Proteopedia - User contributions [en]

https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Rhiannon+Khela Proteopedia - User contributions [en] 2026-10-07T00:39:45Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1225211 Sandbox Reserved 347 2011-04-04T15:23:51Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> <br /> {{STRUCTURE_2iko | PDB=2iko | SCENE=Sandbox_Reserved_347/Close_up/1 }}<br /> =Introduction=<br /> <scene name='Sandbox_Reserved_347/Close_up/1'>Renin</scene> (pronounced /ˈriːnɨn/ REE-nin) is also known as angiotensinogenase, a monospecific enzyme that participates in the body's renin-angiotensin system (RAS). Renin is responsible for catalyzing the rate-limiting step in the synthesis of angiotensin II. Once renin and pro-renin bind to the pro-renin receptor, there is an increased enzymatic activity and additional physiological effects. <ref name="hypertension">doi:10.1016/j.jacc.2007.10.027<br /> </ref> <br /> <br /> <br /> ==Structure==<br /> Renin belongs in a family called aspartic proteases which use an aspartate residue for the catalysis of their peptide substrate. X-ray diffraction experiments has shown there is a striking similarity among the structures of aspartyl proteases. <ref name="3D">K Akahane, H Umeyama, S Nakagawa, I Moriguchi, S Hirose, K Iizuka, and K Murakami. "Three-dimensional structure of human renin". ''Hypertension''. 1985;7:3-12</ref> Renin consists of two homologous lobes each containing an aspartic acid. Between the lobes is the active site, which is catalyzed by the aspartic acid residues, a characteristic trait of all aspartate proteases. <ref name="hypertension"/> Renin in its full mature form has a mass of 37 kDa and contains 340 amino acids.<ref name="cloning">PMID:9556453</ref> Uniquely from other proteases, Renin has two β-carboxyl groups of Asp32 and Asp215 which protrude from each of the two lobes into the active site and has a large flap covering the <scene name='Sandbox_Reserved_347/Ligand/1'>Active site</scene>.<ref name= "Structure">PMID:2666611</ref> <br /> <br /> <br /> <br /> <Structure load='2iko' size='500' frame='true' align='right' caption='Renin active site' scene='Sandbox_Reserved_347/Ligand/1' /><br /> <br /> <br /> <br /> <br /> ==Function==<br /> [[Image:Man pic.png|thumb|left|Renin-Angiotensin-Aldosterone System]]<br /> <br /> Renin plays a key role in the Renin-Angiotension sysmtem (RAS). It is essential in facilitating the conversion of angiotension to angiotension II, which is the active component of the RAS system.<ref name="review">DOI: 10.1146/annurev.ph.40.030178.002113</ref> This system is responsible for the regulation of blood pressure, stimulation of the secretion of aldosterone which effects the salt and water balance.<ref name="review"/> <br /> *Angiotensinogen is released into the bloodstream by the liver. <br /> *Likewise, Renin is secreted by the kidneys into the bloodstream where is meets with angiotensinogen.<br /> *Once united, angiotensinogen form the decapeptide angiotensin (ANG) I.<br /> *ANG I is then activated by Angiotensin converting enzyme (ACE) to form the octapeptide ANG II.<br /> *ANG II then acts on specific receptors such as ones responsible for vasoconstriction or the release of aldosterone from the adrenal cortex. <ref name="renin review"> doi: 10.1152/physrev.00036.2005 <br /> </ref> <br /> <br /> <br /> <br /> <Structure load='2iko' size='300' frame='true' align='left' caption='Renin: Displaying the Ligand site' scene='Insert optional scene name here' /><br /> <br /> =References=<br /> <references/></div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1225209 Sandbox Reserved 347 2011-04-04T15:19:13Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> <br /> {{STRUCTURE_2iko | PDB=2iko | SCENE=Sandbox_Reserved_347/Close_up/1 }}<br /> =Introduction=<br /> <scene name='Sandbox_Reserved_347/Close_up/1'>Renin</scene> (pronounced /ˈriːnɨn/ REE-nin) is also known as angiotensinogenase, a monospecific enzyme that participates in the body's renin-angiotensin system (RAS). Renin is responsible for catalyzing the rate-limiting step in the synthesis of angiotensin II. Once renin and pro-renin bind to the pro-renin receptor, there is an increased enzymatic activity and additional physiological effects. <ref name="hypertension">doi:10.1016/j.jacc.2007.10.027<br /> </ref> <br /> <br /> <br /> ==Structure==<br /> Renin belongs in a family called aspartic proteases which use an aspartate residue for the catalysis of their peptide substrate. X-ray diffraction experiments has shown there is a striking similarity among the structures of aspartyl proteases. <ref name="3D">K Akahane, H Umeyama, S Nakagawa, I Moriguchi, S Hirose, K Iizuka, and K Murakami. "Three-dimensional structure of human renin". ''Hypertension''. 1985;7:3-12</ref> Renin consists of two homologous lobes each containing an aspartic acid. Between the lobes is the active site, which is catalyzed by the aspartic acid residues, a characteristic trait of all aspartate proteases. <ref name="hypertension"/> Renin in its full mature form has a mass of 37 kDa and contains 340 amino acids.<ref name="cloning">PMID:9556453</ref> Uniquely from other proteases, Renin has two β-carboxyl groups of Asp32 and Asp215 which protrude from each of the two lobes into the active site and has a large flap covering the <scene name='Sandbox_Reserved_347/Ligand/1'>Active site</scene>.<ref name= "Structure">PMID:2666611</ref> <br /> <br /> <br /> <br /> <Structure load='2iko' size='500' frame='true' align='right' caption='Renin active site' scene='Sandbox_Reserved_347/Ligand/1' /><br /> <br /> <br /> <br /> <br /> ==Function==<br /> [[Image:Man pic.png|thumb|left|Renin-Angiotensin-Aldosterone System]]<br /> <br /> Renin plays a key role in the Renin-Angiotension sysmtem (RAS). It is essential in facilitating the conversion of angiotension to angiotension II, which is the active component of the RAS system.<ref name="review">DOI: 10.1146/annurev.ph.40.030178.002113</ref> This system is responsible for the regulation of blood pressure, stimulation of the secretion of aldosterone which effects the salt and water balance.<ref name="review"/> <br /> *Angiotensinogen is released into the bloodstream by the liver. <br /> *Likewise, Renin is secreted by the kidneys into the bloodstream where is meets with angiotensinogen.<br /> *Once united, angiotensinogen form the decapeptide angiotensin (ANG) I.<br /> *ANG I is then activated by Angiotensin converting enzyme (ACE) to form the octapeptide ANG II.<br /> *ANG II then acts on specific receptors such as ones responsible for vasoconstriction or the release of aldosterone from the adrenal cortex. <ref name="renin review"> doi: 10.1152/physrev.00036.2005 <br /> </ref> <br /> <br /> <br /> <br /> <Structure load='2iko' size='300' frame='true' align='right' caption='Ligand site' scene='Insert optional scene name here' /><br /> <br /> =References=<br /> <references/></div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1225027 Sandbox Reserved 347 2011-04-04T08:33:40Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> <br /> {{STRUCTURE_2iko | PDB=2iko | SCENE=Sandbox_Reserved_347/Close_up/1 }}<br /> =Introduction=<br /> <scene name='Sandbox_Reserved_347/Close_up/1'>Renin</scene> (pronounced /ˈriːnɨn/ REE-nin) is also known as angiotensinogenase, a monospecific enzyme that participates in the body's renin-angiotensin system (RAS). Renin is responsible for catalyzing the rate-limiting step in the synthesis of angiotensin II. Once renin and pro-renin bind to the pro-renin receptor, there is an increased enzymatic activity and additional physiological effects. <ref name="hypertension">doi:10.1016/j.jacc.2007.10.027<br /> </ref> <br /> <br /> <br /> ==Structure==<br /> Renin belongs in a family called aspartic proteases which use an aspartate residue for the catalysis of their peptide substrate. X-ray diffraction experiments has shown there is a striking similarity among the structures of aspartyl proteases. <ref name="3D">K Akahane, H Umeyama, S Nakagawa, I Moriguchi, S Hirose, K Iizuka, and K Murakami. "Three-dimensional structure of human renin". ''Hypertension''. 1985;7:3-12</ref> Renin consists of two homologous lobes each containing an aspartic acid. Between the lobes is the active site, which is catalyzed by the aspartic acid residues, a characteristic trait of all aspartate proteases. <ref name="hypertension"/> Renin in its full mature form has a mass of 37 kDa and contains 340 amino acids.<ref name="cloning">PMID:9556453</ref> <br /> <br /> ==Biochemistry==<br /> [[Image:Man pic.png|thumb|left|Renin-Angiotensin-Aldosterone System]]<br /> Renin is an aspartyl protease. <ref name= "Structure">PMID:2666611</ref><br /> <Structure load='2iko' size='500' frame='true' align='right' caption='Renin active site' scene='Sandbox_Reserved_347/Ligand/1' /><br /> <scene name='Sandbox_Reserved_347/Ligand/1'>TextToBeDisplayed</scene><br /> *Renin is found in the blood stream where it breaks down angiotensinogen, which is secreted from the liver, into angiotensin I. <br /> *Angiotensin I is then cleaved in the lungs by angiotensin converting enzymes (ACE) into angiotensin II.<br /> <br /> <br /> ==Function==<br /> Renin plays a key role in the Renin-Angiotension sysmtem (RAS). It is essential in facilitating the conversion of angiotension to angiotension II, which is the active component of the system.<ref name="review">DOI: 10.1146/annurev.ph.40.030178.002113</ref> This system is responsible for the regulation of blood pressure, stimulation of the secretion of aldosterone which effects the salt and water balance.<ref name="review"/> <br /> <br /> <br /> <Structure load='2iko' size='300' frame='true' align='right' caption='Ligand site' scene='Insert optional scene name here' /><br /> <br /> =References=<br /> <references/></div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1225004 Sandbox Reserved 347 2011-04-04T08:12:09Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> <br /> {{STRUCTURE_2iko | PDB=2iko | SCENE=Sandbox_Reserved_347/Close_up/1 }}<br /> =Introduction=<br /> <scene name='Sandbox_Reserved_347/Close_up/1'>Renin</scene> (pronounced /ˈriːnɨn/ REE-nin) is also known as angiotensinogenase, a monospecific enzyme that participates in the body's renin-angiotensin system (RAS). Renin is responsible for catalyzing the rate-limiting step in the synthesis of angiotensin II. Once renin and pro-renin bind to the pro-renin receptor, there is an increased enzymatic activity and additional physiological effects. <ref name="hypertension">doi:10.1016/j.jacc.2007.10.027<br /> </ref> <br /> <br /> <br /> ==Structure==<br /> Renin belongs in a family called aspartic proteases which use an aspartate residue for the catalysis of their peptide substrate. X-ray diffraction experiments has shown there is a striking similarity among the structures of aspartyl proteases. <ref name="3D">K Akahane, H Umeyama, S Nakagawa, I Moriguchi, S Hirose, K Iizuka, and K Murakami. "Three-dimensional structure of human renin". ''Hypertension''. 1985;7:3-12</ref> Renin consists of two homologous lobes each containing an aspartic acid. Between the lobes is the active site, which is catalyzed by the aspartic acid residues, a characteristic trait of all aspartate proteases. <ref name="hypertension"/> Renin in its full mature form has a mass of 37 kDa and contains 340 amino acids.<ref name="cloning">PMID:9556453</ref> <br /> <br /> ==Biochemistry==<br /> Renin is an aspartyl protease. <ref name= "Structure">PMID:2666611</ref><br /> [[Image:Man pic.png|thumb|left|Renin-Angiotensin-Aldosterone System]]<br /> <Structure load='2iko' size='500' frame='true' align='right' caption='Renin active site' scene='Sandbox_Reserved_347/Ligand/1' /><br /> <scene name='Sandbox_Reserved_347/Ligand/1'>TextToBeDisplayed</scene><br /> <br /> ==Function==<br /> Renin plays a key role in the Renin-Angiotension sysmtem (RAS). It is essential in facilitating the conversion of angiotension to angiotension II, which is the active component of the system.