gt;HIS 195&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_109/1'&gt;ARG 109&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Asp_168/1'&gt;ASP 168&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_171/1'&gt;ARG 171&lt;/scene&gt;<br /> <br /> ==Structure==<br /> <br /> LDH is comprized of 40% alpha helixes and 23% beta sheets.(2)<br /> <br /> SCOP<br /> 1I10- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> 1I0Z- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:11276087&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=File:2nd.png&diff=1051253 2010-03-03T09:17:30Z

<p>Jasper Small: </p> <hr /> <div></div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Small_Lactate_Sandbox_1&diff=1051252 2010-03-03T09:16:34Z

<p>Jasper Small: </p> <hr /> <div>{{Seed}}<br /> [[Image:1i10.png|left|200px]]<br /> <br /> &lt;!--<br /> The line below this paragraph, containing &quot;STRUCTURE_1i10&quot;, creates the &quot;Structure Box&quot; on the page.<br /> You may change the PDB parameter (which sets the PDB file loaded into the applet) <br /> or the SCENE parameter (which sets the initial scene displayed when the page is loaded),<br /> or leave the SCENE parameter empty for the default display.<br /> --&gt;<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> Lactate Dehydrogenase (LDH) is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver.<br /> <br /> ==Function==<br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH]]<br /> LDH preforms an important metabolic function in the body. The enzyme catalyzes both the conversion of pyruvate to lactose as well as the conversion of lactose to pyruvate. The conversion of pyruvate to lactose occurs in the muscles of the body when oxygen is absent. The lactate acid is then moved back to the liver where LDH catalyzes the Cori cycle which converts the lactose back into pyruvate. The reaction is also important as it is coupled with the interconversion of NADH and NAD+.<br /> <br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NAD+ must bind to the enzyme first followed by lactate. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two teranary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NADH. The rate limiting step in this reaction is the rate of dissociation of NADH. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable(1).<br /> <br /> [[Image:2nd.jpeg|left|thumb|355px|]]<br /> Important Sites:<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/His_195/1'&gt;HIS 195&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_109/1'&gt;ARG 109&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Asp_168/1'&gt;ASP 168&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_171/1'&gt;ARG 171&lt;/scene&gt;<br /> <br /> ==Structure==<br /> <br /> LDH is comprized of 40% alpha helixes and 23% beta sheets.(2)<br /> <br /> SCOP<br /> 1I10- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> 1I0Z- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:11276087&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Small_Lactate_Sandbox_1&diff=1051251 2010-03-03T09:14:59Z

<p>Jasper Small: </p> <hr /> <div>{{Seed}}<br /> [[Image:1i10.png|left|200px]]<br /> <br /> &lt;!--<br /> The line below this paragraph, containing &quot;STRUCTURE_1i10&quot;, creates the &quot;Structure Box&quot; on the page.<br /> You may change the PDB parameter (which sets the PDB file loaded into the applet) <br /> or the SCENE parameter (which sets the initial scene displayed when the page is loaded),<br /> or leave the SCENE parameter empty for the default display.<br /> --&gt;<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> Lactate Dehydrogenase (LDH) is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver.<br /> <br /> ==Function==<br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH]]<br /> <br /> LDH preforms an important metabolic function in the body. The enzyme catalyzes both the conversion of pyruvate to lactose as well as the conversion of lactose to pyruvate. The conversion of pyruvate to lactose occurs in the muscles of the body when oxygen is absent. The lactate acid is then moved back to the liver where LDH catalyzes the Cori cycle which converts the lactose back into pyruvate. The reaction is also important as it is coupled with the interconversion of NADH and NAD+.<br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NAD+ must bind to the enzyme first followed by lactate. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two teranary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NADH. The rate limiting step in this reaction is the rate of dissociation of NADH. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable(1).<br /> <br /> Important Sites:<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/His_195/1'&gt;HIS 195&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_109/1'&gt;ARG 109&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Asp_168/1'&gt;ASP 168&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_171/1'&gt;ARG 171&lt;/scene&gt;<br /> <br /> ==Structure==<br /> <br /> LDH is comprized of 40% alpha helixes and 23% beta sheets.(2)<br /> <br /> SCOP<br /> 1I10- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> 1I0Z- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:11276087&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> 1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm<br /> 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Small_Lactate_Sandbox_1&diff=1051250 2010-03-03T09:01:07Z

