EC number:1.14.14.138
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen |
| 1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor |
| ID: | 1.14.14.138 | ||
|---|---|---|---|
| Description: | Lithocholate 6-beta-hydroxylase. | ||
| Alternative Name: |
Lithocholic acid 6-beta-hydroxylase. Lithocholate 6-beta-monooxygenase. Cytochrome P450 3A10. 6-beta-hydroxylase. | ||
| Prosite: | PDOC00081; | ||
| PDB: |
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3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.14.14.138 |
| BRENDA Enzyme Link: | BRENDA 1.14.14.138 |
| KEGG Enzyme Link: | KEGG1.14.14.138 |
| BioCyc Enzyme Link: | BioCyc 1.14.14.138 |
| ExPASy Enzyme Link: | ExPASy1.14.14.138 |
| EC2PDB Enzyme Link: | EC2PDB 1.14.14.138 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.14.14.138 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.14.14.138 |
| IntEnz Enzyme Link: | IntEnz 1.14.14.138 |
| MEDLINE Enzyme Link: | MEDLINE 1.14.14.138 |
EC number:1.14.14.138
| MSA: | |
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| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:18857 | lithocholate + O2 + reduced [NADPH--hemoprotein reductase] = 6beta-hydroxylithocholate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[*:3].[*:4]-[N;H0;+0:5]1-[CH;+0:6]=[C;H0;+0:7](-[*:8])-[CH2;+0:9]-[CH;+0:10]=[CH;+0:11]-1.[H+;H0:12].[O;H0;+0:13]=[O;H0;+0:14]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:13].[*:4]-[n+;H0:5]1:[cH;+0:6]:[c;H0;+0:7](-[*:8]):[cH;+0:9]:[cH;+0:10]:[cH;+0:11]:1.[OH2;+0:14] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The lithocholic acid 6 beta-hydroxylase cytochrome P-450, CYP 3A10, is an active catalyst of steroid-hormone 6 beta-hydroxylation. | Chang TK, Teixeira J, Gil G, Waxman DJ | 1993 Apr 15 | 8484723 |
| Cloning, expression, and regulation of lithocholic acid 6 beta-hydroxylase. | Teixeira J, Gil G | 1991 Nov 5 | 1840595 |
| The enzymes, regulation, and genetics of bile acid synthesis. | Russell DW | 2003 | 12543708 |