Proteopedia - User contributions [en]

https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Keegan+Gelvoria Proteopedia - User contributions [en] 2026-10-08T21:40:41Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1065058 Pyruvate Kinase 2010-04-02T13:21:59Z

<p>Keegan Gelvoria: </p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=501|}}</ref>.<br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}<br /> <br /> <br /> ==Structure==<br /> This particular protein is found in Homo sapiens and has the abbreviation PK. Pyruvate kinase belongs to the all beta proteins class and has the PK beta-barrel domain-like fold. It belongs to the PK beta-barrel domain-like superfamily and pyruvate kinase beta-barrel domain family<ref>{{website| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>.<br /> <br /> Though pyruvate kinase is classified into all beta proteins, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of both alpha helices and beta sheets. In the quaternary structure of pyruvate kinase, it can be observed to have <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the <scene name='Keegan_Gelvoria_Sandbox_1/Ligands/1'>K+</scene> and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue)<ref>{{website| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>.<br /> <br /> ==Mechanism==<br /> [[image:one.gif|left|300px]]<br /> <ref>{{website1| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?|url=http://www.sportsci.org/jour/0102/rar.htm|}}</ref><br /> <scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=502|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=503|}}</ref>.<br /> <br /> <br /> <br /> ==Kinetics and Regulation==<br /> <br /> In the glycolytic cycle, there are three compounds that have a large negative ∆G which includes the reaction pyruvate kinase catalyzes. Due to these three steps regulating the overall activity of the cycle, they are generally irreversible in vivo. Through numerous studies, the activity of pyruvate kinase has been found to be regulated by these effectors <ref>{{article |author=Dann, Leighton G.; Britton, Hubert G.|title=Kinetics and Mechanism of Action of Muscle Pyruvate Kinase|volume=169|pages=39-54|}}</ref>.:<br /> <br /> a. Phosphoenolpyruvate, the substrate, can impact enzymatic activity by enhancing the reaction <br /> by allowing the process to operate faster with more substrate present.<br /> <br /> b. ATP and pyruvate have been found to be a negative allosteric inhibitor.<br /> <br /> c. Alanine has also been found to be a negative allosteric modulator.<br /> <br /> <br /> <br /> As indicated earlier, phosphoenolpyruvate can enhance the activity of the reaction by adding into the enzyme because it is the rate limiting step. The enzyme follows hyperbolic kinetics. Experiments found that no incorporation was found in the reaction, indicating a random, rapid dissociation of the products. This, then, assumes that the products inhibit the enzyme’s reaction by simply reversing the reaction. Both pyruvate and ATP have been shown to be non-competitive inhibitors of pyruvate kinase <ref>{{article |author=Dann, Leighton G.; Britton, Hubert G.|title=Kinetics and Mechanism of Action of Muscle Pyruvate Kinase|volume=169|pages=39-54|}}</ref>.<br /> <br /> ==References==<br /> <references/></div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1064345 Pyruvate Kinase 2010-03-31T11:06:36Z

<p>Keegan Gelvoria: /* Kinetics and Regulation */</p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=501|}}</ref>.<br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}<br /> <br /> ==Mechanism==<br /> [[image:one.gif|left|300px]]<br /> <ref>{{website1| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?|url=http://www.sportsci.org/jour/0102/rar.htm|}}</ref><br /> <scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=502|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=503|}}</ref>.<br /> <br /> <br /> <br /> <br /> ==Structure==<br /> This particular protein is found in Homo sapiens and has the abbreviation PK. Pyruvate kinase belongs to the all beta proteins class and has the PK beta-barrel domain-like fold. It belongs to the PK beta-barrel domain-like superfamily and pyruvate kinase beta-barrel domain family<ref>{{website| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>.<br /> <br /> Though pyruvate kinase is classified into all beta proteins, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of both alpha helices and beta sheets. In the quaternary structure of pyruvate kinase, it can be observed to have <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the <scene name='Keegan_Gelvoria_Sandbox_1/Ligands/1'>K+</scene> and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue)<ref>{{website| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>.<br /> <br /> ==Kinetics and Regulation==<br /> <br /> In the glycolytic cycle, there are three compounds that have a large negative ∆G which includes the reaction pyruvate kinase catalyzes. Due to these three steps regulating the overall activity of the cycle, they are generally irreversible in vivo. Through numerous studies, the activity of pyruvate kinase has been found to be regulated by these effectors <ref>{{article |author=Dann, Leighton G.; Britton, Hubert G.|title=Kinetics and Mechanism of Action of Muscle Pyruvate Kinase|volume=169|pages=39-54|}}</ref>.:<br /> <br /> a. Phosphoenolpyruvate, the substrate, can impact enzymatic activity by enhancing the reaction <br /> by allowing the process to operate faster with more substrate present.<br /> <br /> b. ATP and pyruvate have been found to be a negative allosteric inhibitor.<br /> <br /> c. Alanine has also been found to be a negative allosteric modulator.<br /> <br /> <br /> <br /> As indicated earlier, phosphoenolpyruvate can enhance the activity of the reaction by adding into the enzyme because it is the rate limiting step. The enzyme follows hyperbolic kinetics. Experiments found that no incorporation was found in the reaction, indicating a random, rapid dissociation of the products. This, then, assumes that the products inhibit the enzyme’s reaction by simply reversing the reaction. Both pyruvate and ATP have been shown to be non-competitive inhibitors of pyruvate kinase <ref>{{article |author=Dann, Leighton G.; Britton, Hubert G.|title=Kinetics and Mechanism of Action of Muscle Pyruvate Kinase|volume=169|pages=39-54|}}</ref>.<br /> <br /> ==References==<br /> <references/></div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1064341 Pyruvate Kinase 2010-03-31T11:01:28Z

