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.
DHRS1 has evolved over a long period of time, and the SDR family is found in all aspects of life. It has some highly conserved regions, such as LDVLV and the S-Y-K residues. The SDK superfamily can be split into many different families, the two most interesting to our target protein are classic SDR and extended SDR. Classic SDR form the predecessing family from which the extended SDR family originated. Our target protein is part of the extended SDR family.
Abstract | Introduction | Results | Discussion | Conclusion | Method | References
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