Abstract
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 perent. 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.
Keywords: SDR structure, Short chain dehydrogenase, Oxidoreductase, MDR enzymes, Monomeric enzymes, Single domain protein, Rossmann fold, C terminal residues, Coenzyme binding mode, pyrophosphate moiety, active site cleft, ser tyr lys triad, deprotonated phenolic group, coenzyme specificity, Substrate specificity, membrane spainnig domain
Call for Papers in Thematic Issues
Catalytic C-H bond activation as a tool for functionalization of heterocycles
The major topic is the functionalization of heterocycles through catalyzed C-H bond activation. The strategies based on C-H activation not only provide straightforward formation of C-C or C-X bonds but, more importantly, allow for the avoidance of pre-functionalization of one or two of the cross-coupling partners. The beneficial impact of ...read more
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