<p>Keegan Gelvoria: /* Kinetics and Regulation */</p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=501|}}</ref>.<br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}<br /> <br /> ==Mechanism==<br /> [[image:one.gif|left|300px]]<br /> <ref>{{website1| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?|url=http://www.sportsci.org/jour/0102/rar.htm|}}</ref><br /> <scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=502|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=503|}}</ref>.<br /> <br /> <br /> <br /> <br /> ==Structure==<br /> This particular protein is found in Homo sapiens and has the abbreviation PK. Pyruvate kinase belongs to the all beta proteins class and has the PK beta-barrel domain-like fold. It belongs to the PK beta-barrel domain-like superfamily and pyruvate kinase beta-barrel domain family<ref>{{website| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>.<br /> <br /> Though pyruvate kinase is classified into all beta proteins, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of both alpha helices and beta sheets. In the quaternary structure of pyruvate kinase, it can be observed to have <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the <scene name='Keegan_Gelvoria_Sandbox_1/Ligands/1'>K+</scene> and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue)<ref>{{website| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>.<br /> <br /> ==Kinetics and Regulation==<br /> <br /> In the glycolytic cycle, there are three compounds that have a large negative ∆G which includes the reaction pyruvate kinase catalyzes. Due to these three steps regulating the overall activity of the cycle, they are generally irreversible in vivo. Through numerous studies, the activity of pyruvate kinase has been found to be regulated by these effectors <ref>{{article |author=Dann, Leighton G.; Britton, Hubert G.|title=Kinetics and Mechanism of Action of Muscle Pyruvate Kinase|volume=169|pages=39-54|}}</ref>.:<br /> <br /> a. Phosphoenolpyruvate, the substrate, can impact enzymatic activity by enhancing the reaction <br /> by allowing the process to operate faster with more substrate present.<br /> <br /> b. ATP and pyruvate has been found to be a negative allosteric inhibitor.<br /> <br /> c. Alanine has also been found to be a negative allosteric modulator.<br /> <br /> <br /> <br /> As indicated earlier, phosphoenolpyruvate can enhance the activity of the reaction by adding into the enzyme because it is the rate limiting step. The enzyme follows hyperbolic kinetics. Experiments found that no incorporation was found in the reaction, indicating a random, rapid dissociation of the products. This, then, assumes that the products inhibit the enzyme’s reaction by simply reversing the reaction. Both pyruvate and ATP have been shown to be non-competitive inhibitors of pyruvate kinase <ref>{{article |author=Dann, Leighton G.; Britton, Hubert G.|title=Kinetics and Mechanism of Action of Muscle Pyruvate Kinase|volume=169|pages=39-54|}}</ref>.<br /> <br /> ==References==<br /> <references/></div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1059152 Pyruvate Kinase 2010-03-23T18:59:40Z

<p>Keegan Gelvoria: </p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=501|}}</ref>.<br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}<br /> <br /> ==Mechanism==<br /> [[image:one.gif|left|300px]]<br /> <ref>{{website1| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?|url=http://www.sportsci.org/jour/0102/rar.htm|}}</ref><br /> <scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=502|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=503|}}</ref>.<br /> <br /> <br /> <br /> <br /> ==Structure==<br /> This particular protein is found in Homo sapiens and has the abbreviation PK. Pyruvate kinase belongs to the all beta proteins class and has the PK beta-barrel domain-like fold. It belongs to the PK beta-barrel domain-like superfamily and pyruvate kinase beta-barrel domain family<ref>{{website| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>.<br /> <br /> Though pyruvate kinase is classified into all beta proteins, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of both alpha helices and beta sheets. In the quaternary structure of pyruvate kinase, it can be observed to have <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the <scene name='Keegan_Gelvoria_Sandbox_1/Ligands/1'>K+</scene> and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue)<ref>{{website| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>.<br /> <br /> ==Kinetics and Regulation==<br /> <br /> In the glycolytic cycle, there are three compounds that have a large negative ∆G which includes the reaction pyruvate kinase catalyzes. Due to these three steps regulating the overall activity of the cycle, they are generally irreversible in vivo. Through numerous researches, the activity of pyruvate kinase has been found to be regulated by these effectors <ref>{{article |author=Dann, Leighton G.; Britton, Hubert G.|title=Kinetics and Mechanism of Action of Muscle Pyruvate Kinase|volume=169|pages=39-54|}}</ref>.:<br /> <br /> a. Phosphoenolpyruvate, the substrate, can impact enzymatic activity by enhancing the reaction <br /> by allowing the process to operate faster with more substrate present.<br /> <br /> b. ATP and pyruvate has been found to be a negative allosteric inhibitor.<br /> <br /> c. Alanine has also been found to be a negative allosteric modulator.<br /> <br /> <br /> <br /> As indicated earlier, phosphoenolpyruvate can enhance the activity of the reaction by adding into the enzyme because it is the rate limiting step. The enzyme follows hyperbolic kinetics. Experiments found that no incorporation was found in the reaction, indicating a random, rapid dissociation of the products. This, then, assumes that the products inhibit the enzyme’s reaction by simply reversing the reaction. Both pyruvate and ATP have been shown to be non-competitive inhibitors of pyruvate kinase <ref>{{article |author=Dann, Leighton G.; Britton, Hubert G.|title=Kinetics and Mechanism of Action of Muscle Pyruvate Kinase|volume=169|pages=39-54|}}</ref>.<br /> <br /> ==References==<br /> <references/></div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1059150 Pyruvate Kinase 2010-03-23T18:39:15Z

