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

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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/2'>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/2'>Lys232Gly mutation</scene>
to adapt to the absent pyrophosphate group in NADH. Significantly, Gly lacks a side chain since no interaction is necessary due to the absent phosphate group in NADH. In addition, the mutation results with with a reduction in cofactor Ka and kcat.  
to adapt to the absent pyrophosphate group in NADH. Significantly, Gly lacks a side chain since no interaction is necessary due to the absent phosphate group in NADH. In addition, the mutation results in the reduction of cofactor Ka and kcat.  


The <scene name='2010_Pingry_SMART_Team/1m9h_original/3'>Phe22Tyr mutation</scene> reduces the Km for both NADPH and NADH. A reduced Km makes a more efficient enzyme at a lower substrate level, therefore, improving the enzyme. The Arg238His mutation forms a pi-stacking interaction to stabilize the AKR with the cofactor. A pi-stacking interaction is extremely stable and the pi bonds are perpendicular. A common source for pi-stacking is in DNA. The <scene name='2010_Pingry_SMART_Team/1m9h_original/5'>Ala272Gly mutation</scene> mutation improves the kinetic properties by making it easier for the substrate to bind with the substrate and by improving the kinetics of cofactor binding and release.
The <scene name='2010_Pingry_SMART_Team/1m9h_original/3'>Phe22Tyr mutation</scene> reduces the Km for both NADPH and NADH. A reduced Km creates a more efficient enzyme at a lower substrate level, therefore, improving the enzyme. The Arg238His mutation forms a pi-stacking interaction to stabilize the AKR with the cofactor. A pi-stacking interaction is extremely stable and the pi bonds are perpendicular. A common source for pi-stacking is in DNA. The <scene name='2010_Pingry_SMART_Team/1m9h_original/5'>Ala272Gly mutation</scene> mutation improves the kinetic properties by making it easier for the substrate to bind with the substrate and by improving the kinetics of cofactor binding and release.


The residue <scene name='2010_Pingry_SMART_Team/1m9h_original/6'>Trp187</scene> is highlighted by displaying the side chain. The pi-stacking interaction Trp187 has with the nicotinamide ring of the cofactor stabilizes the reaction.
The residue <scene name='2010_Pingry_SMART_Team/1m9h_original/6'>Trp187</scene> is highlighted by displaying the side chain. The pi-stacking interaction Trp187 has with the nicotinamide ring of the cofactor stabilizes the reaction.
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