<ref name="review">DOI: 10.1146/annurev.ph.40.030178.002113</ref> This system is responsible for the regulation of blood pressure, stimulation of the secretion of aldosterone which effects the salt and water balance.<ref name="review"/> <br /> <br /> <br /> <Structure load='2iko' size='300' frame='true' align='right' caption='Ligand site' scene='Insert optional scene name here' /><br /> <br /> =References=<br /> <references/></div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1224989 Sandbox Reserved 347 2011-04-04T08:02:32Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> <br /> {{STRUCTURE_2iko | PDB=2iko | SCENE=Sandbox_Reserved_347/Close_up/1 }}<br /> =Introduction=<br /> <scene name='Sandbox_Reserved_347/Close_up/1'>Renin</scene> (pronounced /ˈriːnɨn/ REE-nin) is also known as angiotensinogenase, a monospecific enzyme that participates in the body's renin-angiotensin system (RAS). Renin is responsible for catalyzing the rate-limiting step in the synthesis of angiotensin II. Once renin and pro-renin bind to the pro-renin receptor, there is an increased enzymatic activity and additional physiological effects. <ref name="hypertension">doi:10.1016/j.jacc.2007.10.027<br /> </ref> <br /> <br /> <br /> ==Structure==<br /> Renin belongs in a family called aspartic proteases which use an aspartate residue for the catalysis of their peptide substrate. X-ray diffraction experiments has shown there is a striking similarity among the structures of aspartyl proteases. <ref name="3D">K Akahane, H Umeyama, S Nakagawa, I Moriguchi, S Hirose, K Iizuka, and K Murakami. "Three-dimensional structure of human renin". ''Hypertension''. 1985;7:3-12</ref> Renin consists of two homologous lobes each containing an aspartic acid. Between the lobes is the active site, which is catalyzed by the aspartic acid residues, a characteristic trait of all aspartate proteases. <ref name="hypertension"/> Renin in its full mature form has a mass of 37 kDa and contains 340 amino acids.<ref name="cloning">PMID:9556453</ref> <br /> <br /> ==Biochemistry==<br /> Renin is an aspartyl protease. <ref name= "Structure">PMID:2666611</ref><br /> [[Image:Man pic.png|thumb|left|caption]]<br /> <Structure load='2iko' size='500' frame='true' align='right' caption='Insert caption here' scene='Sandbox_Reserved_347/Ligand/1' /><br /> <scene name='Sandbox_Reserved_347/Ligand/1'>TextToBeDisplayed</scene><br /> <br /> ==Function==<br /> Renin plays a key role in the Renin-Angiotension sysmtem (RAS). It is essential in facilitating the conversion of angiotension to angiotension II, which is the active component of the system.<ref name="review">DOI: 10.1146/annurev.ph.40.030178.002113</ref> This system is responsible for the regulation of blood pressure, stimulation of the secretion of aldosterone which effects the salt and water balance.<ref name="review"/> <br /> <br /> <br /> <Structure load='2iko' size='300' frame='true' align='right' caption='Ligand site' scene='Insert optional scene name here' /><br /> <br /> =References=<br /> <references/></div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1224980 Sandbox Reserved 347 2011-04-04T07:52:52Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> <br /> {{STRUCTURE_2iko | PDB=2iko | SCENE=Sandbox_Reserved_347/Close_up/1 }}<br /> =Introduction=<br /> <scene name='Sandbox_Reserved_347/Close_up/1'>Renin</scene> (pronounced /ˈriːnɨn/ REE-nin) is also known as angiotensinogenase, a monospecific enzyme that participates in the body's renin-angiotensin system (RAS). Renin is responsible for catalyzing the rate-limiting step in the synthesis of angiotensin II. Once renin and pro-renin bind to the pro-renin receptor, there is an increased enzymatic activity and additional physiological effects. <ref name="hypertension">doi:10.1016/j.jacc.2007.10.027<br /> </ref> <br /> <br /> <br /> ==Structure==<br /> Renin belongs in a family called aspartic proteases which use an aspartate residue for the catalysis of their peptide substrate. X-ray diffraction experiments has shown there is a striking similarity among the structures of aspartyl proteases. <ref name="3D">K Akahane, H Umeyama, S Nakagawa, I Moriguchi, S Hirose, K Iizuka, and K Murakami. "Three-dimensional structure of human renin". ''Hypertension''. 1985;7:3-12</ref> Renin consists of two homologous lobes each containing an aspartic acid. Between the lobes is the active site, which is catalyzed by the aspartic acid residues, a characteristic trait of all aspartate proteases. <ref name="hypertension"/> Renin in its full mature form has a mass of 37 kDa and contains 340 amino acids.<ref name="cloning">PMID:9556453</ref> <br /> <br /> ==Biochemistry==<br /> Renin is an aspartyl protease. <ref name= "Structure">PMID:2666611</ref><br /> [[Image:Man pic.png|thumb|left|caption]]<br /> <Structure load='2iko' size='500' frame='true' align='right' caption='Insert caption here' scene='Sandbox_Reserved_347/Ligand/1' /><br /> <scene name='Sandbox_Reserved_347/Ligand/1'>TextToBeDisplayed</scene><br /> <br /> ==Function==<br /> Renin plays a key role in the Renin-Angiotension sysmtem (RAS). This system is responsible for the control of blood pressure and salt balances in mammals.<br /> <ref name="review">DOI: 10.1146/annurev.ph.40.030178.002113</ref> <br /> <br /> <br /> <Structure load='2iko' size='300' frame='true' align='right' caption='Ligand site' scene='Insert optional scene name here' /><br /> <br /> =References=<br /> <references/></div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1224953 Sandbox Reserved 347 2011-04-04T07:24:41Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> <br /> {{STRUCTURE_2iko | PDB=2iko | SCENE=Sandbox_Reserved_347/Close_up/1 }}<br /> =Introduction=<br /> <scene name='Sandbox_Reserved_347/Close_up/1'>Renin</scene> (pronounced /ˈriːnɨn/ REE-nin) is also known as angiotensinogenase, a monospecific enzyme that participates in the body's renin-angiotensin system (RAS). Renin is responsible for catalyzing the rate-limiting step in the synthesis of angiotensin II. Once renin and pro-renin bind to the pro-renin receptor, there is an increased enzymatic activity and additional physiological effects. <ref name="hypertension">doi:10.1016/j.jacc.2007.10.027<br /> </ref> <br /> <br /> <br /> ==Structure==<br /> Renin belongs in a family called aspartic proteases which use an aspartate residue for the catalysis of their peptide substrate. X-ray diffraction experiments has shown there is a striking similarity among the structures of aspartyl proteases. <ref name="3D">K Akahane, H Umeyama, S Nakagawa, I Moriguchi, S Hirose, K Iizuka, and K Murakami. "Three-dimensional structure of human renin". ''Hypertension''. 1985;7:3-12</ref> Renin consists of two homologous lobes each containing an aspartic acid. Between the lobes is the active site, which is catalyzed by the aspartic acid residues, a characteristic trait of all aspartate proteases. <ref name="hypertension"/> Renin in its full mature form has a mass of 37 kDa and contains 340 amino acids.<ref name="cloning">PMID:9556453</ref> <br /> <br /> ==Biochemistry==<br /> Renin is an aspartyl protease. <ref name= "Structure">PMID:2666611</ref><br /> [[Image:Man pic.png|thumb|left|caption]]<br /> <Structure load='2iko' size='500' frame='true' align='right' caption='Insert caption here' scene='Sandbox_Reserved_347/Ligand/1' /><br /> <scene name='Sandbox_Reserved_347/Ligand/1'>TextToBeDisplayed</scene><br /> ==Function==<br /> Renin plays a key role in the Renin-Angiotension sysmtem (RAS). This system is responsible for the control of blood pressure and salt balances in mammals.<br /> <Structure load='2iko' size='300' frame='true' align='right' caption='Ligand site' scene='Insert optional scene name here' /><br /> <br /> =References=<br /> <references/></div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1224855 Sandbox Reserved 347 2011-04-04T05:42:38Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> <br /> {{STRUCTURE_2iko | PDB=2iko | SCENE=Sandbox_Reserved_347/Close_up/1 }}<br /> =Introduction=<br /> <scene name='Sandbox_Reserved_347/Close_up/1'>Renin</scene> (pronounced /ˈriːnɨn/ REE-nin) is also known as angiotensinogenase, a monospecific enzyme that participates in the body's renin-angiotensin system (RAS). Renin is responsible for catalyzing the rate-limiting step in the synthesis of angiotensin II. Once renin and pro-renin bind to the pro-renin receptor, there is an increased enzymatic activity and additional physiological effects. <ref name="hypertension">doi:10.1016/j.jacc.2007.10.027<br /> </ref> <br /> <br /> <br /> ==Structure==<br /> Renin belongs in the family called aspartic proteases because they use an aspartate residue for catalysis of their peptide substrate.<ref name="hypertension"/><br /> 3D structure <ref name="3D">K Akahane, H Umeyama, S Nakagawa, I Moriguchi, S Hirose, K Iizuka, and K Murakami. "Three-dimensional structure of human renin". ''Hypertension''. 1985;7:3-12</ref> <br /> <br /> ==Biochemistry==<br /> Renin is an aspartyl protease. <ref name= "Structure">PMID:2666611</ref><br /> [[Image:Man pic.png|thumb|left|caption]]<br /> <Structure load='2iko' size='500' frame='true' align='right' caption='Insert caption here' scene='Sandbox_Reserved_347/Ligand/1' /><br /> <scene name='Sandbox_Reserved_347/Ligand/1'>TextToBeDisplayed</scene><br /> ==Function==<br /> Renin plays a key role in the Renin-Angiotension sysmtem (RAS). This system is responsible for the control of blood pressure and salt balances in mammals.<br /> <Structure load='2iko' size='300' frame='true' align='right' caption='Ligand site' scene='Insert optional scene name here' /><br /> <br /> =References=<br /> <references/></div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1224785 Sandbox Reserved 347 2011-04-04T04:05:42Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> <br /> {{STRUCTURE_2iko | PDB=2iko | SCENE=Sandbox_Reserved_347/Close_up/1 }}<br /> =Introduction=<br /> <scene name='Sandbox_Reserved_347/Close_up/1'>Renin</scene> (pronounced /ˈriːnɨn/ REE-nin) is also known as angiotensinogenase, a monospecific enzyme that participates in the body's renin-angiotensin system (RAS). Renin is responsible for catalyzing the rate-limiting step in the synthesis of angiotensin II. Once renin and pro-renin bind to the pro-renin receptor, there is an increased enzymatic activity and additional physiological effects. <ref name="hypertension">doi:10.1016/j.jacc.2007.10.027<br /> </ref> <br /> <br /> <br /> ==Structure==<br /> Renin belongs in the family called aspartic proteases because they use an aspartate residue for catalysis of their peptide substrate.<ref name="hypertension"/><br /> <br /> ==Biochemistry==<br /> Renin is an aspartyl protease. <ref name= "Structure">PMID:2666611</ref><br /> [[Image:Man pic.png|thumb|left|caption]]<br /> <Structure load='2iko' size='500' frame='true' align='right' caption='Insert caption here' scene='Sandbox_Reserved_347/Ligand/1' /><br /> <scene name='Sandbox_Reserved_347/Ligand/1'>TextToBeDisplayed</scene><br /> ==Function==<br /> Renin plays a key role in the Renin-Angiotension sysmtem (RAS). This system is responsible for the control of blood pressure and salt balances in mammals.<br /> <Structure load='2iko' size='300' frame='true' align='right' caption='Ligand site' scene='Insert optional scene name here' /><br /> <br /> =References=<br /> <references/></div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1224778 Sandbox Reserved 347 2011-04-04T04:00:37Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> <br /> {{STRUCTURE_2iko | PDB=2iko | SCENE=Sandbox_Reserved_347/Close_up/1 }}<br /> =Introduction=<br /> <scene name='Sandbox_Reserved_347/Close_up/1'>Renin</scene> (pronounced /ˈriːnɨn/ REE-nin) is also known as angiotensinogenase, a monospecific enzyme that participates in the body's renin-angiotensin system (RAS). Renin is responsible for catalyzing the rate-limiting step in the synthesis of angiotensin II. Once renin and pro-renin bind to the pro-renin receptor, there is an increased enzymatic activity and additional physiological effects. <ref name= ”hypertension”>doi:10.1016/j.jacc.2007.10.027<br /> </ref> <br /> <br /> <br /> ==Structure==<br /> Renin belongs in the family called aspartic proteases because they use an aspartate residue for catalysis of their peptide substrate.