<p>Keegan Gelvoria: /* Structure */</p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=501|}}</ref>.<br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}<br /> <br /> ==Mechanism==<br /> [[image:one.gif|left|300px]]<br /> <ref>{{website1| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?|url=http://www.sportsci.org/jour/0102/rar.htm|}}</ref><br /> <scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=502|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=503|}}</ref>.<br /> <br /> <br /> <br /> <br /> ==Structure==<br /> This particular protein is found in Homo sapiens and has the abbreviation PK. Pyruvate kinase belongs to the all beta proteins class and has the PK beta-barrel domain-like fold. It belongs to the PK beta-barrel domain-like superfamily and pyruvate kinase beta-barrel domain family<ref>{{website| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>.<br /> <br /> Though pyruvate kinase is classified into all beta proteins, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of both alpha helices and beta sheets. In the quaternary structure of pyruvate kinase, it can be observed to have <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the K+ and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue)<ref>{{website| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>.<br /> <br /> ==Kinetics and Regulation==<br /> <br /> In the glycolytic cycle, there are three compounds that have a large negative ∆G which includes the reaction pyruvate kinase catalyzes. Due to these three steps regulating the overall activity of the cycle, they are generally irreversible in vivo. Through numerous researches, the activity of pyruvate kinase has been found to be regulated by these effectors <ref>{{article |author=Dann, Leighton G.; Britton, Hubert G.|title=Kinetics and Mechanism of Action of Muscle Pyruvate Kinase|volume=169|pages=39-54|}}</ref>.:<br /> <br /> a. Phosphoenolpyruvate, the substrate, can impact enzymatic activity by enhancing the reaction <br /> by allowing the process to operate faster with more substrate present.<br /> <br /> b. ATP and pyruvate has been found to be a negative allosteric inhibitor.<br /> <br /> c. Alanine has also been found to be a negative allosteric modulator.<br /> <br /> <br /> <br /> As indicated earlier, phosphoenolpyruvate can enhance the activity of the reaction by adding into the enzyme because it is the rate limiting step. The enzyme follows hyperbolic kinetics. Experiments found that no incorporation was found in the reaction, indicating a random, rapid dissociation of the products. This, then, assumes that the products inhibit the enzyme’s reaction by simply reversing the reaction. Both pyruvate and ATP have been shown to be non-competitive inhibitors of pyruvate kinase <ref>{{article |author=Dann, Leighton G.; Britton, Hubert G.|title=Kinetics and Mechanism of Action of Muscle Pyruvate Kinase|volume=169|pages=39-54|}}</ref>.<br /> <br /> ==References==<br /> <references/></div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1059149 Pyruvate Kinase 2010-03-23T18:35:13Z

<p>Keegan Gelvoria: </p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=501|}}</ref>.<br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}<br /> <br /> ==Mechanism==<br /> [[image:one.gif|left|300px]]<br /> <ref>{{website1| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?|url=http://www.sportsci.org/jour/0102/rar.htm|}}</ref><br /> <scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=502|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=503|}}</ref>.<br /> <br /> <br /> <br /> <br /> ==Structure==<br /> Class: All Beta Proteins<br /> <br /> Fold: PK beta-barrel domain-like<br /> <br /> Superfamily: PK beta-barrel domain-like<br /> <br /> Family: Pyruvate kinase beta-barrel domain<br /> <br /> Protein: Pyruvate Kinase (PK)<br /> <br /> Species: Human (Homo sapiens)<br /> <br /> Though pyruvate kinase is classified into all beta proteins, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of both alpha helices and beta sheets. In the quaternary structure of pyruvate kinase, it can be observed to have <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the K+ and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue)<ref>{{website| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>.<br /> <br /> ==Kinetics and Regulation==<br /> <br /> In the glycolytic cycle, there are three compounds that have a large negative ∆G which includes the reaction pyruvate kinase catalyzes. Due to these three steps regulating the overall activity of the cycle, they are generally irreversible in vivo. Through numerous researches, the activity of pyruvate kinase has been found to be regulated by these effectors <ref>{{article |author=Dann, Leighton G.; Britton, Hubert G.|title=Kinetics and Mechanism of Action of Muscle Pyruvate Kinase|volume=169|pages=39-54|}}</ref>.:<br /> <br /> a. Phosphoenolpyruvate, the substrate, can impact enzymatic activity by enhancing the reaction <br /> by allowing the process to operate faster with more substrate present.<br /> <br /> b. ATP and pyruvate has been found to be a negative allosteric inhibitor.<br /> <br /> c. Alanine has also been found to be a negative allosteric modulator.<br /> <br /> <br /> <br /> As indicated earlier, phosphoenolpyruvate can enhance the activity of the reaction by adding into the enzyme because it is the rate limiting step. The enzyme follows hyperbolic kinetics. Experiments found that no incorporation was found in the reaction, indicating a random, rapid dissociation of the products. This, then, assumes that the products inhibit the enzyme’s reaction by simply reversing the reaction. Both pyruvate and ATP have been shown to be non-competitive inhibitors of pyruvate kinase <ref>{{article |author=Dann, Leighton G.; Britton, Hubert G.|title=Kinetics and Mechanism of Action of Muscle Pyruvate Kinase|volume=169|pages=39-54|}}</ref>.<br /> <br /> ==References==<br /> <references/></div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Template:Article&diff=1059148 Template:Article 2010-03-23T18:34:43Z

<p>Keegan Gelvoria: New page: Dann, Leighton G. and Britton, Hubert G. Kinetics and Mechanism of Action of Muscle Pyruvate Kinase. Journal of Biochemistry. 1978 169:39-54.</p> <hr /> <div>Dann, Leighton G. and Britton, Hubert G. Kinetics and Mechanism of Action of Muscle Pyruvate Kinase. Journal of Biochemistry. 1978 169:39-54.</div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1059147 Pyruvate Kinase 2010-03-23T18:31:44Z

