DHRS1 Conclusion: Difference between revisions
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Through comparison of DHRS1 against proteins with similar structure it was possible to identify several conserved regions that are important in the folding and function of HSDR1. | |||
Through comparison of | |||
DHRS1 may reduce Glucose by using NAD(P) as an electron donor. Further kinetic studies with other likely substrates (sugars) are needed to confirm this. An [G-x(3)-G-x-G] motif that is a Characteristic co-enzyme binding fold may bind a substrate possibly glucose. Site directed mutagenasis and further kinetic studies will reveal the role of this motif, if any. Future studies of DHRS1 or similar related proteins may also lead to greater understanding of the SDR family and its biological importance or may potentially hold keys to better understanding of clinical problems like disease. | |||
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[[Dehydrogenase/reductase (SDR family) member 1 | Back to Main Page]] | [[Dehydrogenase/reductase (SDR family) member 1 | Back to Main Page]] | ||
Revision as of 13:07, 9 June 2008
Through comparison of DHRS1 against proteins with similar structure it was possible to identify several conserved regions that are important in the folding and function of HSDR1.
DHRS1 may reduce Glucose by using NAD(P) as an electron donor. Further kinetic studies with other likely substrates (sugars) are needed to confirm this. An [G-x(3)-G-x-G] motif that is a Characteristic co-enzyme binding fold may bind a substrate possibly glucose. Site directed mutagenasis and further kinetic studies will reveal the role of this motif, if any. Future studies of DHRS1 or similar related proteins may also lead to greater understanding of the SDR family and its biological importance or may potentially hold keys to better understanding of clinical problems like disease.
Back to Main Page