<ref name=”hypertension”/><br /> <br /> ==Biochemistry==<br /> Renin is an aspartyl protease. <ref name= "Structure">PMID:2666611</ref><br /> [[Image:Man pic.png|thumb|left|caption]]<br /> <Structure load='2iko' size='500' frame='true' align='right' caption='Insert caption here' scene='Sandbox_Reserved_347/Ligand/1' /><br /> <scene name='Sandbox_Reserved_347/Ligand/1'>TextToBeDisplayed</scene><br /> ==Function==<br /> Renin plays a key role in the Renin-Angiotension sysmtem (RAS). This system is responsible for the control of blood pressure and salt balances in mammals.<br /> <Structure load='2iko' size='300' frame='true' align='right' caption='Ligand site' scene='Insert optional scene name here' /><br /> <br /> =References=<br /> <references/></div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1224728 Sandbox Reserved 347 2011-04-04T02:49:02Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> <br /> {{STRUCTURE_2iko | PDB=2iko | SCENE=Sandbox_Reserved_347/Close_up/1 }}<br /> =Introduction=<br /> <scene name='Sandbox_Reserved_347/Close_up/1'>Renin</scene> (pronounced /ˈriːnɨn/ REE-nin) is also known as angiotensinogenase, a monospecific enzyme that participates in the body's renin-angiotensin system (RAS). Renin is responsible for catalyzing the rate-limiting step in the synthesis of angiotensin II. Once renin and pro-renin bind to the pro-renin receptor, there is an increased enzymatic activity and additional physiological effects. <ref name= ”hypertension”>doi:10.1016/j.jacc.2007.10.027<br /> </ref> <br /> <br /> <br /> ==Structure==<br /> Renin belongs in the family called aspartic proteases because they use an aspartate residue for catalysis of their peptide substrate. <ref name= ”hypertension”>doi:10.1016/j.jacc.2007.10.027<br /> </ref><br /> <br /> ==Biochemistry==<br /> Renin is an aspartyl protease. <ref name= "Structure">PMID:2666611</ref><br /> [[Image:Man pic.png|thumb|left|caption]]<br /> <Structure load='2iko' size='500' frame='true' align='right' caption='Insert caption here' scene='Sandbox_Reserved_347/Ligand/1' /><br /> <scene name='Sandbox_Reserved_347/Ligand/1'>TextToBeDisplayed</scene><br /> ==Function==<br /> Renin plays a key role in the Renin-Angiotension sysmtem (RAS). This system is responsible for the control of blood pressure and salt balances in mammals.<br /> <Structure load='2iko' size='300' frame='true' align='right' caption='Ligand site' scene='Insert optional scene name here' /><br /> <br /> =References=<br /> <references/></div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1224689 Sandbox Reserved 347 2011-04-04T02:07:17Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> <br /> {{STRUCTURE_2iko | PDB=2iko | SCENE=Sandbox_Reserved_347/Close_up/1 }}<br /> =Introduction=<br /> <br /> <scene name='Sandbox_Reserved_347/Close_up/1'>Renin</scene> (pronounced /ˈriːnɨn/ REE-nin) is also known as angiotensinogenase, a monospecific enzyme that participates in the body's renin-angiotensin system (RAS). Renin is responsible for catalyzing the rate-limiting step in the synthesis of angiotensin II. Once renin and pro-renin bind to the pro-renin receptor, there is an increased enzymatic activity and additional physiological effects. <ref name= ”hypertension”>doi:10.1016/j.jacc.2007.10.027<br /> </ref> <br /> <br /> <br /> ==Structure==<br /> Renin belongs in the family called aspartic proteases because they use an aspartate residue for catalysis of their peptide substrate. <ref name= ”hypertension”>doi:10.1016/j.jacc.2007.10.027<br /> </ref><br /> <br /> ==Biochemistry==<br /> Renin is an aspartyl protease. <ref name= "Structure">PMID:2666611</ref><br /> [[Image:Man pic.png|thumb|left|caption]]<br /> <Structure load='2iko' size='500' frame='true' align='right' caption='Insert caption here' scene='Sandbox_Reserved_347/Ligand/1' /><br /> <scene name='Sandbox_Reserved_347/Ligand/1'>TextToBeDisplayed</scene><br /> ==Function==<br /> Renin plays a key role in the Renin-Angiotension sysmtem (RAS). This system is responsible for the control of blood pressure and salt balances in mammals.<br /> <Structure load='2iko' size='300' frame='true' align='right' caption='Ligand site' scene='Insert optional scene name here' /><br /> <br /> =References=<br /> <references/></div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1224683 Sandbox Reserved 347 2011-04-04T02:00:57Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> <br /> {{STRUCTURE_2iko | PDB=2iko | SCENE=Sandbox_Reserved_347/Close_up/1 }}<br /> =Introduction=<br /> Renin (pronounced /ˈriːnɨn/ REE-nin) is also known as angiotensinogenase, a monospecific enzyme that participates in the body's renin-angiotensin system (RAS). Renin is responsible for catalyzing the rate-limiting step in the synthesis of angiotensin II. Once renin and pro-renin bind to the pro-renin receptor, there is an increased enzymatic activity and additional physiological effects. <ref name= ”hypertension”>doi:10.1016/j.jacc.2007.10.027<br /> </ref> <br /> <br /> <scene name='Sandbox_Reserved_347/Close_up/1'>TextToBeDisplayed</scene><br /> <br /> ==Structure==<br /> Renin belongs in the family called aspartic proteases because they use an aspartate residue for catalysis of their peptide substrate. <ref name= ”hypertension”>doi:10.1016/j.jacc.2007.10.027<br /> </ref><br /> <br /> ==Biochemistry==<br /> Renin is an aspartyl protease. <ref name= "Structure">PMID:2666611</ref><br /> [[Image:Man pic.png|thumb|left|caption]]<br /> <Structure load='2iko' size='500' frame='true' align='right' caption='Insert caption here' scene='Sandbox_Reserved_347/Ligand/1' /><br /> <scene name='Sandbox_Reserved_347/Ligand/1'>TextToBeDisplayed</scene><br /> ==Function==<br /> Renin plays a key role in the Renin-Angiotension sysmtem (RAS). This system is responsible for the control of blood pressure and salt balances in mammals.<br /> <Structure load='2iko' size='300' frame='true' align='right' caption='Ligand site' scene='Insert optional scene name here' /><br /> <br /> =References=<br /> <references/></div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1224624 Sandbox Reserved 347 2011-04-04T01:19:44Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> =Introduction=<br /> {{STRUCTURE_2iko | PDB=2iko | SCENE=Sandbox_Reserved_347/Close_up/1 }}<br /> <br /> :Renin (pronounced /ˈriːnɨn/ REE-nin)is also known as angiotensinogenase,an enzyme that participates in the body's renin-angiotensin system (RAS) which mediates extracellular volume and arterial vasoconstriction. <br /> ::Thus, it regulates the body's mean arterial blood pressure. <ref name= "3D">PMID:3884499</ref><br /> <scene name='Sandbox_Reserved_347/Close_up/1'>TextToBeDisplayed</scene><br /> <br /> ==Structure==<br /> Renin belongs in the family called aspartic proteases because they use an aspartate residue for catalysis of their peptide substrate. <ref name= ”hypertension”>doi:10.1016/j.jacc.2007.10.027<br /> </ref><br /> <br /> ==Biochemistry==<br /> Renin is an aspartyl protease. <ref name= "Structure">PMID:2666611</ref><br /> [[Image:Man pic.png|thumb|left|caption]]<br /> <Structure load='2iko' size='500' frame='true' align='right' caption='Insert caption here' scene='Sandbox_Reserved_347/Ligand/1' /><br /> <scene name='Sandbox_Reserved_347/Ligand/1'>TextToBeDisplayed</scene><br /> ==Function==<br /> Renin plays a key role in the Renin-Angiotension sysmtem (RAS). This system is responsible for the control of blood pressure and salt balances in mammals.<br /> <Structure load='2iko' size='300' frame='true' align='right' caption='Ligand site' scene='Insert optional scene name here' /><br /> <br /> =References=<br /> <references/></div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1224601 Sandbox Reserved 347 2011-04-04T00:49:25Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> =Introduction=<br /> {{STRUCTURE_2iko | PDB=2iko | SCENE=Sandbox_Reserved_347/Close_up/1 }}<br /> <br /> :Renin (pronounced /ˈriːnɨn/ REE-nin)is also known as angiotensinogenase,an enzyme that participates in the body's renin-angiotensin system (RAS) which mediates extracellular volume and arterial vasoconstriction. <br /> ::Thus, it regulates the body's mean arterial blood pressure. <ref name= "3D">PMID:3884499</ref><br /> <scene name='Sandbox_Reserved_347/Close_up/1'>TextToBeDisplayed</scene><br /> <br /> ==Structure==<br /> Renin belongs in the family called aspartic proteases because they use an aspartate residue for catalysis of their peptide substrate. <ref name= ”hypertension”>doi:10.1016</ref><br /> <br /> ==Biochemistry==<br /> Renin is an aspartyl protease. <ref name= "Structure">PMID:2666611</ref><br /> [[Image:Man pic.png|thumb|left|caption]]<br /> <Structure load='2iko' size='500' frame='true' align='right' caption='Insert caption here' scene='Sandbox_Reserved_347/Ligand/1' /><br /> <scene name='Sandbox_Reserved_347/Ligand/1'>TextToBeDisplayed</scene><br /> ==Function==<br /> Renin plays a key role in the Renin-Angiotension sysmtem (RAS). This system is responsible for the control of blood pressure and salt balances in mammals.<br /> <Structure load='2iko' size='300' frame='true' align='right' caption='Ligand site' scene='Insert optional scene name here' /><br /> <br /> =References=<br /> <references/></div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1200875 Sandbox Reserved 347 2011-03-04T00:13:42Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> =Introduction=<br /> {{STRUCTURE_2iko | PDB=2iko | SCENE=Sandbox_Reserved_347/Close_up/1 }}<br /> <br /> :Renin (pronounced /ˈriːnɨn/ REE-nin), also known as angiotensinogenase is an enzyme that participates in the body's renin-angiotensin system (RAS) that mediates extracellular volume (i.e., that of the blood plasma, lymph and interstitial fluid), and arterial vasoconstriction. <br /> ::Thus, it regulates the body's mean arterial blood pressure. <ref name= "3D">PMID:3884499</ref><br /> <scene name='Sandbox_Reserved_347/Close_up/1'>TextToBeDisplayed</scene><br /> <br /> ==Biochemistry==<br /> Renin is an aspartyl protease. <ref name= "Structure">PMID:2666611</ref><br /> [[Image:Man pic.png|thumb|left|caption]]<br /> <Structure load='2iko' size='500' frame='true' align='right' caption='Insert caption here' scene='Sandbox_Reserved_347/Ligand/1' /><br /> <scene name='Sandbox_Reserved_347/Ligand/1'>TextToBeDisplayed</scene><br /> ==Function==<br /> Renin plays a key role in the Renin-Angiotension sysmtem (RAS). This system is responsible for the control of blood pressure and salt balances in mammals.<br /> <Structure load='2iko' size='300' frame='true' align='right' caption='Ligand site' scene='Insert optional scene name here' /><br /> <br /> =References=<br /> <references/></div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1200871 Sandbox Reserved 347 2011-03-04T00:03:57Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> =Introduction=<br /> {{STRUCTURE_2iko | PDB=2iko | SCENE=Sandbox_Reserved_347/Close_up/1 }}<br /> <br /> :Renin (pronounced /ˈriːnɨn/ REE-nin), also known as angiotensinogenase is an enzyme that participates in the body's renin-angiotensin system (RAS) that mediates extracellular volume (i.e., that of the blood plasma, lymph and interstitial fluid), and arterial vasoconstriction. <br /> ::Thus, it regulates the body's mean arterial blood pressure. <ref name= "3D">PMID:3884499</ref><br /> <scene name='Sandbox_Reserved_347/Close_up/1'>TextToBeDisplayed</scene><br /> <br /> ==Biochemistry==<br /> Renin is an aspartyl protease. <ref name= "Structure">PMID:2666611</ref><br /> [[Image:Man pic.png|thumb|left|caption]]<br /> <br /> ==Function==<br /> Renin plays a key role in the Renin-Angiotension sysmtem (RAS). This system is responsible for the control of blood pressure and salt balances in mammals.<br /> <Structure load='2iko' size='300' frame='true' align='right' caption='Ligand site' scene='Insert optional scene name here' /><br /> <br /> =References=<br /> <references/></div>