<p>Keegan Gelvoria: </p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=501|}}</ref>.<br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}<br /> <br /> ==Mechanism==<br /> [[image:one.gif|left|300px]]<br /> <ref>{{website1| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?|url=http://www.sportsci.org/jour/0102/rar.htm|}}</ref><br /> <scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=502|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=503|}}</ref>.<br /> <br /> <br /> <br /> <br /> ==Structure==<br /> Class: All Beta Proteins<br /> <br /> Fold: PK beta-barrel domain-like<br /> <br /> Superfamily: PK beta-barrel domain-like<br /> <br /> Family: Pyruvate kinase beta-barrel domain<br /> <br /> Protein: Pyruvate Kinase (PK)<br /> <br /> Species: Human (Homo sapiens)<br /> <br /> Though pyruvate kinase is classified into all beta proteins, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of both alpha helices and beta sheets. In the quaternary structure of pyruvate kinase, it can be observed to have <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the K+ and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue)<ref>{{website| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>.<br /> <br /> ==Kinetics and Regulation==<br /> <br /> In the glycolytic cycle, there are three compounds that have a large negative ∆G which includes the reaction pyruvate kinase catalyzes. Due to these three steps regulating the overall activity of the cycle, they are generally irreversible in vivo. Through numerous researches, the activity of pyruvate kinase has been found to be regulated by these effectors:<br /> <br /> a. Phosphoenolpyruvate, the substrate, can impact enzymatic activity by enhancing the reaction <br /> by allowing the process to operate faster with more substrate present.<br /> <br /> b. ATP and pyruvate has been found to be a negative allosteric inhibitor.<br /> <br /> c. Alanine has also been found to be a negative allosteric modulator.<br /> <br /> <br /> <br /> As indicated earlier, phosphoenolpyruvate can enhance the activity of the reaction by adding into the enzyme because it is the rate limiting step. The enzyme follows hyperbolic kinetics. Experiments found that no incorporation was found in the reaction, indicating a random, rapid dissociation of the products. This, then, assumes that the products inhibit the enzyme’s reaction by simply reversing the reaction. Both pyruvate and ATP have been shown to be non-competitive inhibitors of pyruvate kinase <ref>{{article |author=Dann, Leighton G.; Britton, Hubert G.|title=Kinetics and Mechanism of Action of Muscle Pyruvate Kinase|volume=169|pages=39-54|}}</ref>.<br /> <br /> ==References==<br /> <references/></div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Template:Book&diff=1059146 Template:Book 2010-03-23T18:26:20Z

<p>Keegan Gelvoria: </p> <hr /> <div>Voet, Donald, Judith G. Voet, and Charlotte W. Pratt. Fundamentals of Biochemistry: Life at the Molecular Level. 3rd ed. Hoboken, NJ: John Wiley & Sons, Inc., 2008, 501-503.</div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1059145 Pyruvate Kinase 2010-03-23T18:21:56Z

<p>Keegan Gelvoria: /* Structure */</p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=501|}}</ref>.<br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}<br /> <br /> ==Mechanism==<br /> [[image:one.gif|left|300px]]<br /> <ref>{{website1| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?|url=http://www.sportsci.org/jour/0102/rar.htm|}}</ref><br /> <scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=502|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=503|}}</ref>.<br /> <br /> <br /> <br /> <br /> ==Structure==<br /> Class: All Beta Proteins<br /> <br /> Fold: PK beta-barrel domain-like<br /> <br /> Superfamily: PK beta-barrel domain-like<br /> <br /> Family: Pyruvate kinase beta-barrel domain<br /> <br /> Protein: Pyruvate Kinase (PK)<br /> <br /> Species: Human (Homo sapiens)<br /> <br /> Though pyruvate kinase is classified into all beta proteins, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of both alpha helices and beta sheets. In the quaternary structure of pyruvate kinase, it can be observed to have <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the K+ and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue)<ref>{{website| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>.<br /> <br /> ==Kinetics and Regulation==<br /> <br /> In the glycolytic cycle, there are three compounds that have a large negative ∆G which includes the reaction pyruvate kinase catalyzes. Due to these three steps regulating the overall activity of the cycle, they are generally irreversible in vivo. Through numerous researches, the activity of pyruvate kinase has been found to be regulated by these effectors:<br /> <br /> a. Phosphoenolpyruvate, the substrate, can impact enzymatic activity by enhancing the reaction <br /> by allowing the process to operate faster with more substrate present.<br /> <br /> b. ATP and pyruvate has been found to be a negative allosteric inhibitor.<br /> <br /> c. Alanine has also been found to be a negative allosteric modulator.<br /> <br /> <br /> <br /> As indicated earlier, phosphoenolpyruvate can enhance the activity of the reaction by adding into the enzyme because it is the rate limiting step. The enzyme follows hyperbolic kinetics. Experiments found that no incorporation was found in the reaction, indicating a random, rapid dissociation of the products. This, then, assumes that the products inhibit the enzyme’s reaction by simply reversing the reaction. Both pyruvate and ATP have been shown to be non-competitive inhibitors of pyruvate kinase.<br /> <br /> ==References==<br /> <references/></div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1059144 Pyruvate Kinase 2010-03-23T18:18:55Z