<p>Jasper Small: </p> <hr /> <div>{{Seed}}<br /> [[Image:1i10.png|left|200px]]<br /> <br /> &lt;!--<br /> The line below this paragraph, containing &quot;STRUCTURE_1i10&quot;, creates the &quot;Structure Box&quot; on the page.<br /> You may change the PDB parameter (which sets the PDB file loaded into the applet) <br /> or the SCENE parameter (which sets the initial scene displayed when the page is loaded),<br /> or leave the SCENE parameter empty for the default display.<br /> --&gt;<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> Lactate Dehydrogenase (LDH) is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver.<br /> <br /> ==Function==<br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH]]<br /> <br /> LDH preforms an important metabolic function in the body. The enzyme catalyzes both the conversion of pyruvate to lactose as well as the conversion of lactose to pyruvate. The conversion of pyruvate to lactose occurs in the muscles of the body when oxygen is absent. The lactate acid is then moved back to the liver where LDH catalyzes the Cori cycle which converts the lactose back into pyruvate. The reaction is also important as it is coupled with the interconversion of NADH and NAD+.<br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NAD+ must bind to the enzyme first followed by lactate. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two teranary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NADH. The rate limiting step in this reaction is the rate of dissociation of NADH. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable.<br /> <br /> Important Sites:<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/His_195/1'&gt;HIS 195&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_109/1'&gt;ARG 109&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Asp_168/1'&gt;ASP 168&lt;/scene&gt;<br /> *&lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_171/1'&gt;ARG 171&lt;/scene&gt;<br /> <br /> ==Structure==<br /> <br /> LDH is comprized of 40% alpha helixes and 23% beta sheets.<br /> <br /> SCOP<br /> 1I10- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> 1I0Z- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:11276087&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> Article text.&lt;ref name=&quot;test&quot;&gt;[http://www.example.org Link text], additional text.&lt;/ref&gt;</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Small_Lactate_Sandbox_1&diff=1051249 2010-03-03T08:52:35Z

<p>Jasper Small: </p> <hr /> <div>{{Seed}}<br /> [[Image:1i10.png|left|200px]]<br /> <br /> &lt;!--<br /> The line below this paragraph, containing &quot;STRUCTURE_1i10&quot;, creates the &quot;Structure Box&quot; on the page.<br /> You may change the PDB parameter (which sets the PDB file loaded into the applet) <br /> or the SCENE parameter (which sets the initial scene displayed when the page is loaded),<br /> or leave the SCENE parameter empty for the default display.<br /> --&gt;<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> Lactate Dehydrogenase (LDH) is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver.<br /> <br /> ==Function==<br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH]]<br /> <br /> LDH preforms an important metabolic function in the body. The enzyme catalyzes both the conversion of pyruvate to lactose as well as the conversion of lactose to pyruvate. The conversion of pyruvate to lactose occurs in the muscles of the body when oxygen is absent. The lactate acid is then moved back to the liver where LDH catalyzes the Cori cycle which converts the lactose back into pyruvate. The reaction is also important as it is coupled with the interconversion of NADH and NAD+.<br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NAD+ must bind to the enzyme first followed by lactate. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two teranary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NADH. The rate limiting step in this reaction is the rate of dissociation of NADH. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable.<br /> <br /> Important Sites:<br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/His_195/1'&gt;HIS 195&lt;/scene&gt;<br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_109/1'&gt;ARG 109&lt;/scene&gt;<br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Asp_168/1'&gt;ASP 168&lt;/scene&gt;<br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/Arg_171/1'&gt;ARG 171&lt;/scene&gt;<br /> <br /> ==Structure==<br /> <br /> LDH is comprized of 40% alpha helixes and 23% beta sheets.<br /> <br /> SCOP<br /> 1I10- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> 1I0Z- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:11276087&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Homo sapiens]]<br /> [[Category: L-lactate dehydrogenase]]<br /> [[Category: Brady, R L.]]<br /> [[Category: Eszes, C M.]]<br /> [[Category: Read, J A.]]<br /> [[Category: Sessions, R B.]]<br /> [[Category: Winter, V J.]]<br /> [[Category: Dehydrogenase]]<br /> [[Category: Rossman fold]]</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Small_Lactate_Sandbox_1&diff=1051248 2010-03-03T08:45:19Z

