Group:SMART:2010 Pingry SMART Team: Difference between revisions

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'''Design description'''

~~The confirmation of~~

2.5-DKGR A possesses a parallel alpha-beta structure motif common among other enzymes of the aldo-keto reductase family of eight <scene name='2010_Pingry_SMART_Team/1a80-default/2'>alpha helices(highlighted red) and eight beta strands(highlighted blue).</scene> Also conserved in members of the aldo-keto reductase family is the residue,<scene name='2010_Pingry_SMART_Team/1a80-original/10'>Tyr50</scene> that functions as both the proton donor and part of the catalytic triad. The residues,<scene name='2010_Pingry_SMART_Team/1a80-original/7'>Ala47 and Trp77;</scene>, are demonstrated in all AKR (aldo-keto reductase) enzymes as well as contributors to the formation of the active-site pocket. Located at the C-terminal side of the barrel is the active site for the

2.5-DKGR A ~~has~~ a parallel alpha-beta structure motif ~~conformation~~ common among other enzymes of the aldo-keto reductase family of eight <scene name='2010_Pingry_SMART_Team/1a80-default/2'>alpha helices(highlighted red) and eight beta strands(highlighted blue).</scene> ~~In addition to~~ the ~~conserved structure~~ the residue,<scene name='2010_Pingry_SMART_Team/1a80-original/10'>Tyr50</scene>~~, is also found in all aldo-keto-reductases and~~ functions as both the proton donor and part of the catalytic triad. The residues,<scene name='2010_Pingry_SMART_Team/1a80-original/7'>Ala47 and Trp77;</scene>, are ~~conserved~~ in all AKR (aldo-keto reductase) enzymes as well as contributors to the formation of the active-site pocket. Located at the C-terminal side of the barrel is the active site for the

<scene name='2010_Pingry_SMART_Team/1a80-original/12'>NADPH cofactor(shown in wireframe and colored CPK)</scene> to bind to 2.5-DKGR A. The NADPH cofactor is stabilized through hydrogen bonds, ionic bonds, and an aromatic pi-stacking interaction between <scene name='2010_Pingry_SMART_Team/1a80-original/2'>Trp187</scene> and the nicotinamide ring of NADPH . Although 2,5-DKGR A functions with NADPH as a cofactor, NADH is preferred for a more efficient production of vitamin C. To achieve this, mutations of the original side chains of <scene name='2010_Pingry_SMART_Team/1a80-default/1'>Lys232, Phe22, Arg238, Ala272</scene> were conducted. Significantly, the<scene name='2010_Pingry_SMART_Team/1a80-original/8'>Lys232, Ser233, and Val234</scene> sidechain interact with the phosphate group of NADPH. In order to acommodate for the cofactor, NADH, and the absent phosphate group, these side chains have been modified in the mutant form.

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 '''Design description'''
-The confirmation of
+.5-DKGR A possesses a parallel alpha-beta structure motif common among other enzymes of the aldo-keto reductase family of eight <scene name='2010_Pingry_SMART_Team/1a80-default/2'>alpha helices(highlighted red) and eight beta strands(highlighted blue).</scene> Also conserved in members of the aldo-keto reductase family is the residue,<scene name='2010_Pingry_SMART_Team/1a80-original/10'>Tyr50</scene> that functions as both the proton donor and part of the catalytic triad. The residues,<scene name='2010_Pingry_SMART_Team/1a80-original/7'>Ala47 and Trp77;</scene>, are demonstrated in all AKR (aldo-keto reductase) enzymes as well as contributors to the formation of the active-site pocket. Located at the C-terminal side of the barrel is the active site for the
-.5-DKGR A has a parallel alpha-beta structure motif conformation common among other enzymes of the aldo-keto reductase family of eight <scene name='2010_Pingry_SMART_Team/1a80-default/2'>alpha helices(highlighted red) and eight beta strands(highlighted blue).</scene>  In addition to the conserved structure the residue,<scene name='2010_Pingry_SMART_Team/1a80-original/10'>Tyr50</scene>, is also found in all aldo-keto-reductases and functions as both the proton donor and part of the catalytic triad. The residues,<scene name='2010_Pingry_SMART_Team/1a80-original/7'>Ala47 and Trp77;</scene>, are conserved in all AKR (aldo-keto reductase) enzymes as well as contributors to the formation of the active-site pocket. Located at the C-terminal side of the barrel is the active site for the
 <scene name='2010_Pingry_SMART_Team/1a80-original/12'>NADPH cofactor(shown in wireframe and colored CPK)</scene> to bind to 2.5-DKGR A. The NADPH cofactor is stabilized through hydrogen bonds, ionic bonds, and an aromatic pi-stacking interaction between <scene name='2010_Pingry_SMART_Team/1a80-original/2'>Trp187</scene> and the nicotinamide ring of NADPH . Although 2,5-DKGR A functions with NADPH as a cofactor, NADH is preferred for a more efficient production of vitamin C. To achieve this, mutations of the original side chains of <scene name='2010_Pingry_SMART_Team/1a80-default/1'>Lys232, Phe22, Arg238, Ala272</scene> were conducted. Significantly, the<scene name='2010_Pingry_SMART_Team/1a80-original/8'>Lys232, Ser233, and Val234</scene> sidechain interact with the phosphate group of NADPH. In order to acommodate for the cofactor, NADH, and the absent phosphate group, these side chains have been modified in the mutant form.