| EC |
1.1.1.395 |
| Accepted name: |
3α-hydroxy bile acid-CoA-ester 3-dehydrogenase |
| Reaction: |
a 3α-hydroxy bile acid CoA ester + NAD+ = a 3-oxo bile acid CoA ester + NADH + H+ |
| Other name(s): |
baiA1 (gene name); baiA2 (gene name); baiA3 (gene name) |
| Systematic name: |
3α-hydroxy-bile-acid-CoA-ester:NAD+ 3-oxidoreductase |
| Comments: |
This bacterial enzyme is involved in the 7-dehydroxylation process associated with bile acid degradation. The enzyme has very little activity with unconjugated bile acid substrates. It has similar activity with choloyl-CoA, chenodeoxycholoyl-CoA, deoxycholoyl-CoA, and lithocholoyl-CoA. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Mallonee, D.H., Lijewski, M.A. and Hylemon, P.B. Expression in Escherichia coli and characterization of a bile acid-inducible 3α-hydroxysteroid dehydrogenase from Eubacterium sp. strain VPI 12708. Curr. Microbiol. 30 (1995) 259–263. [PMID: 7766153] |
| 2. |
Bhowmik, S., Jones, D.H., Chiu, H.P., Park, I.H., Chiu, H.J., Axelrod, H.L., Farr, C.L., Tien, H.J., Agarwalla, S. and Lesley, S.A. Structural and functional characterization of BaiA, an enzyme involved in secondary bile acid synthesis in human gut microbe. Proteins 82 (2014) 216–229. [DOI] [PMID: 23836456] |
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| [EC 1.1.1.395 created 2016] |
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