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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Bibliographic Details
Main Authors: Chi-Ching Hwang, Yi-Hsun Chang, Hwei-Jen Lee, Tzu-Pin Wang, Yu-Mei Su, Hsin-Wei Chen, Po-Huang Liang
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2013-01-01
Series:PLoS ONE
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23717450/pdf/?tool=EBI

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https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23717450/pdf/?tool=EBI

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