Group:SMART:2010 Pingry SMART Team: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Tommie Hata (talk | contribs) |
Tommie Hata (talk | contribs) |
||
| Line 91: | Line 91: | ||
==='''Inherent dual cofactor use, Xylose reductase'''=== | ==='''Inherent dual cofactor use, Xylose reductase'''=== | ||
[[2010 Pingry SMART Team Models]] | [[Group:SMART:2010 Pingry SMART Team Models]] | ||
Xylose reductase is an unusual protein from the aldo-keto reductase superfamily in that the wild type is able to efficiently utilize both NADH and NADPH in its reduction of the 5 carbon sugar xylose into xylitol. Normally found in the yeast ''Candida tenuis'', it functions biologically as a homodimer unlike the majority of AKR proteins. While Dr. Banta is not actively researching this protein, Xylose Reductase's dual substrate specificity has influenced his engineering of AdhD. Because of its ability to change the conformation of two major loops, which enable different side chain orientations and therefore interactions, Xylose Reductase can accomodate both the presence and absence of a phosphate in the cofactor. | Xylose reductase is an unusual protein from the aldo-keto reductase superfamily in that the wild type is able to efficiently utilize both NADH and NADPH in its reduction of the 5 carbon sugar xylose into xylitol. Normally found in the yeast ''Candida tenuis'', it functions biologically as a homodimer unlike the majority of AKR proteins. While Dr. Banta is not actively researching this protein, Xylose Reductase's dual substrate specificity has influenced his engineering of AdhD. Because of its ability to change the conformation of two major loops, which enable different side chain orientations and therefore interactions, Xylose Reductase can accomodate both the presence and absence of a phosphate in the cofactor. | ||
| Line 135: | Line 135: | ||
{{Clear}} | {{Clear}} | ||
== Substrate specificity == | == Substrate specificity == | ||