Rhiannon Khela https://proteopedia.org/index.php?title=File:Man_pic.png&diff=1200850 File:Man pic.png 2011-03-03T23:50:21Z

<p>Rhiannon Khela: </p> <hr /> <div></div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1200830 Sandbox Reserved 347 2011-03-03T23:37:31Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> =Introduction=<br /> {{STRUCTURE_2iko | PDB=2iko | SCENE= }}<br /> <br /> :Renin (pronounced /ˈriːnɨn/ REE-nin), also known as angiotensinogenase is an enzyme that participates in the body's renin-angiotensin system (RAS) that mediates extracellular volume (i.e., that of the blood plasma, lymph and interstitial fluid), and arterial vasoconstriction. <br /> ::Thus, it regulates the body's mean arterial blood pressure. <ref name= "3D">PMID:3884499</ref><br /> <scene name='Sandbox_Reserved_347/Close_up/1'>TextToBeDisplayed</scene><br /> <br /> ==Biochemistry==<br /> Renin is an aspartyl protease. <ref name= "Structure">PMID:2666611</ref><br /> <br /> ==Function==<br /> Renin plays a key role in the Renin-Angiotension sysmtem (RAS). This system is responsible for the control of blood pressure and salt balances in mammals.<br /> <Structure load='2iko' size='300' frame='true' align='right' caption='Ligand site' scene='Insert optional scene name here' /><br /> <br /> =References=<br /> <references/></div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1200827 Sandbox Reserved 347 2011-03-03T23:36:56Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> =Introduction=<br /> {{STRUCTURE_2iko | PDB=2iko | SCENE= }}<br /> <br /> :Renin (pronounced /ˈriːnɨn/ REE-nin), also known as angiotensinogenase is an enzyme that participates in the body's renin-angiotensin system (RAS) that mediates extracellular volume (i.e., that of the blood plasma, lymph and interstitial fluid), and arterial vasoconstriction. <br /> ::Thus, it regulates the body's mean arterial blood pressure. <ref name= "3D">PMID:3884499</ref><br /> <scene name='Sandbox_Reserved_347/Close_up/1'>TextToBeDisplayed</scene><br /> <br /> ==Biochemistry==<br /> Renin is an aspartyl protease. <ref name= "Structure"> 2666611</ref><br /> <br /> ==Function==<br /> Renin plays a key role in the Renin-Angiotension sysmtem (RAS). This system is responsible for the control of blood pressure and salt balances in mammals.<br /> <Structure load='2iko' size='300' frame='true' align='right' caption='Ligand site' scene='Insert optional scene name here' /><br /> <br /> =References=<br /> <references/></div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1200825 Sandbox Reserved 347 2011-03-03T23:36:20Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> =Introduction=<br /> {{STRUCTURE_2iko | PDB=2iko | SCENE= }}<br /> <br /> :Renin (pronounced /ˈriːnɨn/ REE-nin), also known as angiotensinogenase is an enzyme that participates in the body's renin-angiotensin system (RAS) that mediates extracellular volume (i.e., that of the blood plasma, lymph and interstitial fluid), and arterial vasoconstriction. <br /> ::Thus, it regulates the body's mean arterial blood pressure. <ref name= "3D"> 3884499</ref><br /> <scene name='Sandbox_Reserved_347/Close_up/1'>TextToBeDisplayed</scene><br /> <br /> ==Biochemistry==<br /> Renin is an aspartyl protease. <ref name= "Structure"> 2666611</ref><br /> <br /> ==Function==<br /> Renin plays a key role in the Renin-Angiotension sysmtem (RAS). This system is responsible for the control of blood pressure and salt balances in mammals.<br /> <Structure load='2iko' size='300' frame='true' align='right' caption='Ligand site' scene='Insert optional scene name here' /><br /> <br /> =References=<br /> <references/></div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1200797 Sandbox Reserved 347 2011-03-03T23:20:51Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> =Introduction=<br /> {{STRUCTURE_2iko | PDB=2iko | SCENE= }}<br /> <br /> :Renin (pronounced /ˈriːnɨn/ REE-nin), also known as angiotensinogenase is an enzyme that participates in the body's renin-angiotensin system (RAS) that mediates extracellular volume (i.e., that of the blood plasma, lymph and interstitial fluid), and arterial vasoconstriction. <br /> ::Thus, it regulates the body's mean arterial blood pressure. <ref name= "3D"> 3884499</ref><br /> <scene name='Sandbox_Reserved_347/Close_up/1'>TextToBeDisplayed</scene><br /> <br /> ==Biochemistry==<br /> Renin is an aspartyl protease. <ref name= "Structure"> 2666611</ref><br /> <br /> ==Function==<br /> Renin plays a key role in the Renin-Angiotension sysmtem (RAS). This system is responsible for the control of blood pressure and salt balances in mammals.<br /> <br /> =References=<br /> <references/></div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1200793 Sandbox Reserved 347 2011-03-03T23:08:43Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> =Introduction=<br /> {{STRUCTURE_2iko | PDB=2iko | SCENE= }}<br /> :Renin (pronounced /ˈriːnɨn/ REE-nin), also known as angiotensinogenase is an enzyme that participates in the body's renin-angiotensin system (RAS) that mediates extracellular volume (i.e., that of the blood plasma, lymph and interstitial fluid), and arterial vasoconstriction. <br /> ::Thus, it regulates the body's mean arterial blood pressure. <ref name= "3D"> 3884499</ref><br /> <br /> ==Biochemistry==<br /> Renin is an aspartyl protease. <ref name= "Structure"> 2666611</ref><br /> <br /> ==Function==<br /> Renin plays a key role in the Renin-Angiotension sysmtem (RAS). This system is responsible for the control of blood pressure and salt balances in mammals.<br /> <br /> =References=<br /> <references/></div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1200789 Sandbox Reserved 347 2011-03-03T23:08:06Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> =Introduction=<br /> {{STRUCTURE_2iko | PDB=2iko | SCENE= }}<br /> :Renin (pronounced /ˈriːnɨn/ REE-nin), also known as angiotensinogenase is an enzyme that participates in the body's renin-angiotensin system (RAS) that mediates extracellular volume (i.e., that of the blood plasma, lymph and interstitial fluid), and arterial vasoconstriction. <br /> ::Thus, it regulates the body's mean arterial blood pressure. <ref name= "Structure"> 3884499</ref><br /> <br /> ==Biochemistry==<br /> Renin is an aspartyl protease. <ref name= "Structure"> 2666611</ref><br /> <br /> ==Function==<br /> Renin plays a key role in the Renin-Angiotension sysmtem (RAS). This system is responsible for the control of blood pressure and salt balances in mammals.<br /> <br /> =References=<br /> <references/></div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1200782 Sandbox Reserved 347 2011-03-03T23:03:25Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> =Introduction=<br /> {{STRUCTURE_2iko | PDB=2iko | SCENE= }}<br /> :Renin (pronounced /ˈriːnɨn/ REE-nin), also known as angiotensinogenase is an enzyme that participates in the body's renin-angiotensin system (RAS) that mediates extracellular volume (i.e., that of the blood plasma, lymph and interstitial fluid), and arterial vasoconstriction. <br /> ::Thus, it regulates the body's mean arterial blood pressure. <<br /> <br /> ==Biochemistry==<br /> Renin is an aspartyl protease. <ref name= "Structure"> 2666611</ref><br /> <br /> ==Function==<br /> Renin plays a key role in the Renin-Angiotension sysmtem (RAS). This system is responsible for the control of blood pressure and salt balances in mammals.<br /> <br /> =References=<br /> <references/></div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1200781 Sandbox Reserved 347 2011-03-03T23:02:40Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> =Introduction=<br /> {{STRUCTURE_2iko | PDB=2iko | SCENE= }}<br /> :Renin (pronounced /ˈriːnɨn/ REE-nin), also known as angiotensinogenase is an enzyme that participates in the body's renin-angiotensin system (RAS) that mediates extracellular volume (i.e., that of the blood plasma, lymph and interstitial fluid), and arterial vasoconstriction. <br /> ::Thus, it regulates the body's mean arterial blood pressure. <<br /> <br /> ==Biochemistry==<br /> Renin is an aspartyl protease. <ref name= "Structure"> 2666611</ref><br /> <br /> ==Function==<br /> Renin plays a key role in the Renin-Angiotension sysmtem (RAS). This system is responsible for the control of blood pressure and salt balances in mammals.</div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1200780 Sandbox Reserved 347 2011-03-03T22:53:06Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> =intro=<br /> {{STRUCTURE_2iko | PDB=2iko | SCENE= }}<br /> :Renin (pronounced /ˈriːnɨn/ REE-nin), also known as angiotensinogenase is an enzyme that participates in the body's renin-angiotensin system (RAS) that mediates extracellular volume (i.e., that of the blood plasma, lymph and interstitial fluid), and arterial vasoconstriction. <br /> ::Thus, it regulates the body's mean arterial blood pressure.</div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1200779 Sandbox Reserved 347 2011-03-03T22:50:41Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> =intro=<br /> {{STRUCTURE_2iko | PDB=2iko | SCENE= }}</div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1200774 Sandbox Reserved 347 2011-03-03T22:49:21Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> <br /> {{STRUCTURE_2IK0|PDB=2IK0|SCENE=}}</div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1200772 Sandbox Reserved 347 2011-03-03T22:48:40Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> <br /> {{STRUCTURE_2IKO|PDB=2IKO|SCENE=}}</div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1200771 Sandbox Reserved 347 2011-03-03T22:47:15Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> <br /> {{STRUCTURE_2IKO | PDB=2IKO | SCENE=}}</div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1200770 Sandbox Reserved 347 2011-03-03T22:42:51Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> <br /> {{STRUCTURE_2IKO | 2IKO | SCENE=}}</div>

Rhiannon Khela https://proteopedia.org/index.php?title=Sandbox_Reserved_347&diff=1200769 Sandbox Reserved 347 2011-03-03T22:39:53Z

<p>Rhiannon Khela: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> <br /> <br /> {{STRUCTURE_2IKO|2IKO|SCENE=}}</div>

Rhiannon Khela https://proteopedia.org/index.php?title=Glutamine_synthetase&diff=1064791 Glutamine synthetase 2010-04-01T04:06:09Z

<p>Rhiannon Khela: </p> <hr /> <div>=''' Glutamine Synthetase '''=<br /> <br /> <br /> <br /> ==Structure==<br /> {{STRUCTURE_2gls| PDB=2gls | SCENE=Sandbox_169/2gls/1 }}<br /> An unrefined structure of glutamine synthetase is made of two layers, each containing 6 subunits, for a total of 12 subunits. <ref name="Yamashita">PMID:2572586 </ref> Each subunit contains an <scene name='Sandbox_169/Mn_in_the_active_site/2'>active site </scene>which is defined by a cylindrical shape formed by six antiparalel β starnds contributed by one subunit and two more strands by the neighbouring subunit. <ref name="Yamashita"/> In each cylindrical active site there are two Mn2+ ions: Mn 2+ 469 and 470. Both are attached to three protein chains and two water molecules, one of the water molecules are shared by both Mn2+. The protein ligands. Attached to Mn 2+ 469 is: Glu-131, GLu-212 and Glu-220, and the protein ligands attached to Mn 2+ are: Glu-129, His-269 and Glu-357.<ref name="Yamashita"/> <br /> <br /> Unique to glutamine synthetase, unlike other enzymes, is it's "passive site". This refers to the central loop which is formed by a segment of the backbone that extends into the central aqueous cavity. <ref name="Yamashita"/>Unlike other sites in glutamine synthetase under the same conditions, this site is suceptible to proteolysis by four secreated proteases from the V8 protease of ''Staphylococcus aureus''.<ref name="Yamashita"/><br /> <br /> [[Image:Passive site.png |left||thumb|Figure 1: A clear view of glutamine synthetases "passive site".]]<br /> <br /> <br /> <br /> ==Classes==<br /> <br /> Glutamine synthetase has been described as having three destinctive types:<ref name="Brown">PMID:7916055 </ref><br /> *Class I (GSI): Genes for this class have only been found in bacteria (eubacteria) and archaea (arhaebacteria. The paper by Kumada ''et. al'' goes into detail on these two.<ref name="Kumada">PMID:8096645 </ref><br /> *Class II (GSII): Genes for this class have only been found in eukaryotes and a few soil-dwelling bacteria.The paper by Kumada gets into further detail about these bacteria. <ref name="Kumada"/><br /> *Class III (GSIII): Genes from this class have only been found in a few bacterial species.It is a hexamer of identical chains. It is much larger (about 700 amino acids) than the GSI (450 to 470 amino acids) or GSII (350 to 420 amino acids) enzymes. <ref name="Brown"/> Brown ''et. al.''(1994) explain in their paper the idea that lateral gene transfer from archeal GSI may have happened and explain the gene mutation.<ref name="Brown"/> <br /> <br /> [[Image:Glutamine-synthesis.jpg|thumb | Figure 2: Two step process of sythesis of glutamine from glutamate, synthesised by glutamine synthesis.]]<br /> <br /> ==Function==<br /> <br /> Glutamine synthetase (GS) is an essential enzyme in the cellular nitrogen metabolism and has been found to play a role in both ammonia assimilation and glutamine byosynthesis.<ref name="Kumada"/> It is the only enzyme capable of glutamine synthesis and is required for the two step process synthesizing glutamate to glutamine. The glutamine produced is an essential precursor for purine and pyrimidine synthesis, a modulator of protein turnover or an intermediate for gluconeogenesis and acid-base balance. <ref>He,Youji, Hakvoort,Theodorus, B.M., Kohler,S.Eleonor, Vermeulen,Jacqueline L.M.,Rudi de Waart, D., Theije,Chiel de, Gabrie A.M. ten Have, Van Eijk,Hans M.H., Kunne,Cindy, Labruyere,Wilelmina T., Houten,Sander M., Sokolovic,Mika, Tuijter,Jan M., Deutz,Nicolaas E.P., and Lamers, Wouter H. Glutamine Synthetase in muscle is required for glutamine production druing fasting and extrahepatic ammonia detoxification. The American Society for Biochemistry and Molecular Biology, January 11, 2010 </ref><br /> <br /> <br /> ==References==<br /> <references/><br /> <br /> <table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr><br /> Rhiannon Khela</div>

Rhiannon Khela https://proteopedia.org/index.php?title=Glutamine_synthetase&diff=1064784 Glutamine synthetase 2010-04-01T04:00:58Z

<p>Rhiannon Khela: </p> <hr /> <div>=''' Glutamine Synthetase '''=<br /> <br /> <br /> <br /> ==Structure==<br /> {{STRUCTURE_2gls| PDB=2gls | SCENE=Sandbox_169/2gls/1 }}<br /> An unrefined structure of glutamine synthetase is made of two layers, each containing 6 subunits, for a total of 12 subunits. <ref name="Yamashita">PMID:2572586 </ref> Each subunit contains an <scene name='Sandbox_169/Mn_in_the_active_site/2'>active site </scene>which is defined by a cylindrical shape formed by six antiparalel β starnds contributed by one subunit and two more strands by the neighbouring subunit. <ref name="Yamashita"/> In each cylindrical active site there are two Mn2+ ions: Mn 2+ 469 and 470. Both are attached to three protein chains and two water molecules, one of the water molecules are shared by both Mn2+. The protein ligands. Attached to Mn 2+ 469 is: Glu-131, GLu-212 and Glu-220, and the protein ligands attached to Mn 2+ are: Glu-129, His-269 and Glu-357.<ref name="Yamashita"/> <br /> <br /> Unique to glutamine synthetase, unlike other enzymes, is it's "passive site". This refers to the central loop which is formed by a segment of the backbone that extends into the central aqueous cavity. <ref name="Yamashita"/>Unlike other sites in glutamine synthetase under the same conditions, this site is suceptible to proteolysis by four secreated proteases from the V8 protease of ''Staphylococcus aureus''.<ref name="Yamashita"/><br /> <br /> [[Image:Passive site.png |left||thumb|Figure 1: A clear view of glutamine synthetases "passive site".]]<br /> <br /> <br /> <br /> ==Classes==<br /> <br /> Glutamine synthetase has been described as having three destinctive types:<ref name="Brown">PMID:7916055 </ref><br /> *Class I (GSI): Genes for this class have only been found in bacteria (eubacteria) and archaea (arhaebacteria. The paper by Kumada ''et. al'' goes into detail on these two.<ref name="Kumada">PMID:8096645 </ref><br /> *Class II (GSII): Genes for this class have only been found in eukaryotes and a few soil-dwelling bacteria.The paper by Kumada gets into further detail about these bacteria. <ref name="Kumada"/><br /> *Class III (GSIII): Genes from this class have only been found in a few bacterial species.It is a hexamer of identical chains. It is much larger (about 700 amino acids) than the GSI (450 to 470 amino acids) or GSII (350 to 420 amino acids) enzymes. <ref name="Brown"/> Brown ''et. al.''(1994)explain in their paper the idea that lateral gene transfer from archeal GSI may have happened and explain the gene mutation.<ref name="Brown"/> <br /> <br /> [[Image:Glutamine-synthesis.jpg|thumb | Figure 2: Two step process of sythesis of glutamine from glutamate, synthesised by glutamine synthesis.]]<br /> <br /> ==Function==<br /> <br /> Glutamine synthetase (GS) is an essential enzyme in the cellular nitrogen metabolism and has been found to play a role in both ammonia assimilation and glutamine byosynthesis.<ref name="Kumada"/> It is the only enzyme capable of glutamine synthesis and is required for the two step process synthesizing glutamate to glutamine. The glutamine produced is an essential precursor for purine and pyrimidine synthesis, a modulator of protein turnover or an intermediate for gluconeogenesis and acid-base balance. <ref>He,Youji, Hakvoort,Theodorus, B.M., Kohler,S.Eleonor, Vermeulen,Jacqueline L.M.,Rudi de Waart, D., Theije,Chiel de, Gabrie A.M. ten Have, Van Eijk,Hans M.H., Kunne,Cindy, Labruyere,Wilelmina T., Houten,Sander M., Sokolovic,Mika, Tuijter,Jan M., Deutz,Nicolaas E.P., and Lamers, Wouter H. Glutamine Synthetase in muscle is required for glutamine production druing fasting and extrahepatic ammonia detoxification. The American Society for Biochemistry and Molecular Biology, January 11, 2010 </ref><br /> <br /> <br /> ==References==<br /> <references/><br /> <br /> <table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr><br /> Rhiannon Khela</div>

Rhiannon Khela https://proteopedia.org/index.php?title=Glutamine_synthetase&diff=1064590 Glutamine synthetase 2010-03-31T23:01:50Z

