SDR: Structure, mechanism of action, and substrate recognition

被引:90
作者
Tanaka, N
Nonaka, T
Nakamura, KT
Hara, A
机构
[1] Showa Univ, Sch Pharmaceut Sci, Shinagawa Ku, Tokyo 1428555, Japan
[2] Nagaoka Univ Technol, Dept Bioengn, Nagaoka, Niigata 9402188, Japan
[3] Gifu Pharmaceut Univ, Biochem Lab, Gifu 5028585, Japan
关键词
D O I
10.2174/1385272013375751
中图分类号
O62 [有机化学];
学科分类号
070303 ; 081704 ;
摘要
Short-chain dehydrogenases/reductases (SDR) constitute a large protein family. The SDR family now includes more than 1,000 enzymes from humans, mammals, insects and bacteria, and exhibits a wide variety of substrate specificity for steroids, retinoids, prostaglandins, sugars, alcohols and other small molecules. These enzymes have a residue identity level of 15-30 %. Much has been done in the last decade to understand the structure-function relationships in the SDR enzymes. This review summarizes recent progress of structural and functional studies of the enzymes belonging to the SDR family (X-ray crystal structure analyses and site-directed mutagenesis studies). Based on these studies, the three-dimensional structure, catalytic mechanism, coenzyme specificity, and substrate specificity of the SDR enzymes are discussed.
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页码:89 / 111
页数:23
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