Group:SMART:2010 Pingry SMART Team: Difference between revisions
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Although it can use NADP+ more efficiently, the active site of xylose reductase has evolved to also utilize NAD+. Glu227, Asn276, and Arg280 all interact with both cofactors but in slightly different ways depending on which cofactor is present. The properties of the residues are perfect to interact with multiple key regions on the NAD+ and NADP+ molecules. | Although it can use NADP+ more efficiently, the active site of xylose reductase has evolved to also utilize NAD+. Glu227, Asn276, and Arg280 all interact with both cofactors but in slightly different ways depending on which cofactor is present. The properties of the residues are perfect to interact with multiple key regions on the NAD+ and NADP+ molecules. | ||
<scene name='2010_Pingry_SMART_Team/1k8c_default/16'>Glu227</scene> changes its interactions with the cofactor depending upon if the cofactor is NAD+ or NADP+, it has water-mediated reaction with the 3-prime alcohol group on the ribose. Similarly, <scene name='2010_Pingry_SMART_Team/1k8c_default/ | <scene name='2010_Pingry_SMART_Team/1k8c_default/16'>Glu227</scene> changes its interactions with the cofactor depending upon if the cofactor is NAD+ or NADP+, it has water-mediated reaction with the 3-prime alcohol group on the ribose. Similarly, <scene name='2010_Pingry_SMART_Team/1k8c_default/20'> Arg280 </scene> changes position and interacts differently with the two cofactors. <scene name='2010_Pingry_SMART_Team/1k8c_default/13'>Asn276</scene> employs hydrogen bonds with the different cofactors. The relative location on the cofacor differs in NAD+ and NADP+. | ||
