3alpha(or 20beta)-hydroxysteroid dehydrogenase
NADH-20beta-hydroxysteroid dehydrogenase
The altered specificity of cortisone reductase with certain retroandrostan-3-one substrates.
The functioning of a nicotinamide--adenine dinucleotide-dependent dehydrogenase and the structure adjacent to the reacting carbon atom of the substrate.
Cortisone reductase and some small non-steroid analogues of its steroid substrates.
Renaturation and urea-induced denaturation of 20 beta-hydroxysteroid dehydrogenase studied in solution and in the immobilized state.
Structural requirements in 20-oxo-steroids for interaction with the catalytic site of 20 beta-hydroxysteroid dehydrogenase.
Bifunctional enzyme activity at the same active site: competitive inhibition kinetics with 3 alpha/20 beta-hydroxysteroid dehydrogenase.
Structural requirements in 20-oxo-steroids for interaction with the binding site of 20beta-hydroxysteroid dehydrogenase.
Crystallization and preliminary crystallographic study of 3 alpha, 20 beta-hydroxysteroid dehydrogenase from Streptomyces hydrogenans.
Crystals of active tetramers of 3 alpha, 20 beta-hydroxysteroid dehydrogenase.
20 beta-hydroxysteroid dehydrogenase of neonatal pig testis: 3 alpha/beta-hydroxysteroid dehydrogenase activities catalyzed by highly purified enzyme.
Three-dimensional structure of holo 3 alpha,20 beta-hydroxysteroid dehydrogenase: a member of a short-chain dehydrogenase family.
Mechanism of inhibition of 3 alpha, 20 beta-hydroxysteroid dehydrogenase by a licorice-derived steroidal inhibitor.
The refined three-dimensional structure of 3 alpha,20 beta-hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases.
The rat 17 alpha-hydroxylase-17,20-desmolase (CYP17) active site: computerized homology modeling and site directed mutagenesis.
Structure and function of steroid dehydrogenases involved in hypertension, fertility, and cancer.
Directed evolution approach to a structural genomics project: Rv2002 from Mycobacterium tuberculosis.
This enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily, along with its homologous enzyme (S00326 in EzCatDB) and Drosophia alcohol dehydrogenase (S00319 in EzCatDB). However, this enzyme has got an additional catalytic residue, Glu142, in addition to a classical catalytic triad composed of conserved residues, Ser, Tyr, and Lys. Moreover, the conformation of these residues, compared to that of the NAD molecule and substrate, seems to be slightly different from that of the homologous enzymes. Glu142 seems to interact with the substrate oxygen atom, whereas Ser140 does not interact with the oxygen atom, unlike those catalytic Ser residues in the other homologous enzymes (see [16]). According to the literature [16], Glu142 might reverse the effect of Lys157, which is supposed to modulate the pKa of Tyr153 in the homologous enzymes.