<p>Jasper Small: </p> <hr /> <div>{{Seed}}<br /> [[Image:1i10.png|left|200px]]<br /> <br /> &lt;!--<br /> The line below this paragraph, containing &quot;STRUCTURE_1i10&quot;, creates the &quot;Structure Box&quot; on the page.<br /> You may change the PDB parameter (which sets the PDB file loaded into the applet) <br /> or the SCENE parameter (which sets the initial scene displayed when the page is loaded),<br /> or leave the SCENE parameter empty for the default display.<br /> --&gt;<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> Lactate Dehydrogenase (LDH) is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver.<br /> <br /> ==Function==<br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH]]<br /> <br /> LDH preforms an important metabolic function in the body. The enzyme catalyzes both the conversion of pyruvate to lactose as well as the conversion of lactose to pyruvate. The conversion of pyruvate to lactose occurs in the muscles of the body when oxygen is absent. The lactate acid is then moved back to the liver where LDH catalyzes the Cori cycle which converts the lactose back into pyruvate. The reaction is also important as it is coupled with the interconversion of NADH and NAD+.<br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NAD+ must bind to the enzyme first followed by lactate. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two teranary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NADH. The rate limiting step in this reaction is the rate of dissociation of NADH. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable.<br /> <br /> Important Sites:<br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/His_195/1'&gt;HIS 195&lt;/scene&gt;<br /> ARG 109<br /> ASP 168<br /> ARG 171<br /> <br /> ==Structure==<br /> <br /> LDH is comprized of 40% alpha helixes and 23% beta sheets.<br /> <br /> SCOP<br /> 1I10- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> 1I0Z- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:11276087&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Homo sapiens]]<br /> [[Category: L-lactate dehydrogenase]]<br /> [[Category: Brady, R L.]]<br /> [[Category: Eszes, C M.]]<br /> [[Category: Read, J A.]]<br /> [[Category: Sessions, R B.]]<br /> [[Category: Winter, V J.]]<br /> [[Category: Dehydrogenase]]<br /> [[Category: Rossman fold]]</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Small_Lactate_Sandbox_1&diff=1051247 2010-03-03T04:19:00Z

<p>Jasper Small: </p> <hr /> <div>{{Seed}}<br /> [[Image:1i10.png|left|200px]]<br /> <br /> &lt;!--<br /> The line below this paragraph, containing &quot;STRUCTURE_1i10&quot;, creates the &quot;Structure Box&quot; on the page.<br /> You may change the PDB parameter (which sets the PDB file loaded into the applet) <br /> or the SCENE parameter (which sets the initial scene displayed when the page is loaded),<br /> or leave the SCENE parameter empty for the default display.<br /> --&gt;<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> Lactate Dehydrogenase (LDH) is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver.<br /> <br /> ==Function==<br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH]]<br /> <br /> LDH preforms an important metabolic function in the body. The enzyme catalyzes both the conversion of pyruvate to lactose as well as the conversion of lactose to pyruvate. The conversion of pyruvate to lactose occurs in the muscles of the body when oxygen is absent. The lactate acid is then moved back to the liver where LDH catalyzes the Cori cycle which converts the lactose back into pyruvate. The reaction is also important as it is coupled with the interconversion of NADH and NAD+.<br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NAD+ must bind to the enzyme first followed by lactate. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two teranary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NADH. The rate limiting step in this reaction is the rate of dissociation of NADH. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable.<br /> <br /> Active Sites:<br /> &lt;scene name='Jasper_Small_Lactate_Sandbox_1/His_195/1'&gt;HIS 195&lt;/scene&gt;<br /> <br /> <br /> ==Structure==<br /> <br /> LDH is comprized of 40% alpha helixes and 23% beta sheets.<br /> <br /> SCOP<br /> 1I10- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> 1I0Z- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:11276087&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Homo sapiens]]<br /> [[Category: L-lactate dehydrogenase]]<br /> [[Category: Brady, R L.]]<br /> [[Category: Eszes, C M.]]<br /> [[Category: Read, J A.]]<br /> [[Category: Sessions, R B.]]<br /> [[Category: Winter, V J.]]<br /> [[Category: Dehydrogenase]]<br /> [[Category: Rossman fold]]</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Small_Lactate_Sandbox_1&diff=1051242 2010-03-03T03:29:11Z

