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Selectivity determinants of inhibitor binding to human 20alpha-hydroxysteroid dehydrogenase: crystal structure of the enzyme in ternary complex with coenzyme and the potent inhibitor
The crystal structure of human 20alpha-hydroxysteroid dehydrogenase (AKR1C1) in ternary complex with the coenzyme NADP (+) and the potent inhibitor 3,5-dichlorosalicylic acid and the important role of the nonconserved residues Leu54, His222, Leu306, and Leu308 in inhibitor binding and selectivity was determined by site-directed mutagenesis.
Structures of dimeric dihydrodiol dehydrogenase apoenzyme and inhibitor complex: Probing the subunit interface with site‐directed mutagenesis
The similarity between the quaternary structures of mammalian DD and glucose‐fructose oxidoreductase isolated from the prokaryotic organism Zymomonas mobilis suggests that both enzymes are members of a unique family of oligomeric proteins and may share a common ancestral gene.
Structure of monkey dimeric dihydrodiol dehydrogenase in complex with isoascorbic acid.
Mammalian dimeric dihydrodiol dehydrogenase (DD) is identical to NADP+-dependent D-xylose dehydrogenases, but differs from both GFO and AFR in its specificity for sugars and hydrophobic xenobiotic compounds as substrates.
Crystallization and preliminary X-ray crystallographic analysis of rabbit L-gulonate 3-dehydrogenase.
Rabbit L-gulonate 3-dehydrogenase was crystallized using the oil-microbatch method and the presence of a monomeric protomer in the asymmetric unit gives a V(M) value of 2.21 A(3) Da(-1) and a solvent content of 44.4%.