<p>Rhiannon Khela: </p> <hr /> <div>=''' Glutamine Synthetase '''=<br /> <br /> <br /> <br /> ==Structure==<br /> {{STRUCTURE_2gls| PDB=2gls | SCENE=Sandbox_169/2gls/1 }}<br /> An unrefined structure of glutamine synthetase is made of two layers, each containing 6 subunits, for a total of 12 subunits. <ref name="Yamashita">PMID:2572586 </ref> Each subunit contains an <scene name='Sandbox_169/Mn_in_the_active_site/2'>active site </scene>which is defined by a cylindrical shape formed by six antiparalel β starnds contributed by one subunit and two more strands by the neighbouring subunit. <ref name="Yamashita"/> In each cylindrical active site there are two Mn2+ ions: Mn 2+ 469 and 470. Both are attached to three protein chains and two water molecules, one of the water molecules are shared by both Mn2+. The protein ligands. Attached to Mn 2+ 469 is: Glu-131, GLu-212 and Glu-220, and the protein ligands attached to Mn 2+ are: Glu-129, His-269 and Glu-357.<ref name="Yamashita"/> <br /> <br /> Unique to glutamine synthetase, unlike other enzymes, is it's "passive site". This refers to the central loop which is formed by a segment of the backbone that extends into the central aqueous cavity. <ref name="Yamashita"/>Unlike other sites in glutamine synthetase under the same conditions, this site is suceptible to proteolysis by four secreated proteases from the V8 protease of ''Staphylococcus aureus''.<ref name="Yamashita"/><br /> <br /> [[Image:Passive site.png |left||thumb|Figure 1: A clear view of glutamine synthetases "passive site".]]<br /> <br /> <br /> <br /> ==Classes==<br /> <br /> Glutamine synthetase has been described as having three destinctive types:<ref name="Brown">PMID:7916055 </ref><br /> *Class I (GSI): Genes for this class have only been found in bacteria (eubacteria) and archaea (arhaebacteria. The paper by Kumada ''et. al'' goes into detail on these two.<ref name="Kumada">PMID:8096645 </ref><br /> *Class II (GSII): Genes for this class have only been found in eukaryotes and a few soil-dwelling bacteria.The paper by Kumada gets into further detail about these bacteria. <ref name="Kumada"/><br /> *Class III (GSIII): Genes from this class have only been found in a few bacterial species.It is a hexamer of identical chains. It is much larger (about 700 amino acids) than the GSI (450 to 470 amino acids) or GSII (350 to 420 amino acids) enzymes <ref name="Brown"/><br /> <br /> <br /> [[Image:Glutamine-synthesis.jpg|thumb | Figure 2: Two step process of sythesis of glutamine from glutamate, synthesised by glutamine synthesis.]]<br /> <br /> ==Function==<br /> <br /> Glutamine synthetase (GS) is an essential enzyme in the cellular nitrogen metabolism and has been found to play a role in both ammonia assimilation and glutamine byosynthesis.<ref name="Kumada"/> It is the only enzyme capable of glutamine synthesis and is required for the two step process synthesizing glutamate to glutamine. The glutamine produced is an essential precursor for purine and pyrimidine synthesis, a modulator of protein turnover or an intermediate for gluconeogenesis and acid-base balance. <ref>He,Youji, Hakvoort,Theodorus, B.M., Kohler,S.Eleonor, Vermeulen,Jacqueline L.M.,Rudi de Waart, D., Theije,Chiel de, Gabrie A.M. ten Have, Van Eijk,Hans M.H., Kunne,Cindy, Labruyere,Wilelmina T., Houten,Sander M., Sokolovic,Mika, Tuijter,Jan M., Deutz,Nicolaas E.P., and Lamers, Wouter H. Glutamine Synthetase in muscle is required for glutamine production druing fasting and extrahepatic ammonia detoxification. The American Society for Biochemistry and Molecular Biology, January 11, 2010 </ref><br /> <br /> <br /> ==References==<br /> <references/><br /> <br /> <table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr><br /> Rhiannon Khela</div>

Rhiannon Khela https://proteopedia.org/index.php?title=Glutamine_synthetase&diff=1064588 Glutamine synthetase 2010-03-31T22:58:39Z

<p>Rhiannon Khela: </p> <hr /> <div>=''' Glutamine Synthetase '''=<br /> <br /> <br /> <br /> ==Structure==<br /> {{STRUCTURE_2gls| PDB=2gls | SCENE=Sandbox_169/2gls/1 }}<br /> An unrefined structure of glutamine synthetase is made of two layers, each containing 6 subunits, for a total of 12 subunits. <ref name="Yamashita">PMID:2572586 </ref> Each subunit contains an <scene name='Sandbox_169/Mn_in_the_active_site/2'>active site </scene>which is defined by a cylindrical shape formed by six antiparalel β starnds contributed by one subunit and two more strands by the neighbouring subunit. <ref name="Yamashita"/> In each cylindrical active site there are two Mn2+ ions: Mn 2+ 469 and 470. Both are attached to three protein chains and two water molecules, one of the water molecules are shared by both Mn2+. The protein ligands. Attached to Mn 2+ 469 is: Glu-131, GLu-212 and Glu-220, and the protein ligands attached to Mn 2+ are: Glu-129, His-269 and Glu-357.<ref name="Yamashita"/> <br /> <br /> Unique to glutamine synthetase, unlike other enzymes, is it's "passive site". This refers to the central loop which is formed by a segment of the backbone that extends into the central aqueous cavity. <ref name="Yamashita"/>Unlike other sites in glutamine synthetase under the same conditions, this site is suceptible to proteolysis by four secreated proteases from the V8 protease of ''Staphylococcus aureus''.<ref name="Yamashita"/><br /> <br /> [[Image:Passive site.png |left||thumb|Figure 1: A clear view of glutamine synthetases "passive site".]]<br /> <br /> <br /> <br /> ==Classes==<br /> <br /> Glutamine synthetase has been described as having three destinctive types:<ref name="Brown">PMID:7916055 </ref><br /> *Class I (GSI): Genes for this class have only been found in bacteria (eubacteria) and archaea (arhaebacteria. The paper by Kumada ''et. al'' goes into detail on these two.<ref name="Kumada">PMID:8096645 </ref><br /> *Class II (GSII): Genes for this class have only been found in eukaryotes and a few soil-dwelling bacteria.The paper by .... gets into further detail about these bacteria. :<ref>PMID:7916055 </ref><br /> *Class III (GSIII): Genes from this class have only been found in a few bacterial species.It is a hexamer of identical chains. It is much larger (about 700 amino acids) than the GSI (450 to 470 amino acids) or GSII (350 to 420 amino acids) enzymes <ref name="Brown"/>. <br /> <br /> <br /> [[Image:Glutamine-synthesis.jpg|thumb | Figure 2: Two step process of sythesis of glutamine from glutamate, synthesised by glutamine synthesis.]]<br /> <br /> ==Function==<br /> <br /> Glutamine synthetase (GS) is an essential enzyme in the cellular nitrogen metabolism and has been found to play a role in both ammonia assimilation and glutamine byosynthesis.<ref name="Kumada"/> It is the only enzyme capable of glutamine synthesis and is required for the two step process synthesizing glutamate to glutamine. The glutamine produced is an essential precursor for purine and pyrimidine synthesis, a modulator of protein turnover or an intermediate for gluconeogenesis and acid-base balance. <ref>He,Youji, Hakvoort,Theodorus, B.M., Kohler,S.Eleonor, Vermeulen,Jacqueline L.M.,Rudi de Waart, D., Theije,Chiel de, Gabrie A.M. ten Have, Van Eijk,Hans M.H., Kunne,Cindy, Labruyere,Wilelmina T., Houten,Sander M., Sokolovic,Mika, Tuijter,Jan M., Deutz,Nicolaas E.P., and Lamers, Wouter H. Glutamine Synthetase in muscle is required for glutamine production druing fasting and extrahepatic ammonia detoxification. The American Society for Biochemistry and Molecular Biology, January 11, 2010 </ref><br /> <br /> <br /> ==References==<br /> <references/><br /> <br /> <table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr><br /> Rhiannon Khela</div>

Rhiannon Khela https://proteopedia.org/index.php?title=Glutamine_synthetase&diff=1064586 Glutamine synthetase 2010-03-31T22:57:48Z

<p>Rhiannon Khela: </p> <hr /> <div>=''' Glutamine Synthetase '''=<br /> <br /> <br /> <br /> ==Structure==<br /> {{STRUCTURE_2gls| PDB=2gls | SCENE=Sandbox_169/2gls/1 }}<br /> An unrefined structure of glutamine synthetase is made of two layers, each containing 6 subunits, for a total of 12 subunits. <ref name="Yamashita">PMID:2572586 </ref> Each subunit contains an <scene name='Sandbox_169/Mn_in_the_active_site/2'>active site </scene>which is defined by a cylindrical shape formed by six antiparalel β starnds contributed by one subunit and two more strands by the neighbouring subunit. <ref name="Yamashita"/> In each cylindrical active site there are two Mn2+ ions: Mn 2+ 469 and 470. Both are attached to three protein chains and two water molecules, one of the water molecules are shared by both Mn2+. The protein ligands. Attached to Mn 2+ 469 is: Glu-131, GLu-212 and Glu-220, and the protein ligands attached to Mn 2+ are: Glu-129, His-269 and Glu-357.<ref name="Yamashita"/> <br /> <br /> Unique to glutamine synthetase, unlike other enzymes, is it's "passive site". This refers to the central loop which is formed by a segment of the backbone that extends into the central aqueous cavity. <ref name="Yamashita"/>Unlike other sites in glutamine synthetase under the same conditions, this site is suceptible to proteolysis by four secreated proteases from the V8 protease of ''Staphylococcus aureus''.<ref name="Yamashita"/> [[Image:Passive site.png |left||thumb|Figure 1: A clear view of glutamine synthetases "passive site".]]<br /> <br /> <br /> <br /> ==Classes==<br /> <br /> Glutamine synthetase has been described as having three destinctive types:<ref name="Brown">PMID:7916055 </ref><br /> *Class I (GSI): Genes for this class have only been found in bacteria (eubacteria) and archaea (arhaebacteria. The paper by Kumada ''et. al'' goes into detail on these two.<ref name="Kumada">PMID:8096645 </ref><br /> *Class II (GSII): Genes for this class have only been found in eukaryotes and a few soil-dwelling bacteria.The paper by .... gets into further detail about these bacteria. :<ref>PMID:7916055 </ref><br /> *Class III (GSIII): Genes from this class have only been found in a few bacterial species.It is a hexamer of identical chains. It is much larger (about 700 amino acids) than the GSI (450 to 470 amino acids) or GSII (350 to 420 amino acids) enzymes <ref name="Brown"/>. <br /> <br /> <br /> [[Image:Glutamine-synthesis.jpg|thumb | Figure 2: Two step process of sythesis of glutamine from glutamate, synthesised by glutamine synthesis.]]<br /> <br /> ==Function==<br /> <br /> Glutamine synthetase (GS) is an essential enzyme in the cellular nitrogen metabolism and has been found to play a role in both ammonia assimilation and glutamine byosynthesis.<ref name="Kumada"/> It is the only enzyme capable of glutamine synthesis and is required for the two step process synthesizing glutamate to glutamine. The glutamine produced is an essential precursor for purine and pyrimidine synthesis, a modulator of protein turnover or an intermediate for gluconeogenesis and acid-base balance. <ref>He,Youji, Hakvoort,Theodorus, B.M., Kohler,S.Eleonor, Vermeulen,Jacqueline L.M.,Rudi de Waart, D., Theije,Chiel de, Gabrie A.M. ten Have, Van Eijk,Hans M.H., Kunne,Cindy, Labruyere,Wilelmina T., Houten,Sander M., Sokolovic,Mika, Tuijter,Jan M., Deutz,Nicolaas E.P., and Lamers, Wouter H. Glutamine Synthetase in muscle is required for glutamine production druing fasting and extrahepatic ammonia detoxification. The American Society for Biochemistry and Molecular Biology, January 11, 2010 </ref><br /> <br /> <br /> ==References==<br /> <references/><br /> <br /> <table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr><br /> Rhiannon Khela</div>

Rhiannon Khela https://proteopedia.org/index.php?title=Glutamine_synthetase&diff=1064577 Glutamine synthetase 2010-03-31T22:41:02Z

