Group:SMART:2010 Pingry SMART Team: Difference between revisions
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Four mutations of 2,5-Diketo-d-gluconic acid reductase have been conducted to alternate its cofcator specificity to <scene name='2010_Pingry_SMART_Team/1m9h_original/16'>NADH (shown in wireframe and colored CPK)</scene> rather than NADPH. These mutations of <scene name='2010_Pingry_SMART_Team/1m9h_original/17'>(Lys232Gly, Phe22Tyr, Arg238His, Ala272Gly).</scene>and their backbones have been highlighted orange to distinguish the change in amino acids between the 2,5-DKGR wildtype and the NADP-binding mutant. | Four mutations of 2,5-Diketo-d-gluconic acid reductase have been conducted to alternate its cofcator specificity to <scene name='2010_Pingry_SMART_Team/1m9h_original/16'>NADH (shown in wireframe and colored CPK)</scene> rather than NADPH. These mutations of <scene name='2010_Pingry_SMART_Team/1m9h_original/17'>(Lys232Gly, Phe22Tyr, Arg238His, Ala272Gly).</scene>and their backbones have been highlighted orange to distinguish the change in amino acids between the 2,5-DKGR wildtype and the NADP-binding mutant. | ||
Lys 232 in the 2,5-DKGR wildtype interacts directly with the pyrophosphate group of NADPH through hydrogen bonds. However, in the 2,5-DKGR mutant,this residue has been altered into a <scene name='2010_Pingry_SMART_Team/1m9h_original/19'>Lys232Gly mutation</scene> | Lys 232 in the 2,5-DKGR wildtype interacts directly with the pyrophosphate group of NADPH through hydrogen bonds. However, in the 2,5-DKGR mutant,this residue has been altered into a <scene name='2010_Pingry_SMART_Team/1m9h_original/19'>Lys232Gly mutation</scene> | ||