<p>Keegan Gelvoria: /* Kinetics and Regulation */</p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=501|}}</ref>.<br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}<br /> <br /> ==Mechanism==<br /> [[image:one.gif|left|300px]]<br /> <ref>{{website1| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?|url=http://www.sportsci.org/jour/0102/rar.htm|}}</ref><br /> <scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=502|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=503|}}</ref>.<br /> <br /> <br /> <br /> <br /> ==Structure==<br /> Class: All Beta Proteins<br /> <br /> Fold: PK beta-barrel domain-like<br /> <br /> Superfamily: PK beta-barrel domain-like<br /> <br /> Family: Pyruvate kinase beta-barrel domain<br /> <br /> Protein: Pyruvate Kinase (PK)<br /> <br /> Species: Human (Homo sapiens)<br /> <br /> As can be seen, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the K+ and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue)<ref>{{website| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>.<br /> <br /> ==Kinetics and Regulation==<br /> <br /> In the glycolytic cycle, there are three compounds that have a large negative ∆G which includes the reaction pyruvate kinase catalyzes. Due to these three steps regulating the overall activity of the cycle, they are generally irreversible in vivo. Through numerous researches, the activity of pyruvate kinase has been found to be regulated by these effectors:<br /> <br /> a. Phosphoenolpyruvate, the substrate, can impact enzymatic activity by enhancing the reaction <br /> by allowing the process to operate faster with more substrate present.<br /> <br /> b. ATP and pyruvate has been found to be a negative allosteric inhibitor.<br /> <br /> c. Alanine has also been found to be a negative allosteric modulator.<br /> <br /> <br /> <br /> As indicated earlier, phosphoenolpyruvate can enhance the activity of the reaction by adding into the enzyme because it is the rate limiting step. The enzyme follows hyperbolic kinetics. Experiments found that no incorporation was found in the reaction, indicating a random, rapid dissociation of the products. This, then, assumes that the products inhibit the enzyme’s reaction by simply reversing the reaction. Both pyruvate and ATP have been shown to be non-competitive inhibitors of pyruvate kinase.<br /> <br /> ==References==<br /> <references/></div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1059143 Pyruvate Kinase 2010-03-23T18:09:13Z

<p>Keegan Gelvoria: </p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=501|}}</ref>.<br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}<br /> <br /> ==Mechanism==<br /> [[image:one.gif|left|300px]]<br /> <ref>{{website1| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?|url=http://www.sportsci.org/jour/0102/rar.htm|}}</ref><br /> <scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=502|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=503|}}</ref>.<br /> <br /> <br /> <br /> <br /> ==Structure==<br /> Class: All Beta Proteins<br /> <br /> Fold: PK beta-barrel domain-like<br /> <br /> Superfamily: PK beta-barrel domain-like<br /> <br /> Family: Pyruvate kinase beta-barrel domain<br /> <br /> Protein: Pyruvate Kinase (PK)<br /> <br /> Species: Human (Homo sapiens)<br /> <br /> As can be seen, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the K+ and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue)<ref>{{website| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>.<br /> <br /> ==Kinetics and Regulation==<br /> <br /> In the glycolytic cycle, there are three compounds that have a large negative ∆G which includes the reaction pyruvate kinase catalyzes. Due to these three steps regulating the overall activity of the cycle, they are generally irreversible in vivo. Through numerous researches, the activity of pyruvate kinase has been found to be regulated by these effectors:<br /> <br /> a. Phosphoenolpyruvate, the substrate, can impact enzymatic activity by enhancing the reaction <br /> by allowing the process to operate faster with more substrate present.<br /> <br /> b. ATP and pyruvate has been found to be a negative allosteric inhibitor.<br /> <br /> c. Alanine has also been found to be a negative allosteric modulator.<br /> [[image:kinetics.gif|center|400px]]<br /> <br /> <br /> As indicated earlier, phosphoenolpyruvate can enhance the activity of the reaction by adding into the enzyme because it is the rate limiting step. The enzyme follows hyperbolic kinetics. Experiments found that no incorporation was found in the reaction, indicating a random, rapid dissociation of the products. This, then, assumes that the products inhibit the enzyme’s reaction by simply reversing the reaction. Both pyruvate and ATP have been shown to be non-competitive inhibitors of pyruvate kinase.<br /> [[image:inhibition.gif|center|400px]]<br /> <br /> ==References==<br /> <references/></div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1059142 Pyruvate Kinase 2010-03-23T18:05:57Z

<p>Keegan Gelvoria: /* Kinetics and Regulation */</p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=501|}}</ref>.<br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}<br /> <br /> ==Mechanism==<br /> [[image:one.gif|left|300px]]<br /> <ref>{{website1| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?|url=http://www.sportsci.org/jour/0102/rar.htm|}}</ref><br /> <scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=502|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=503|}}</ref>.<br /> <br /> <br /> <br /> <br /> ==Structure==<br /> Class: All Beta Proteins<br /> <br /> Fold: PK beta-barrel domain-like<br /> <br /> Superfamily: PK beta-barrel domain-like<br /> <br /> Family: Pyruvate kinase beta-barrel domain<br /> <br /> Protein: Pyruvate Kinase (PK)<br /> <br /> Species: Human (Homo sapiens)<br /> <br /> As can be seen, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the K+ and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue)<ref>{{website| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>.<br /> <br /> ==Kinetics and Regulation==<br /> <br /> In the glycolytic cycle, there are three compounds that have a large negative ∆G which includes the reaction pyruvate kinase catalyzes. Due to these three steps regulating the overall activity of the cycle, they are generally irreversible in vivo. Through numerous researches, the activity of pyruvate kinase has been found to be regulated by these effectors:<br /> <br /> a. Phosphoenolpyruvate, the substrate, can impact enzymatic activity by enhancing the reaction <br /> by allowing the process to operate faster with more substrate present.<br /> <br /> b. ATP and pyruvate has been found to be a negative allosteric inhibitor.<br /> <br /> c. Alanine has also been found to be a negative allosteric modulator.<br /> <br /> <br /> As indicated earlier, phosphoenolpyruvate can enhance the activity of the reaction by adding into the enzyme because it is the rate limiting step. The enzyme follows hyperbolic kinetics. Experiments found that no incorporation was found in the reaction, indicating a random, rapid dissociation of the products. This, then, assumes that the products inhibit the enzyme’s reaction by simply reversing the reaction. Both pyruvate and ATP have been shown to be non-competitive inhibitors of pyruvate kinase.<br /> <br /> ==References==<br /> <references/></div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1059141 Pyruvate Kinase 2010-03-23T18:04:36Z