<p>Jasper Small: </p> <hr /> <div>{{Seed}}<br /> [[Image:1i10.png|left|200px]]<br /> <br /> &lt;!--<br /> The line below this paragraph, containing &quot;STRUCTURE_1i10&quot;, creates the &quot;Structure Box&quot; on the page.<br /> You may change the PDB parameter (which sets the PDB file loaded into the applet) <br /> or the SCENE parameter (which sets the initial scene displayed when the page is loaded),<br /> or leave the SCENE parameter empty for the default display.<br /> --&gt;<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> Lactate Dehydrogenase (LDH) is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver.<br /> <br /> ==Function==<br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH]]<br /> <br /> LDH preforms an important metabolic function in the body. The enzyme catalyzes both the conversion of pyruvate to lactose as well as the conversion of lactose to pyruvate. The conversion of pyruvate to lactose occurs in the muscles of the body when oxygen is absent. The lactate acid is then moved back to the liver where LDH catalyzes the Cori cycle which converts the lactose back into pyruvate. The reaction is also important as it is coupled with the interconversion of NADH and NAD+.<br /> <br /> ==Catalysis==<br /> Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NAD+ must bind to the enzyme first followed by lactate. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two teranary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NADH. The rate limiting step in this reaction is the rate of dissociation of NADH. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable.<br /> <br /> Active Sites:<br /> HIS 195<br /> <br /> <br /> ==Structure==<br /> <br /> LDH is comprized of 40% alpha helixes and 23% beta sheets.<br /> <br /> SCOP<br /> 1I10- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> 1I0Z- a/b Mainly parallel beta sheets (beta-alpha-beta units)<br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:11276087&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Homo sapiens]]<br /> [[Category: L-lactate dehydrogenase]]<br /> [[Category: Brady, R L.]]<br /> [[Category: Eszes, C M.]]<br /> [[Category: Read, J A.]]<br /> [[Category: Sessions, R B.]]<br /> [[Category: Winter, V J.]]<br /> [[Category: Dehydrogenase]]<br /> [[Category: Rossman fold]]</div>

Jasper Small https://proteopedia.org/index.php?title=Jasper_Small_Lactate_Sandbox_1&diff=1051241 2010-03-03T03:10:05Z

<p>Jasper Small: </p> <hr /> <div>{{Seed}}<br /> [[Image:1i10.png|left|200px]]<br /> <br /> &lt;!--<br /> The line below this paragraph, containing &quot;STRUCTURE_1i10&quot;, creates the &quot;Structure Box&quot; on the page.<br /> You may change the PDB parameter (which sets the PDB file loaded into the applet) <br /> or the SCENE parameter (which sets the initial scene displayed when the page is loaded),<br /> or leave the SCENE parameter empty for the default display.<br /> --&gt;<br /> {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} <br /> <br /> ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE===<br /> <br /> ==Lactate Dehydrogenase==<br /> <br /> Lactate Dehydrogenase (LDH) is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver.<br /> <br /> ==Function==<br /> [[Image:LDH_reaction.jpeg|left|thumb|355px|Catalytic function of LDH]]<br /> <br /> LDH preforms an important metabolic function in the body. The enzyme catalyzes both the conversion of pyruvate to lactose as well as the conversion of lactose to pyruvate. The conversion of pyruvate to lactose occurs in the muscles of the body when oxygen is absent. The lactate acid is then moved back to the liver where LDH catalyzes the Cori cycle which converts the lactose back into pyruvate. The reaction is also important as it is coupled with the interconversion of NADH and NAD+.<br /> <br /> ==Disease==<br /> Known disease associated with this structure: Exertional myoglobinuria due to deficiency of LDH-A OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=150000 150000]]<br /> <br /> ==About this Structure==<br /> 1I10 is a 8 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I10 OCA]. <br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:11276087&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Homo sapiens]]<br /> [[Category: L-lactate dehydrogenase]]<br /> [[Category: Brady, R L.]]<br /> [[Category: Eszes, C M.]]<br /> [[Category: Read, J A.]]<br /> [[Category: Sessions, R B.]]<br /> [[Category: Winter, V J.]]<br /> [[Category: Dehydrogenase]]<br /> [[Category: Rossman fold]]<br /> <br /> ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:19:04 2009''</div>

Jasper Small