Group:SMART:2010 Pingry SMART Team: Difference between revisions
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2,5-DKGR A possesses a parallel alpha-beta structural motif of the <scene name='2010_Pingry_SMART_Team/1a80-default/2'>eight alpha helices (highlighted red) and eight beta strands (highlighted blue)</scene> found in all enzymes in the aldo-keto reductase(AKR) family. | 2,5-DKGR A possesses a parallel alpha-beta structural motif of the <scene name='2010_Pingry_SMART_Team/1a80-default/2'>eight alpha helices (highlighted red) and eight beta strands (highlighted blue)</scene> found in all enzymes in the aldo-keto reductase(AKR) family. | ||
The residue <scene name='2010_Pingry_SMART_Team/1a80-original/ | The residue <scene name='2010_Pingry_SMART_Team/1a80-original/16'>Tyr50</scene> is found at the bottom of the active-site pocket and is conserved in all members of the AKR family. The catalytic mechanism in 2,5 DKGR A is similar to aldose reductase and other members of that super family. | ||
The first step involves transferring a hydride ion (H-) from NADPH to the substrate leaving an oxidized cofactor. | The first step involves transferring a hydride ion (H-) from NADPH to the substrate leaving an oxidized cofactor. | ||
The second step involves transferring a proton (H+) to the substrate | The second step involves transferring a proton (H+) to the substrate | ||