<p>Rhiannon Khela: </p> <hr /> <div>=''' Glutamine Synthetase '''=<br /> <br /> <br /> <br /> ==Structure==<br /> <br /> An unrefined structure of glutamine synthetase is made of two layers, each containing 6 subunits, for a total of 12 subunits. <ref name="Yamashita">PMID:2572586 </ref> Each subunit contains an <scene name='Sandbox_169/Mn_in_the_active_site/2'>active site </scene>which is defined by a cylindrical shape formed by six antiparalel β starnds contributed by one subunit and two more strands by the neighbouring subunit. <ref name="Yamashita"/> In each cylindrical active site there are two Mn2+ ions: Mn 2+ 469 and 470. Both are attached to three protein chains and two water molecules, one of the water molecules are shared by both Mn2+. The protein ligands. Attached to Mn 2+ 469 is: Glu-131, GLu-212 and Glu-220, and the protein ligands attached to Mn 2+ are: Glu-129, His-269 and Glu-357.<ref name="Yamashita"/> <br /> <br /> Unique to glutamine synthetase, unlike other enzymes, is it's "passive site". This refers to the central loop which is formed by a segment of the backbone that extends into the central aqueous cavity. <ref name="Yamashita"/>Unlike other sites in glutamine synthetase under the same conditions, this site is suceptible to proteolysis by four secreated proteases from the V8 protease of ''Staphylococcus aureus''.<ref name="Yamashita"/>[[Image:Passive site.png|thumb|Figure 1: A clear view of glutamine synthetases "passive site".]]<br /> <br /> {{STRUCTURE_2gls| PDB=2gls | SCENE=Sandbox_169/2gls/1 }}<br /> <br /> ==Classes==<br /> <br /> Glutamine synthetase has been described as having three destinctive types:<ref name="Brown">PMID:7916055 </ref><br /> *Class I (GSI): Genes for this class have only been found in bacteria (eubacteria) and archaea (arhaebacteria. The paper by Kumada ''et. al'' goes into detail on these two.<ref name="Kumada">PMID:8096645 </ref><br /> *Class II (GSII): Genes for this class have only been found in eukaryotes and a few soil-dwelling bacteria.The paper by .... gets into further detail about these bacteria. :<ref>PMID:7916055 </ref><br /> *Class III (GSIII): Genes from this class have only been found in a few bacterial species.It is a hexamer of identical chains. It is much larger (about 700 amino acids) than the GSI (450 to 470 amino acids) or GSII (350 to 420 amino acids) enzymes <ref name="Brown">. <br /> <br /> <br /> ==Function==<br /> Glutamine synthetase (GS) is an essential enzyme in the cellular nitrogen metabolism and has been found to play a role in both ammonia assimilation and glutamine byosynthesis.<ref name="Kumada"/> It is the only enzyme capable of glutamine synthesis and is required for the two step process synthesizing glutamate to glutamine. The glutamine produced is an essential precursor for purine and pyrimidine synthesis, a modulator of protein turnover or an intermediate for gluconeogenesis and acid-base balance. <ref>He,Youji, Hakvoort,Theodorus, B.M., Kohler,S.Eleonor, Vermeulen,Jacqueline L.M.,Rudi de Waart, D., Theije,Chiel de, Gabrie A.M. ten Have, Van Eijk,Hans M.H., Kunne,Cindy, Labruyere,Wilelmina T., Houten,Sander M., Sokolovic,Mika, Tuijter,Jan M., Deutz,Nicolaas E.P., and Lamers, Wouter H. Glutamine Synthetase in muscle is required for glutamine production druing fasting and extrahepatic ammonia detoxification. The American Society for Biochemistry and Molecular Biology, January 11, 2010 </ref><br /> <br /> [[Image:Glutamine-synthesis.jpg|thumb|Figure 2: Two step process of sythesis of glutamine from glutamate, synthesised by glutamine synthesis.]]<br /> <br /> ==References==<br /> <references/><br /> <br /> <table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr><br /> Rhiannon Khela</div>

Rhiannon Khela https://proteopedia.org/index.php?title=Glutamine_synthetase&diff=1064574 Glutamine synthetase 2010-03-31T22:38:49Z

<p>Rhiannon Khela: </p> <hr /> <div>=''' Glutamine Synthetase '''=<br /> <br /> <br /> <br /> ==Structure==<br /> <br /> An unrefined structure of glutamine synthetase is made of two layers, each containing 6 subunits, for a total of 12 subunits. <ref name="Yamashita">PMID:2572586 </ref> Each subunit contains an <scene name='Sandbox_169/Mn_in_the_active_site/2'>active site </scene>which is defined by a cylindrical shape formed by six antiparalel β starnds contributed by one subunit and two more strands by the neighbouring subunit. <ref name="Yamashita"/> In each cylindrical active site there are two Mn2+ ions: Mn 2+ 469 and 470. Both are attached to three protein chains and two water molecules, one of the water molecules are shared by both Mn2+. The protein ligands. Attached to Mn 2+ 469 is: Glu-131, GLu-212 and Glu-220, and the protein ligands attached to Mn 2+ are: Glu-129, His-269 and Glu-357.<ref name="Yamashita"/> <br /> <br /> Unique to glutamine synthetase, unlike other enzymes, is it's "passive site". This refers to the central loop which is formed by a segment of the backbone that extends into the central aqueous cavity. <ref name="Yamashita"/>Unlike other sites in glutamine synthetase under the same conditions, this site is suceptible to proteolysis by four secreated proteases from the V8 protease of ''Staphylococcus aureus''.<ref name="Yamashita"/>[[Image:Passive site.png|thumb|Figure 1: A clear view of glutamine synthetases "passive site".]]<br /> <br /> {{STRUCTURE_2gls| PDB=2gls | SCENE=Sandbox_169/2gls/1 }}<br /> <br /> ==Classes==<br /> <br /> Glutamine synthetase has been described as having three destinctive types.<ref name="Kumada">PMID:7916055 </ref><br /> *Class I (GSI): Genes for this class have only been found in bacteria (eubacteria) and archaea (arhaebacteria. The paper by Kumada ''et. al'' goes into detail on these two.<ref name="Kumada">PMID:8096645 </ref><br /> *Class II (GSII): Genes for this class have only been found in eukaryotes and a few soil-dwelling bacteria.The paper by Kumada again, gets into further detail about these bacteria.<ref name="Kumada"><br /> *Class III (GSIII): Genes from this class have only been found in a few bacterial species.It is a hexamer of identical chains. It is much larger (about 700 amino acids) than the GSI (450 to 470 amino acids) or GSII (350 to 420 amino acids) enzymes.<ref name="Brown">. <br /> <br /> <br /> ==Function==<br /> Glutamine synthetase (GS) is an essential enzyme in the cellular nitrogen metabolism and has been found to play a role in both ammonia assimilation and glutamine byosynthesis.<ref name="Kumada"/> It is the only enzyme capable of glutamine synthesis and is required for the two step process synthesizing glutamate to glutamine. The glutamine produced is an essential precursor for purine and pyrimidine synthesis, a modulator of protein turnover or an intermediate for gluconeogenesis and acid-base balance. <ref>He,Youji, Hakvoort,Theodorus, B.M., Kohler,S.Eleonor, Vermeulen,Jacqueline L.M.,Rudi de Waart, D., Theije,Chiel de, Gabrie A.M. ten Have, Van Eijk,Hans M.H., Kunne,Cindy, Labruyere,Wilelmina T., Houten,Sander M., Sokolovic,Mika, Tuijter,Jan M., Deutz,Nicolaas E.P., and Lamers, Wouter H. Glutamine Synthetase in muscle is required for glutamine production druing fasting and extrahepatic ammonia detoxification. The American Society for Biochemistry and Molecular Biology, January 11, 2010 </ref><br /> <br /> [[Image:Glutamine-synthesis.jpg|thumb|Figure 2: Two step process of sythesis of glutamine from glutamate, synthesised by glutamine synthesis.]]<br /> <br /> ==References==<br /> <references/><br /> <br /> <table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr><br /> Rhiannon Khela</div>

Rhiannon Khela https://proteopedia.org/index.php?title=Glutamine_synthetase&diff=1064572 Glutamine synthetase 2010-03-31T22:35:35Z

<p>Rhiannon Khela: </p> <hr /> <div>=''' Glutamine Synthetase '''=<br /> <br /> <br /> <br /> ==Structure==<br /> <br /> An unrefined structure of glutamine synthetase is made of two layers, each containing 6 subunits, for a total of 12 subunits. <ref name="Yamashita">PMID:2572586 </ref> Each subunit contains an <scene name='Sandbox_169/Mn_in_the_active_site/2'>active site </scene>which is defined by a cylindrical shape formed by six antiparalel β starnds contributed by one subunit and two more strands by the neighbouring subunit. <ref name="Yamashita"/> In each cylindrical active site there are two Mn2+ ions: Mn 2+ 469 and 470. Both are attached to three protein chains and two water molecules, one of the water molecules are shared by both Mn2+. The protein ligands. Attached to Mn 2+ 469 is: Glu-131, GLu-212 and Glu-220, and the protein ligands attached to Mn 2+ are: Glu-129, His-269 and Glu-357.<ref name="Yamashita"/> <br /> <br /> Unique to glutamine synthetase, unlike other enzymes, is it's "passive site". This refers to the central loop which is formed by a segment of the backbone that extends into the central aqueous cavity. <ref name="Yamashita"/>Unlike other sites in glutamine synthetase under the same conditions, this site is suceptible to proteolysis by four secreated proteases from the V8 protease of ''Staphylococcus aureus''.<ref name="Yamashita"/>[[Image:Passive site.png|thumb|Figure 1: A clear view of glutamine synthetases "passive site".]]<br /> <br /> {{STRUCTURE_2gls| PDB=2gls | SCENE=Sandbox_169/2gls/1 }}<br /> <br /> ==Classes==<br /> <br /> Glutamine synthetase has been described as having three destinctive types:<ref>PMID:7916055 </ref><br /> *Class I (GSI): Genes for this class have only been found in bacteria (eubacteria) and archaea (arhaebacteria. The paper by Kumada ''et. al'' goes into detail on these two.<ref name="Kumada">PMID:8096645 </ref><br /> *Class II (GSII): Genes for this class have only been found in eukaryotes and a few soil-dwelling bacteria.The paper by Kumada again, gets into further detail about these bacteria.<ref name="Kumada"><br /> *Class III (GSIII): Genes from this class have only been found in a few bacterial species.It is a hexamer of identical chains. It is much larger (about 700 amino acids) than the GSI (450 to 470 amino acids) or GSII (350 to 420 amino acids) enzymes. The paper by Brown ''et. al.'' explains in more detail about the possible gene transfer of GSI that may have occured, and how only a few bacterial species have been found to contain this GSIII gene. <ref>PMID:7916055 </ref> <br /> <br /> <br /> ==Function==<br /> Glutamine synthetase (GS) is an essential enzyme in the cellular nitrogen metabolism and has been found to play a role in both ammonia assimilation and glutamine byosynthesis.<ref name="Kumada"/> It is the only enzyme capable of glutamine synthesis and is required for the two step process synthesizing glutamate to glutamine. The glutamine produced is an essential precursor for purine and pyrimidine synthesis, a modulator of protein turnover or an intermediate for gluconeogenesis and acid-base balance. <ref>He,Youji, Hakvoort,Theodorus, B.M., Kohler,S.Eleonor, Vermeulen,Jacqueline L.M.,Rudi de Waart, D., Theije,Chiel de, Gabrie A.M. ten Have, Van Eijk,Hans M.H., Kunne,Cindy, Labruyere,Wilelmina T., Houten,Sander M., Sokolovic,Mika, Tuijter,Jan M., Deutz,Nicolaas E.P., and Lamers, Wouter H. Glutamine Synthetase in muscle is required for glutamine production druing fasting and extrahepatic ammonia detoxification. The American Society for Biochemistry and Molecular Biology, January 11, 2010 </ref><br /> <br /> [[Image:Glutamine-synthesis.jpg|thumb|Figure 2: Two step process of sythesis of glutamine from glutamate, synthesised by glutamine synthesis.]]<br /> <br /> ==References==<br /> <references/><br /> <br /> <table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr><br /> Rhiannon Khela</div>

Rhiannon Khela https://proteopedia.org/index.php?title=Glutamine_synthetase&diff=1064571 Glutamine synthetase 2010-03-31T22:26:19Z

<p>Rhiannon Khela: </p> <hr /> <div>=''' Glutamine Synthetase '''=<br /> <br /> <br /> <br /> ==Structure==<br /> <br /> An unrefined structure of glutamine synthetase is made of two layers, each containing 6 subunits, for a total of 12 subunits. <ref name="Yamashita">PMID:2572586 </ref> Each subunit contains an <scene name='Sandbox_169/Mn_in_the_active_site/2'>active site </scene>which is defined by a cylindrical shape formed by six antiparalel β starnds contributed by one subunit and two more strands by the neighbouring subunit. <ref name="Yamashita"/> In each cylindrical active site there are two Mn2+ ions: Mn 2+ 469 and 470. Both are attached to three protein chains and two water molecules, one of the water molecules are shared by both Mn2+. The protein ligands. Attached to Mn 2+ 469 is: Glu-131, GLu-212 and Glu-220, and the protein ligands attached to Mn 2+ are: Glu-129, His-269 and Glu-357.<ref name="Yamashita"/> <br /> <br /> Unique to glutamine synthetase, unlike other enzymes, is it's "passive site". This refers to the central loop which is formed by a segment of the backbone that extends into the central aqueous cavity. <ref name="Yamashita"/>Unlike other sites in glutamine synthetase under the same conditions, this site is suceptible to proteolysis by four secreated proteases from the V8 protease of ''Staphylococcus aureus''.<ref name="Yamashita"/>[[Image:Passive site.png|thumb|Figure 1: A clear view of glutamine synthetases "passive site".]]<br /> <br /> {{STRUCTURE_2gls| PDB=2gls | SCENE=Sandbox_169/2gls/1 }}<br /> <br /> ==Classes==<br /> <br /> Glutamine synthetase has been described as having three destinctive types:<ref>PMID:7916055 </ref><br /> *Class I (GSI): Genes for this class have only been found in bacteria (eubacteria) and archaea (arhaebacteria. The paper by Kumada ''et. al'' goes into detail on these two.<ref name="Kumada">PMID:8096645 </ref><br /> *Class II (GSII): Genes for this class have only been found in eukaryotes and a few soil-dwelling bacteria.The paper by .... gets into further detail about these bacteria. :<ref>PMID:7916055 </ref><br /> *Class III (GSIII): Genes from this class have only been found in a few bacterial species.It is a hexamer of identical chains. It is much larger (about 700 amino acids) than the GSI (450 to 470 amino acids) or GSII (350 to 420 amino acids) enzymes. <br /> <br /> <br /> ==Function==<br /> Glutamine synthetase (GS) is an essential enzyme in the cellular nitrogen metabolism and has been found to play a role in both ammonia assimilation and glutamine byosynthesis.<ref name="Kumada"/> It is the only enzyme capable of glutamine synthesis and is required for the two step process synthesizing glutamate to glutamine. The glutamine produced is an essential precursor for purine and pyrimidine synthesis, a modulator of protein turnover or an intermediate for gluconeogenesis and acid-base balance. <ref>He,Youji, Hakvoort,Theodorus, B.M., Kohler,S.Eleonor, Vermeulen,Jacqueline L.M.,Rudi de Waart, D., Theije,Chiel de, Gabrie A.M. ten Have, Van Eijk,Hans M.H., Kunne,Cindy, Labruyere,Wilelmina T., Houten,Sander M., Sokolovic,Mika, Tuijter,Jan M., Deutz,Nicolaas E.P., and Lamers, Wouter H. Glutamine Synthetase in muscle is required for glutamine production druing fasting and extrahepatic ammonia detoxification. The American Society for Biochemistry and Molecular Biology, January 11, 2010 </ref><br /> <br /> [[Image:Glutamine-synthesis.jpg|thumb|Figure 2: Two step process of sythesis of glutamine from glutamate, synthesised by glutamine synthesis.]]<br /> <br /> ==References==<br /> <references/><br /> <br /> <table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr><br /> Rhiannon Khela</div>

