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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Detalles Bibliográficos
Autores principales: Hwang, Chi-Ching, Chang, Yi-Hsun, Lee, Hwei-Jen, Wang, Tzu-Pin, Su, Yu-Mei, Chen, Hsin-Wei, Liang, Po-Huang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3662788/
https://www.ncbi.nlm.nih.gov/pubmed/23717450
http://dx.doi.org/10.1371/journal.pone.0063594

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3662788/
https://www.ncbi.nlm.nih.gov/pubmed/23717450
http://dx.doi.org/10.1371/journal.pone.0063594

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