<p>Keegan Gelvoria: </p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=501|}}</ref>.<br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}<br /> <br /> ==Mechanism==<br /> [[image:one.gif|left|300px]]<br /> <ref>{{website1| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?|url=http://www.sportsci.org/jour/0102/rar.htm|}}</ref><br /> <scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=502|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=503|}}</ref>.<br /> <br /> <br /> <br /> <br /> ==Structure==<br /> Class: All Beta Proteins<br /> <br /> Fold: PK beta-barrel domain-like<br /> <br /> Superfamily: PK beta-barrel domain-like<br /> <br /> Family: Pyruvate kinase beta-barrel domain<br /> <br /> Protein: Pyruvate Kinase (PK)<br /> <br /> Species: Human (Homo sapiens)<br /> <br /> As can be seen, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the K+ and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue)<ref>{{website| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>.<br /> <br /> ==Kinetics and Regulation==<br /> <br /> In the glycolytic cycle, there are three compounds that have a large negative ∆G which includes the reaction pyruvate kinase catalyzes. Due to these three steps regulating the overall activity of the cycle, they are generally irreversible in vivo. Through numerous researches, the activity of pyruvate kinase has been found to be regulated by these effectors:<br /> a. Phosphoenolpyruvate, the substrate, can impact enzymatic activity by enhancing the reaction by allowing the process to operate faster with more substrate present.<br /> b. ATP and pyruvate has been found to be a negative allosteric inhibitor.<br /> c. Alanine has also been found to be a negative allosteric modulator.<br /> <br /> As indicated earlier, phosphoenolpyruvate can enhance the activity of the reaction by adding into the enzyme because it is the rate limiting step. The enzyme follows hyperbolic kinetics. Experiments found that no incorporation was found in the reaction, indicating a random, rapid dissociation of the products. This, then, assumes that the products inhibit the enzyme’s reaction by simply reversing the reaction. Both pyruvate and ATP have been shown to be non-competitive inhibitors of pyruvate kinase.<br /> <br /> ==References==<br /> <references/></div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1051187 Pyruvate Kinase 2010-03-01T22:15:35Z

<p>Keegan Gelvoria: </p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=501|}}</ref>.<br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}<br /> <br /> ==Mechanism==<br /> [[image:one.gif|left|300px]]<br /> <ref>{{website1| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?|url=http://www.sportsci.org/jour/0102/rar.htm|}}</ref><br /> <scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=502|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=503|}}</ref>.<br /> <br /> <br /> <br /> <br /> ==Structure==<br /> Class: All Beta Proteins<br /> <br /> Fold: PK beta-barrel domain-like<br /> <br /> Superfamily: PK beta-barrel domain-like<br /> <br /> Family: Pyruvate kinase beta-barrel domain<br /> <br /> Protein: Pyruvate Kinase (PK)<br /> <br /> Species: Human (Homo sapiens)<br /> <br /> As can be seen, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the K+ and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue)<ref>{{website| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>.<br /> <br /> <br /> ==References==<br /> <references/></div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Template:Website1&diff=1051186 Template:Website1 2010-03-01T22:14:24Z

<p>Keegan Gelvoria: New page: Robergs, Robert. "Exercise-Induced Metabolic Acidosis: Where do the Protons come from?". 2009. 2/27 2010. <http://www.sportsci.org/jour/0102/rar.htm>.</p> <hr /> <div>Robergs, Robert. "Exercise-Induced Metabolic Acidosis: Where do the Protons come from?". 2009. 2/27 2010. <http://www.sportsci.org/jour/0102/rar.htm>.</div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Template:Website&diff=1051185 Template:Website 2010-03-01T22:12:32Z

<p>Keegan Gelvoria: New page: authors, The scop. "Structural Classification of Proteins". 2009. 2/26 2010. <http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html>.</p> <hr /> <div>authors, The scop. "Structural Classification of Proteins". 2009. 2/26 2010. <http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html>.</div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Template:Book&diff=1051184 Template:Book 2010-03-01T22:10:58Z

<p>Keegan Gelvoria: New page: Voet, Donald, Judith G. Voet, and Charlotte W. Pratt. Fundamentals of Biochemistry: Life at the Molecular Level. 3rd ed. Hoboken, NJ: John Wiley & Sons, Inc., 2008.</p> <hr /> <div>Voet, Donald, Judith G. Voet, and Charlotte W. Pratt. Fundamentals of Biochemistry: Life at the Molecular Level. 3rd ed. Hoboken, NJ: John Wiley & Sons, Inc., 2008.</div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1051183 Pyruvate Kinase 2010-03-01T22:04:28Z

<p>Keegan Gelvoria: </p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=501|}}</ref>.<br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}<br /> <br /> ==Mechanism==<br /> [[image:one.gif|left|300px]]<br /> <ref>{{website| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?|url=http://www.sportsci.org/jour/0102/rar.htm|}}</ref><br /> <scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=502|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=503|}}</ref>.<br /> <br /> <br /> <br /> <br /> ==Structure==<br /> Class: All Beta Proteins<br /> <br /> Fold: PK beta-barrel domain-like<br /> <br /> Superfamily: PK beta-barrel domain-like<br /> <br /> Family: Pyruvate kinase beta-barrel domain<br /> <br /> Protein: Pyruvate Kinase (PK)<br /> <br /> Species: Human (Homo sapiens)<br /> <br /> As can be seen, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the K+ and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue)<ref>{{website1| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>.<br /> <br /> <br /> ==References==<br /> <references/></div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1051182 Pyruvate Kinase 2010-03-01T22:01:42Z

