ENZYME entry: EC 1.17.99.5
| Accepted Name |
|---|
| Bile-acid 7-alpha-dehydroxylase.
|
| Alternative Name(s) |
|---|
| 7-alpha-dehydroxylase. |
| Bile acid 7-dehydroxylase. |
| Cholate 7-alpha-dehydroxylase. |
| Reaction catalysed |
|---|
- Deoxycholate + FAD + H(2)O <=> cholate + FADH(2)
- Lithocholate + FAD + H(2)O <=> chenodeoxycholate + FADH(2)
|
| Comment(s) |
|---|
- Under physiological conditions, the reactions occur in the reverse
direction to that shown above.
- Highly specific for bile-acid substrates and requires a free C-24
carboxy group and an unhindered 7-alpha-hydroxy group on the B-ring
of the steroid nucleus for activity, as found in cholate and
chenodeoxycholate.
- The reaction is stimulated by the presence of NAD(+) but is inhibited
by excess NADH.
- This unusual regulation by the NAD(+)/NADH ratio is most likely the
result of the intermediates being linked at C-24 by an anhydride bond
to the 5'-diphosphate of 3'-phospho-ADP.
- Allo-deoxycholate is also formed as a side-product of the 7-alpha-
dehydroxylation of cholate.
- Formerly EC 1.17.1.6.
|
| Cross-references |
|---|
| PROSITE | PDOC00060 |
| BRENDA | 1.17.99.5 |
| EC2PDB | 1.17.99.5 |
| ExplorEnz | 1.17.99.5 |
| PRIAM enzyme-specific profiles | 1.17.99.5 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.17.99.5 |
| IUBMB Enzyme Nomenclature | 1.17.99.5 |
| IntEnz | 1.17.99.5 |
| MEDLINE | Find literature relating to 1.17.99.5 |
| MetaCyc | 1.17.99.5 |
| UniProtKB/Swiss-Prot |
|
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