Rhiannon Khela https://proteopedia.org/index.php?title=Glutamine_synthetase&diff=1064568 Glutamine synthetase 2010-03-31T22:22:57Z

<p>Rhiannon Khela: </p> <hr /> <div>=''' Glutamine Synthetase '''=<br /> <br /> <br /> <br /> ==Structure==<br /> <br /> An unrefined structure of glutamine synthetase is made of two layers, each containing 6 subunits, for a total of 12 subunits. <ref name="Yamashita">PMID:2572586 </ref> Each subunit contains an <scene name='Sandbox_169/Mn_in_the_active_site/2'>active site </scene>which is defined by a cylindrical shape formed by six antiparalel β starnds contributed by one subunit and two more strands by the neighbouring subunit. <ref name="Yamashita"/> In each cylindrical active site there are two Mn2+ ions: Mn 2+ 469 and 470. Both are attached to three protein chains and two water molecules, one of the water molecules are shared by both Mn2+. The protein ligands. Attached to Mn 2+ 469 is: Glu-131, GLu-212 and Glu-220, and the protein ligands attached to Mn 2+ are: Glu-129, His-269 and Glu-357.<ref name="Yamashita"/> <br /> <br /> Unique to glutamine synthetase, unlike other enzymes, is it's "passive site". This refers to the central loop which is formed by a segment of the backbone that extends into the central aqueous cavity. <ref name="Yamashita"/>Unlike other sites in glutamine synthetase under the same conditions, this site is suceptible to proteolysis by four secreated proteases from the V8 protease of ''Staphylococcus aureus''.<ref name="Yamashita"/>[[Image:Passive site.png|thumb|Figure 1: A clear view of glutamine synthetases "passive site".]]<br /> <br /> {{STRUCTURE_2gls| PDB=2gls | SCENE=Sandbox_169/2gls/1 }}<br /> <br /> ==Classes==<br /> <br /> Glutamine synthetase has been described as having three destinctive types:<ref>PMID:7916055 </ref><br /> *Class I (GSI): Genes for this class have only been found in bacteria (eubacteria) and archaea (arhaebacteria. The paper by Kumada ''et. al'' goes into detail on these two.<ref name="Kumada">PMID:8096645 </ref><br /> *Class II (GSII): Genes for this class have only been found in eukaryotes and a few soil-dwelling bacteria.The paper by .... gets into further detail about these bacteria. :<ref>PMID:7916055 </ref><br /> *Class III (GSIII): Genes from this class have only been found in a few bacterial species.It is a hexamer of identical chains. It is much larger (about 700 amino acids) than the GSI (450 to 470 amino acids) or GSII (350 to 420 amino acids) enzymes. <br /> <br /> <br /> ==Function==<br /> Glutamine synthetase (GS) is an essential enzyme in the cellular nitrogen metabolism and has been found to play a role in both ammonia assimilation and glutamine byosynthesis.<ref name="Kumada"/> is the only enzyme capable of glutamine synthesis. The glutamine produced is an essential precursor for purine and pyrimidine synthesis, a modulator of protein turnover or an intermediate for gluconeogenesis and acid-base balance. <ref>He,Youji, Hakvoort,Theodorus, B.M., Kohler,S.Eleonor, Vermeulen,Jacqueline L.M.,Rudi de Waart, D., Theije,Chiel de, Gabrie A.M. ten Have, Van Eijk,Hans M.H., Kunne,Cindy, Labruyere,Wilelmina T., Houten,Sander M., Sokolovic,Mika, Tuijter,Jan M., Deutz,Nicolaas E.P., and Lamers, Wouter H. Glutamine Synthetase in muscle is required for glutamine production druing fasting and extrahepatic ammonia detoxification. The American Society for Biochemistry and Molecular Biology, January 11, 2010 </ref><br /> <br /> [[Image:Glutamine-synthesis.jpg|thumb|Figure 2: Two step process of sythesis of glutamine from glutamate, synthesised by glutamine synthesis.]]<br /> <br /> ==References==<br /> <references/><br /> <br /> <table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr><br /> Rhiannon Khela</div>

Rhiannon Khela https://proteopedia.org/index.php?title=Glutamine_synthetase&diff=1064567 Glutamine synthetase 2010-03-31T22:20:33Z

<p>Rhiannon Khela: </p> <hr /> <div>=''' Glutamine Synthetase '''=<br /> <br /> <br /> <br /> ==Structure==<br /> <br /> An unrefined structure of glutamine synthetase is made of two layers, each containing 6 subunits, for a total of 12 subunits. <ref name="Yamashita">PMID:2572586 </ref> Each subunit contains an <scene name='Sandbox_169/Mn_in_the_active_site/2'>active site </scene>which is defined by a cylindrical shape formed by six antiparalel β starnds contributed by one subunit and two more strands by the neighbouring subunit. <ref name="Yamashita"/> In each cylindrical active site there are two Mn2+ ions: Mn 2+ 469 and 470. Both are attached to three protein chains and two water molecules, one of the water molecules are shared by both Mn2+. The protein ligands. Attached to Mn 2+ 469 is: Glu-131, GLu-212 and Glu-220, and the protein ligands attached to Mn 2+ are: Glu-129, His-269 and Glu-357.<ref name="Yamashita"/> <br /> <br /> Unique to glutamine synthetase, unlike other enzymes, is it's "passive site". This refers to the central loop which is formed by a segment of the backbone that extends into the central aqueous cavity. <ref name="Yamashita"/>Unlike other sites in glutamine synthetase under the same conditions, this site is suceptible to proteolysis by four secreated proteases from the V8 protease of ''Staphylococcus aureus''.<ref name="Yamashita"/>[[Image:Passive site.png|thumb|Figure 1: A clear view of glutamine synthetases "passive site".]]<br /> <br /> {{STRUCTURE_2gls| PDB=2gls | SCENE=Sandbox_169/2gls/1 }}<br /> <br /> ==Classes==<br /> <br /> Glutamine synthetase has been described as having three destinctive types:<ref>PMID:7916055 </ref><br /> *Class I (GSI): Genes for this class have only been found in bacteria (eubacteria) and archaea (arhaebacteria. The paper by Kumada ''et. al'' goes into detail on these two.<ref name="Kumada">PMID:8096645 </ref><br /> *Class II (GSII): Genes for this class have only been found in eukaryotes anda few soil-dwelling bacteria. <br /> *Class III (GSIII): Genes from this class have only been found in a few bacterial species.It is a hexamer of identical chains. It is much larger (about 700 amino acids) than the GSI (450 to 470 amino acids) or GSII (350 to 420 amino acids) enzymes. <br /> <br /> <br /> ==Function==<br /> Glutamine synthetase (GS) is an essential enzyme in the cellular nitrogen metabolism and has been found to play a role in both ammonia assimilation and glutamine byosynthesis.<ref name="Kumada"/> is the only enzyme capable of glutamine synthesis. The glutamine produced is an essential precursor for purine and pyrimidine synthesis, a modulator of protein turnover or an intermediate for gluconeogenesis and acid-base balance. <ref>He,Youji, Hakvoort,Theodorus, B.M., Kohler,S.Eleonor, Vermeulen,Jacqueline L.M.,Rudi de Waart, D., Theije,Chiel de, Gabrie A.M. ten Have, Van Eijk,Hans M.H., Kunne,Cindy, Labruyere,Wilelmina T., Houten,Sander M., Sokolovic,Mika, Tuijter,Jan M., Deutz,Nicolaas E.P., and Lamers, Wouter H. Glutamine Synthetase in muscle is required for glutamine production druing fasting and extrahepatic ammonia detoxification. The American Society for Biochemistry and Molecular Biology, January 11, 2010 </ref><br /> <br /> [[Image:Glutamine-synthesis.jpg|thumb|Figure 2: Two step process of sythesis of glutamine from glutamate, synthesised by glutamine synthesis.]]<br /> <br /> ==References==<br /> <references/><br /> <br /> <table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr><br /> Rhiannon Khela</div>

Rhiannon Khela https://proteopedia.org/index.php?title=Glutamine_synthetase&diff=1064563 Glutamine synthetase 2010-03-31T22:16:46Z

<p>Rhiannon Khela: </p> <hr /> <div>=''' Glutamine Synthetase '''=<br /> <br /> <br /> <br /> ==Structure==<br /> <br /> An unrefined structure of glutamine synthetase is made of two layers, each containing 6 subunits, for a total of 12 subunits. <ref name="Yamashita">PMID:2572586 </ref> Each subunit contains an <scene name='Sandbox_169/Mn_in_the_active_site/2'>active site </scene>which is defined by a cylindrical shape formed by six antiparalel β starnds contributed by one subunit and two more strands by the neighbouring subunit.<ref name="Yamashita"/> In each cylindrical active site there are two Mn2+ ions: Mn 2+ 469 and 470. Both are attached to three protein chains and two water molecules, one of the water molecules are shared by both Mn2+. The protein ligands. Attached to Mn 2+ 469 is: Glu-131, GLu-212 and Glu-220, and the protein ligands attached to Mn 2+ are: Glu-129, His-269 and Glu-357.<ref name="Yamashita"/> <br /> <br /> Unique to glutamine synthetase, unlike other enzymes, is it's "passive site". This refers to the central loop which is formed by a segment of the backbone that extends into the central aqueous cavity.(Ref1)Unlike other sites in glutamine synthetase under the same conditions, this site is suceptible to proteolysis by four secreated proteases from the V8 protease of ''Staphylococcus aureus''.<ref name="Yamashita"/>[[Image:Passive site.png|thumb|Figure 1: A clear view of glutamine synthetases "passive site".]]<br /> <br /> {{STRUCTURE_2gls| PDB=2gls | SCENE=Sandbox_169/2gls/1 }}<br /> <br /> ==Classes==<br /> <br /> Glutamine synthetase has been described as having three destinctive types:<ref>PMID:7916055 </ref><br /> *Class I (GSI): Genes for this class have only been found in bacteria (eubacteria) and archaea (arhaebacteria. The paper by Kumada 'et. al' goes into detail on these two.<ref name="Kumada">PMID:8096645 </ref><br /> *Class II (GSII): Genes for this class have only been found in eukaryotes anda few soil-dwelling bacteria. <br /> *Class III (GSIII): Genes from this class have only been found in a few bacterial species.It is a hexamer of identical chains. It is much larger (about 700 amino acids) than the GSI (450 to 470 amino acids) or GSII (350 to 420 amino acids) enzymes. <br /> <br /> <br /> ==Function==<br /> Glutamine synthetase (GS) is an essential enzyme in the cellular nitrogen metabolism and has been found to play a role in both ammonia assimilation and glutamine byosynthesis.<ref name="Kumada"/> is the only enzyme capable of glutamine synthesis. The glutamine produced is an essential precursor for purine and pyrimidine synthesis, a modulator of protein turnover or an intermediate for gluconeogenesis and acid-base balance. <ref>He,Youji, Hakvoort,Theodorus, B.M., Kohler,S.Eleonor, Vermeulen,Jacqueline L.M.,Rudi de Waart, D., Theije,Chiel de, Gabrie A.M. ten Have, Van Eijk,Hans M.H., Kunne,Cindy, Labruyere,Wilelmina T., Houten,Sander M., Sokolovic,Mika, Tuijter,Jan M., Deutz,Nicolaas E.P., and Lamers, Wouter H. Glutamine Synthetase in muscle is required for glutamine production druing fasting and extrahepatic ammonia detoxification. The American Society for Biochemistry and Molecular Biology, January 11, 2010 </ref><br /> <br /> [[Image:Glutamine-synthesis.jpg|thumb|Figure 2: Two step process of sythesis of glutamine from glutamate, synthesised by glutamine synthesis.]]<br /> <br /> ==References==<br /> <references/><br /> <br /> <table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr><br /> Rhiannon Khela</div>

Rhiannon Khela https://proteopedia.org/index.php?title=Glutamine_synthetase&diff=1064562 Glutamine synthetase 2010-03-31T22:15:32Z