<p>Keegan Gelvoria: </p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP <ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=501|}}</ref>.<br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}<br /> <br /> ==Mechanism==<br /> [[image:one.gif|left|300px]]<br /> <ref>{{web site| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?|url=http://www.sportsci.org/jour/0102/rar.htm|}}</ref><br /> <scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=502|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=503|}}</ref>.<br /> <br /> <br /> <br /> <br /> ==Structure==<br /> Class: All Beta Proteins<br /> <br /> Fold: PK beta-barrel domain-like<br /> <br /> Superfamily: PK beta-barrel domain-like<br /> <br /> Family: Pyruvate kinase beta-barrel domain<br /> <br /> Protein: Pyruvate Kinase (PK)<br /> <br /> Species: Human (Homo sapiens)<br /> <br /> As can be seen, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the K+ and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue)<ref>{{web site| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>.<br /> <br /> <br /> ==References==<br /> <references/></div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1051180 Pyruvate Kinase 2010-03-01T21:59:30Z

<p>Keegan Gelvoria: </p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP <ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=501|}}</ref>.<br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}<br /> <br /> ==Mechanism==<br /> [[image:one.gif|left|300px]]<ref>{{web site| title=Exercise-Induced Metabolic Acidosis: <br /> Where do the Protons come from?|url=http://www.sportsci.org/jour/0102/rar.htm|}}</ref><br /> <scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=502|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=503|}}</ref>.<br /> <br /> <br /> <br /> <br /> ==Structure==<br /> Class: All Beta Proteins<br /> <br /> Fold: PK beta-barrel domain-like<br /> <br /> Superfamily: PK beta-barrel domain-like<br /> <br /> Family: Pyruvate kinase beta-barrel domain<br /> <br /> Protein: Pyruvate Kinase (PK)<br /> <br /> Species: Human (Homo sapiens)<br /> <br /> As can be seen, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the K+ and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue)<ref>{{web site| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>.<br /> <br /> <br /> ==References==<br /> <references/></div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1051178 Pyruvate Kinase 2010-03-01T21:57:11Z

<p>Keegan Gelvoria: </p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP <ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=501|}}</ref>.<br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}<br /> <br /> ==Mechanism==<br /> [[image:one.gif|left|300px]]<ref>{{web site| title=Exercise-Induced Metabolic Acidosis: <br /> Where do the Protons come from?|url=http://www.sportsci.org/jour/0102/rar.htm|}}</ref><br /> <scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=502|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=503|}}</ref>.<br /> <br /> <br /> <br /> <br /> ==Structure==<br /> Class: All Beta Proteins<br /> <br /> Fold: PK beta-barrel domain-like<br /> <br /> Superfamily: PK beta-barrel domain-like<br /> <br /> Family: Pyruvate kinase beta-barrel domain<br /> <br /> Protein: Pyruvate Kinase (PK)<br /> <br /> Species: Human (Homo sapiens)<br /> <br /> As can be seen, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the K+ and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue)<ref>{{web site| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>.<br /> <br /> ==References==<br /> <references/></div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1051176 Pyruvate Kinase 2010-03-01T21:53:51Z

<p>Keegan Gelvoria: </p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP <ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=501|}}</ref>.<br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}<br /> <br /> ==Mechanism==<br /> [[image:one.gif|left|300px]]<ref>{{web site| title=Exercise-Induced Metabolic Acidosis: <br /> Where do the Protons come from?|url=http://www.sportsci.org/jour/0102/rar.htm|}}</ref><br /> <scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=502|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=503|}}</ref>.<br /> <br /> <br /> <br /> <br /> ==Structure==<br /> Class: All Beta Proteins<br /> <br /> Fold: PK beta-barrel domain-like<br /> <br /> Superfamily: PK beta-barrel domain-like<br /> <br /> Family: Pyruvate kinase beta-barrel domain<br /> <br /> Protein: Pyruvate Kinase (PK)<br /> <br /> Species: Human (Homo sapiens)<br /> <br /> As can be seen, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the K+ and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue)<ref>{{web site| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>.<br /> <br /> ==References==<br /> <br /> <references/></div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1051175 Pyruvate Kinase 2010-03-01T21:51:48Z

<p>Keegan Gelvoria: </p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP <ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=501|}}</ref>.<br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}<br /> <br /> ==Mechanism==<br /> [[image:one.gif|left|300px]]<ref>{{web site| title=http://www.sportsci.org/jour/0102/rar.htm|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref><br /> <scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=502|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=503|}}</ref>.<br /> <br /> <br /> <br /> <br /> ==Structure==<br /> Class: All Beta Proteins<br /> <br /> Fold: PK beta-barrel domain-like<br /> <br /> Superfamily: PK beta-barrel domain-like<br /> <br /> Family: Pyruvate kinase beta-barrel domain<br /> <br /> Protein: Pyruvate Kinase (PK)<br /> <br /> Species: Human (Homo sapiens)<br /> <br /> As can be seen, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the K+ and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue)<ref>{{web site| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>.<br /> <br /> ==References==<br /> <br /> <references/></div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1051174 Pyruvate Kinase 2010-03-01T21:50:25Z

<p>Keegan Gelvoria: </p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP <ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=501|}}</ref>.<br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}<br /> <br /> ==Mechanism==<br /> [[image:one.gif|left|300px]]<ref>{{web site| title=http://www.sportsci.org/jour/0102/rar.htm|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref><br /> <scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=502|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=503|}}</ref>.<br /> <br /> <br /> <br /> <br /> ==Structure==<br /> Class: All Beta Proteins<br /> <br /> Fold: PK beta-barrel domain-like<br /> <br /> Superfamily: PK beta-barrel domain-like<br /> <br /> Family: Pyruvate kinase beta-barrel domain<br /> <br /> Protein: Pyruvate Kinase (PK)<br /> <br /> Species: Human (Homo sapiens)<br /> <br /> As can be seen, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the K+ and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue)<ref>{{web site| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>.</div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1051168 Pyruvate Kinase 2010-03-01T21:44:01Z

