SDR: Structure, mechanism of action, and substrate recognition

Citation
N. Tanaka et al., SDR: Structure, mechanism of action, and substrate recognition, CURR ORG CH, 5(1), 2001, pp. 89-111
Citations number
83
Categorie Soggetti
Organic Chemistry/Polymer Science
Journal title
CURRENT ORGANIC CHEMISTRY
ISSN journal
13852728 → ACNP
Volume
5
Issue
1
Year of publication
2001
Pages
89 - 111
Database
ISI
SICI code
1385-2728(200101)5:1<89:SSMOAA>2.0.ZU;2-T
Abstract
Short-chain dehydrogenases/reductases (SDR) constitute a large protein fami ly. The SDR family now includes more than 1,000 enzymes from humans, mammal s, insects and bacteria, and exhibits a wide variety of substrate specifici ty for steroids, retinoids, prostaglandins, sugars, alcohols and other smal l molecules. These enzymes have a residue identity level of 15-30 %. Much h as been done in the last decade to understand the structure-function relati onships in the SDR enzymes. This review summarizes recent progress of struc tural and functional studies of the enzymes belonging to the SDR family (X- ray crystal structure analyses and site-directed mutagenesis studies). Base d on these studies, the three-dimensional structure, catalytic mechanism, c oenzyme specificity, and substrate specificity of the SDR enzymes are discu ssed.