<p>Rhiannon Khela: </p> <hr /> <div>=''' Glutamine Synthetase '''=<br /> <br /> <br /> <br /> ==Structure==<br /> <br /> An unrefined structure of glutamine synthetase is made of two layers, each containing 6 subunits, for a total of 12 subunits. <ref name="Yamashita">PMID:2572586 </ref> Each subunit contains an <scene name='Sandbox_169/Mn_in_the_active_site/2'>active site </scene>which is defined by a cylindrical shape formed by six antiparalel β starnds contributed by one subunit and two more strands by the neighbouring subunit.<ref name="Yamashita"/> In each cylindrical active site there are two Mn2+ ions: Mn 2+ 469 and 470. Both are attached to three protein chains and two water molecules, one of the water molecules are shared by both Mn2+. The protein ligands. Attached to Mn 2+ 469 is: Glu-131, GLu-212 and Glu-220, and the protein ligands attached to Mn 2+ are: Glu-129, His-269 and Glu-357.<ref name="Yamashita"/> <br /> <br /> Unique to glutamine synthetase, unlike other enzymes, is it's "passive site". This refers to the central loop which is formed by a segment of the backbone that extends into the central aqueous cavity.(Ref1)Unlike other sites in glutamine synthetase under the same conditions, this site is suceptible to proteolysis by four secreated proteases from the V8 protease of ''Staphylococcus aureus''.<ref name="Yamashita"/>[[Image:Passive site.png|thumb|Figure 1: A clear view of glutamine synthetases "passive site".]]<br /> <br /> {{STRUCTURE_2gls| PDB=2gls | SCENE=Sandbox_169/2gls/1 }}<br /> <br /> ==Classes==<br /> <br /> Glutamine synthetase has been described as having three destinctive types:<ref>PMID:7916055 </ref><br /> *Class I (GSI): Genes for this class have only been found in bacteria (eubacteria) and archaea (arhaebacteria. The paper by Kumada "et. al" goes into detail on these two..<ref name="Kumada">PMID:8096645 </ref><br /> *Class II (GSII): Genes for this class have only been found in eukaryotes anda few soil-dwelling bacteria. <br /> *Class III (GSIII): Genes from this class have only been found in a few bacterial species.It is a hexamer of identical chains. It is much larger (about 700 amino acids) than the GSI (450 to 470 amino acids) or GSII (350 to 420 amino acids) enzymes. <br /> <br /> <br /> ==Function==<br /> Glutamine synthetase (GS) is an essential enzyme in the cellular nitrogen metabolism and has been found to play a role in both ammonia assimilation and glutamine byosynthesis.<ref name="Kumada"/> is the only enzyme capable of glutamine synthesis. The glutamine produced is an essential precursor for purine and pyrimidine synthesis, a modulator of protein turnover or an intermediate for gluconeogenesis and acid-base balance. <ref>He,Youji, Hakvoort,Theodorus, B.M., Kohler,S.Eleonor, Vermeulen,Jacqueline L.M.,Rudi de Waart, D., Theije,Chiel de, Gabrie A.M. ten Have, Van Eijk,Hans M.H., Kunne,Cindy, Labruyere,Wilelmina T., Houten,Sander M., Sokolovic,Mika, Tuijter,Jan M., Deutz,Nicolaas E.P., and Lamers, Wouter H. Glutamine Synthetase in muscle is required for glutamine production druing fasting and extrahepatic ammonia detoxification. The American Society for Biochemistry and Molecular Biology, January 11, 2010 </ref><br /> <br /> [[Image:Glutamine-synthesis.jpg|thumb|Figure 2: Two step process of sythesis of glutamine from glutamate, synthesised by glutamine synthesis.]]<br /> <br /> ==References==<br /> <references/><br /> <br /> <table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr><br /> Rhiannon Khela</div>

Rhiannon Khela https://proteopedia.org/index.php?title=Glutamine_synthetase&diff=1064559 Glutamine synthetase 2010-03-31T22:03:42Z

<p>Rhiannon Khela: </p> <hr /> <div>=''' Glutamine Synthetase '''=<br /> <br /> <br /> <br /> ==Structure==<br /> <br /> An unrefined structure of glutamine synthetase is made of two layers, each containing 6 subunits, for a total of 12 subunits. <ref name="Yamashita">PMID:2572586 </ref> Each subunit contains an <scene name='Sandbox_169/Mn_in_the_active_site/2'>active site </scene>which is defined by a cylindrical shape formed by six antiparalel β starnds contributed by one subunit and two more strands by the neighbouring subunit.<ref name="Yamashita"/> In each cylindrical active site there are two Mn2+ ions: Mn 2+ 469 and 470. Both are attached to three protein chains and two water molecules, one of the water molecules are shared by both Mn2+. The protein ligands. Attached to Mn 2+ 469 is: Glu-131, GLu-212 and Glu-220, and the protein ligands attached to Mn 2+ are: Glu-129, His-269 and Glu-357.<ref name="Yamashita"/> <br /> <br /> Unique to glutamine synthetase, unlike other enzymes, is it's "passive site". This refers to the central loop which is formed by a segment of the backbone that extends into the central aqueous cavity.(Ref1)Unlike other sites in glutamine synthetase under the same conditions, this site is suceptible to proteolysis by four secreated proteases from the V8 protease of ''Staphylococcus aureus''.<ref name="Yamashita"/><br /> <br /> [[Image:Passive site.png|thumb|Figure 1: A clear view of glutamine synthetases "passive site".]]<br /> <br /> {{STRUCTURE_2gls| PDB=2gls | SCENE=Sandbox_169/2gls/1 }}<br /> <br /> ==Classes==<br /> <br /> Glutamine synthetase has been described as having three destinctive types:<ref>PMID:7916055 </ref><br /> *Class I (GSI): Genes for this class have only been found in bacteria (eubacteria) and archaea (arhaebacteria)<br /> *Class II (GSII): Genes for this class have only been found in eukaryotes anda few soil-dwelling bacteria. <br /> *Class III (GSIII): Genes from this class have only been found in a few bacterial species.It is a hexamer of identical chains. It is much larger (about 700 amino acids) than the GSI (450 to 470 amino acids) or GSII (350 to 420 amino acids) enzymes. <br /> <br /> <br /> ==Function==<br /> Glutamine synthetase (GS) is an essential enzyme in the cellular nitrogen metabolism and has been found to play a role in both ammonia assimilation and glutamine byosynthesis.<ref name="Kumada">PMID:8096645 </ref> GS is the only enzyme capable of glutamine synthesis. The glutamine produced is an essential precursor for purine and pyrimidine synthesis, a modulator of protein turnover or an intermediate for gluconeogenesis and acid-base balance. <ref>He,Youji, Hakvoort,Theodorus, B.M., Kohler,S.Eleonor, Vermeulen,Jacqueline L.M.,Rudi de Waart, D., Theije,Chiel de, Gabrie A.M. ten Have, Van Eijk,Hans M.H., Kunne,Cindy, Labruyere,Wilelmina T., Houten,Sander M., Sokolovic,Mika, Tuijter,Jan M., Deutz,Nicolaas E.P., and Lamers, Wouter H. Glutamine Synthetase in muscle is required for glutamine production druing fasting and extrahepatic ammonia detoxification. The American Society for Biochemistry and Molecular Biology, January 11, 2010 </ref><br /> <br /> [[Image:Glutamine-synthesis.jpg|thumb|Figure 2: Two step process of sythesis of glutamine from glutamate, synthesised by glutamine synthesis.]]<br /> <br /> ==References==<br /> <references/><br /> <br /> <table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr><br /> Rhiannon Khela</div>

Rhiannon Khela https://proteopedia.org/index.php?title=Glutamine_synthetase&diff=1064558 Glutamine synthetase 2010-03-31T22:02:20Z

<p>Rhiannon Khela: </p> <hr /> <div>=''' Glutamine Synthetase '''=<br /> <br /> <br /> <br /> ==Structure==<br /> <br /> An unrefined structure of glutamine synthetase is made of two layers, each containing 6 subunits, for a total of 12 subunits. <ref name="Yamashita">PMID:2572586 </ref> Each subunit contains an <scene name='Sandbox_169/Mn_in_the_active_site/2'>active site </scene>which is defined by a cylindrical shape formed by six antiparalel β starnds contributed by one subunit and two more strands by the neighbouring subunit.<ref name="Yamashita"/> In each cylindrical active site there are two Mn2+ ions: Mn 2+ 469 and 470. Both are attached to three protein chains and two water molecules, one of the water molecules are shared by both Mn2+. The protein ligands. Attached to Mn 2+ 469 is: Glu-131, GLu-212 and Glu-220, and the protein ligands attached to Mn 2+ are: Glu-129, His-269 and Glu-357.<ref name="Yamashita"/> <br /> <br /> Unique to glutamine synthetase, unlike other enzymes, is it's "passive site". This refers to the central loop which is formed by a segment of the backbone that extends into the central aqueous cavity.(Ref1)Unlike other sites in glutamine synthetase under the same conditions, this site is suceptible to proteolysis by four secreated proteases from the V8 protease of ''Staphylococcus aureus''.<ref name="Yamashita"/><br /> <br /> [[Image:Passive site.png|thumb|Figure 1: A clear view of glutamine synthetases "passive site".]]<br /> <br /> {{STRUCTURE_2gls| PDB=2gls | SCENE=Sandbox_169/2gls/1 }}<br /> <br /> ==Classes==<br /> <br /> Glutamine synthetase has been described as having three destinctive types:<ref>PMID:7916055 </ref> [[Image:2gls120.png]]<br /> *Class I (GSI): Genes for this class have only been found in bacteria (eubacteria) and archaea (arhaebacteria)<br /> *Class II (GSII): Genes for this class have only been found in eukaryotes anda few soil-dwelling bacteria. <br /> *Class III (GSIII): Genes from this class have only been found in a few bacterial species.It is a hexamer of identical chains. It is much larger (about 700 amino acids) than the GSI (450 to 470 amino acids) or GSII (350 to 420 amino acids) enzymes. <br /> <br /> <br /> ==Function==<br /> Glutamine synthetase (GS) is an essential enzyme in the cellular nitrogen metabolism and has been found to play a role in both ammonia assimilation and glutamine byosynthesis.<ref name="Kumada">PMID:8096645 </ref> GS is the only enzyme capable of glutamine synthesis. The glutamine produced is an essential precursor for purine and pyrimidine synthesis, a modulator of protein turnover or an intermediate for gluconeogenesis and acid-base balance. <ref>He,Youji, Hakvoort,Theodorus, B.M., Kohler,S.Eleonor, Vermeulen,Jacqueline L.M.,Rudi de Waart, D., Theije,Chiel de, Gabrie A.M. ten Have, Van Eijk,Hans M.H., Kunne,Cindy, Labruyere,Wilelmina T., Houten,Sander M., Sokolovic,Mika, Tuijter,Jan M., Deutz,Nicolaas E.P., and Lamers, Wouter H. Glutamine Synthetase in muscle is required for glutamine production druing fasting and extrahepatic ammonia detoxification. The American Society for Biochemistry and Molecular Biology, January 11, 2010 </ref><br /> <br /> [[Image:Glutamine-synthesis.jpg|thumb|Figure 2: Two step process of sythesis of glutamine from glutamate, synthesised by glutamine synthesis.]]<br /> <br /> ==References==<br /> <references/><br /> <br /> <table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr><br /> Rhiannon Khela</div>

Rhiannon Khela https://proteopedia.org/index.php?title=Glutamine_synthetase&diff=1064557 Glutamine synthetase 2010-03-31T21:58:40Z

<p>Rhiannon Khela: </p> <hr /> <div>=''' Glutamine Synthetase '''=<br /> <br /> <br /> <br /> ==Structure==<br /> <br /> An unrefined structure of glutamine synthetase is made of two layers, each containing 6 subunits, for a total of 12 subunits. <ref name="Yamashita">PMID:2572586 </ref> Each subunit contains an <scene name='Sandbox_169/Mn_in_the_active_site/2'>active site </scene>which is defined by a cylindrical shape formed by six antiparalel β starnds contributed by one subunit and two more strands by the neighbouring subunit.<ref name="Yamashita"/> In each cylindrical active site there are two Mn2+ ions: Mn 2+ 469 and 470. Both are attached to three protein chains and two water molecules, one of the water molecules are shared by both Mn2+. The protein ligands. Attached to Mn 2+ 469 is: Glu-131, GLu-212 and Glu-220, and the protein ligands attached to Mn 2+ are: Glu-129, His-269 and Glu-357.<ref name="Yamashita"/> <br /> <br /> Unique to glutamine synthetase, unlike other enzymes, is it's "passive site". This refers to the central loop which is formed by a segment of the backbone that extends into the central aqueous cavity.(Ref1)Unlike other sites in glutamine synthetase under the same conditions, this site is suceptible to proteolysis by four secreated proteases from the V8 protease of ''Staphylococcus aureus''.<ref name="Yamashita"/><br /> <br /> [[Image:Passive site.png|thumb|Figure 1: A clear view of glutamine synthetases "passive site".]]<br /> <br /> ==Classes==<br /> <br /> Glutamine synthetase has been described as having three destinctive types:<ref>PMID:7916055 </ref> [[Image:2gls120.png]]<br /> *Class I (GSI): Genes for this class have only been found in bacteria (eubacteria) and archaea (arhaebacteria)<br /> *Class II (GSII): Genes for this class have only been found in eukaryotes anda few soil-dwelling bacteria. <br /> *Class III (GSIII): Genes from this class have only been found in a few bacterial species.It is a hexamer of identical chains. It is much larger (about 700 amino acids) than the GSI (450 to 470 amino acids) or GSII (350 to 420 amino acids) enzymes. <br /> <br /> <br /> ==Function==<br /> Glutamine synthetase (GS) is an essential enzyme in the cellular nitrogen metabolism and has been found to play a role in both ammonia assimilation and glutamine byosynthesis.<ref name="Kumada">PMID:8096645 </ref> GS is the only enzyme capable of glutamine synthesis. The glutamine produced is an essential precursor for purine and pyrimidine synthesis, a modulator of protein turnover or an intermediate for gluconeogenesis and acid-base balance. <ref>He,Youji, Hakvoort,Theodorus, B.M., Kohler,S.Eleonor, Vermeulen,Jacqueline L.M.,Rudi de Waart, D., Theije,Chiel de, Gabrie A.M. ten Have, Van Eijk,Hans M.H., Kunne,Cindy, Labruyere,Wilelmina T., Houten,Sander M., Sokolovic,Mika, Tuijter,Jan M., Deutz,Nicolaas E.P., and Lamers, Wouter H. Glutamine Synthetase in muscle is required for glutamine production druing fasting and extrahepatic ammonia detoxification. The American Society for Biochemistry and Molecular Biology, January 11, 2010 </ref><br /> <br /> [[Image:Glutamine-synthesis.jpg|thumb|Figure 2: Two step process of sythesis of glutamine from glutamate, synthesised by glutamine synthesis.]]<br /> <br /> ==References==<br /> <references/><br /> <br /> <table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr><br /> Rhiannon Khela</div>

Rhiannon Khela https://proteopedia.org/index.php?title=File:Passive_site.png&diff=1064556 File:Passive site.png 2010-03-31T21:52:32Z

<p>Rhiannon Khela: </p> <hr /> <div></div>

Rhiannon Khela