<p>Keegan Gelvoria: </p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP.<br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}<br /> <br /> ==Mechanism==<br /> [[image:one.gif|left|300px]]<br /> <scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate.<br /> <br /> <br /> <br /> <br /> ==Structure==<br /> Class: All Beta Proteins<br /> <br /> Fold: PK beta-barrel domain-like<br /> <br /> Superfamily: PK beta-barrel domain-like<br /> <br /> Family: Pyruvate kinase beta-barrel domain<br /> <br /> Protein: Pyruvate Kinase (PK)<br /> <br /> Species: Human (Homo sapiens)<br /> <br /> As can be seen, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the K+ and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue).</div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1051166 Pyruvate Kinase 2010-03-01T21:43:13Z

<p>Keegan Gelvoria: </p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP.<br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}<br /> <br /> ==Mechanism==<br /> [[image:one.gif|left|300px]]<br /> <scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate.<br /> [[image:one.gif|left|300px]]<br /> <br /> <br /> <br /> ==Structure==<br /> Class: All Beta Proteins<br /> <br /> Fold: PK beta-barrel domain-like<br /> <br /> Superfamily: PK beta-barrel domain-like<br /> <br /> Family: Pyruvate kinase beta-barrel domain<br /> <br /> Protein: Pyruvate Kinase (PK)<br /> <br /> Species: Human (Homo sapiens)<br /> <br /> As can be seen, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the K+ and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue).</div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1051165 Pyruvate Kinase 2010-03-01T21:41:45Z

<p>Keegan Gelvoria: </p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP.<br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}<br /> <br /> ==Mechanism==<br /> <scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate.<br /> [[image:one.gif|left|300px]]<br /> <br /> <br /> <br /> ==Structure==<br /> Class: All Beta Proteins<br /> <br /> Fold: PK beta-barrel domain-like<br /> <br /> Superfamily: PK beta-barrel domain-like<br /> <br /> Family: Pyruvate kinase beta-barrel domain<br /> <br /> Protein: Pyruvate Kinase (PK)<br /> <br /> Species: Human (Homo sapiens)<br /> <br /> As can be seen, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the K+ and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue). <br /> <br /> <br /> <br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}</div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1051158 Pyruvate Kinase 2010-03-01T21:39:58Z

<p>Keegan Gelvoria: </p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP.<br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}<br /> <br /> ==Mechanism==<br /> <scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate.<br /> [[image:one.gif|left|300px]]<br /> ==Structure==<br /> Class: All Beta Proteins<br /> <br /> Fold: PK beta-barrel domain-like<br /> <br /> Superfamily: PK beta-barrel domain-like<br /> <br /> Family: Pyruvate kinase beta-barrel domain<br /> <br /> Protein: Pyruvate Kinase (PK)<br /> <br /> Species: Human (Homo sapiens)<br /> <br /> As can be seen, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the K+ and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue). <br /> <br /> <br /> <br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}</div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1051152 Pyruvate Kinase 2010-03-01T21:34:12Z

<p>Keegan Gelvoria: </p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP.<br /> <br /> ==Mechanism==<br /> <scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate.<br /> <br /> ==Structure==<br /> Class: All Beta Proteins<br /> <br /> Fold: PK beta-barrel domain-like<br /> <br /> Superfamily: PK beta-barrel domain-like<br /> <br /> Family: Pyruvate kinase beta-barrel domain<br /> <br /> Protein: Pyruvate Kinase (PK)<br /> <br /> Species: Human (Homo sapiens)<br /> <br /> As can be seen, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the K+ and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue). <br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}</div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1051131 Pyruvate Kinase 2010-03-01T20:47:27Z

<p>Keegan Gelvoria: </p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP.<br /> <br /> ==Mechanism==<br /> Pyruvate kinase catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate.<br /> <br /> ==Structure==<br /> Class: All Beta Proteins<br /> <br /> Fold: PK beta-barrel domain-like<br /> <br /> Superfamily: PK beta-barrel domain-like<br /> <br /> Family: Pyruvate kinase beta-barrel domain<br /> <br /> Protein: Pyruvate Kinase (PK)<br /> <br /> Species: Human (Homo sapiens)<br /> <br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}</div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1051130 Pyruvate Kinase 2010-03-01T20:46:36Z

<p>Keegan Gelvoria: </p> <hr /> <div>==Pyruvate Kinase==<br /> Pyruvate kinase is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP.<br /> <br /> ==Mechanism==<br /> Pyruvate kinase catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates both K+ and Mg2+ cations, which has two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate.<br /> <br /> ==Structure==<br /> Class: All Beta Proteins<br /> Fold: PK beta-barrel domain-like<br /> Superfamily: PK beta-barrel domain-like<br /> Family: Pyruvate kinase beta-barrel domain<br /> Protein: Pyruvate Kinase (PK)<br /> Species: Human (Homo sapiens)<br /> <br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_1liu | PDB=1liu | SCENE= }}</div>

Keegan Gelvoria https://proteopedia.org/index.php?title=Pyruvate_Kinase&diff=1051075 Pyruvate Kinase 2010-03-01T19:52:35Z

<p>Keegan Gelvoria: New page: ==Pyruvate Kinase== This is a test Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load and display another structure. {{STRUCTURE_2vgb | PDB=2vgb | SCENE=...</p> <hr /> <div>==Pyruvate Kinase==<br /> This is a test<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }}</div>

Keegan Gelvoria