The catalytic roles of P185 and T188 and substrate-binding loop flexibility in 3α-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni.

The catalytic roles of P185 and T188 and substrate-binding loop flexibility in 3α-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni.

3α-Hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni reversibly catalyzes the oxidation of androsterone with NAD(+) to form androstanedione and NADH. Structurally the substrate-binding loop of the residues, T188-K208, is unresolved, while binding with NAD(+) causes the appe...

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Autores principales: Chi-Ching Hwang, Yi-Hsun Chang, Hwei-Jen Lee, Tzu-Pin Wang, Yu-Mei Su, Hsin-Wei Chen, Po-Huang Liang
Formato: article
Lenguaje:EN
Publicado: Public Library of Science (PLoS) 2013
Materias:
Medicine
R
Science
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Acceso en línea:https://doaj.org/article/5d21877c0bad475fb497996253eccd6d
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