EC number:1.14.15.15
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen |
| 1.14.15 With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor |
| ID: | 1.14.15.15 | ||
|---|---|---|---|
| Description: | Cholestanetriol 26-monooxygenase. | ||
| Alternative Name: |
Vitamin D(3) 25-hydroxylase. Sterol 27-hydroxylase. Sterol 26-hydroxylase. Cytochrome P450 27A1'. Cholesterol 27-hydroxylase. Cholestanetriol 26-hydroxylase. 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol hydroxylase. 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 26-hydroxylase. | ||
| Prosite: | PDOC00081; | ||
| PDB: |
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| Cath: | 1.10.630.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.14.15.15 |
| BRENDA Enzyme Link: | BRENDA 1.14.15.15 |
| KEGG Enzyme Link: | KEGG1.14.15.15 |
| BioCyc Enzyme Link: | BioCyc 1.14.15.15 |
| ExPASy Enzyme Link: | ExPASy1.14.15.15 |
| EC2PDB Enzyme Link: | EC2PDB 1.14.15.15 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.14.15.15 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.14.15.15 |
| IntEnz Enzyme Link: | IntEnz 1.14.15.15 |
| MEDLINE Enzyme Link: | MEDLINE 1.14.15.15 |
EC number:1.14.15.15
| MSA: | |
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| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:34631 | 5beta-cholestane-3alpha,7alpha,12alpha-triol + 5 H(+) + 3 O2 + 6 reduced [adrenodoxin] = (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + 4 H2O + 6 oxidized [adrenodoxin] |
| RULE(radius=1) | [*:1]-[CH3;+0:2].[*:3]-[Fe;H0;+0:4]-[*:5].[*:6]-[Fe;H0;+0:7]-[*:8].[H+;H0:9].[H+;H0:10].[O;H0;+0:11]=[O;H0;+0:12]>>[*:1]-[C;H0;+0:2](=[O;H0;+0:11])-[OH;+0:12].[*:3]-[Fe+;H0:4]-[*:5].[*:6]-[Fe+;H0:7]-[*:8] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Activities of recombinant human cytochrome P450c27 (CYP27) which produce intermediates of alternative bile acid biosynthetic pathways. | Pikuleva IA, Babiker A, Waterman MR, Björkhem I | 1998 Jul 17 | 9660774 |
| Sterol 27-hydroxylase in bile acid biosynthesis. Mechanism of oxidation of 5 beta-cholestane-3 alpha,7 alpha,12 alpha,27-tetrol into 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoic acid. | Holmberg-Betsholtz I, Lund E, Björkhem I, Wikvall K | 1993 May 25 | 8496170 |
| Hydroxylations in biosynthesis of bile acids. Isolation of a cytochrome P-450 from rabbit liver mitochondria catalyzing 26-hydroxylation of C27-steroids. | Wikvall K | 1984 Mar 25 | 6423637 |
| Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme. | Andersson S, Davis DL, Dahlbäck H, Jörnvall H, Russell DW | 1989 May 15 | 2722778 |
| Oxidation of 5 beta-cholestane-3 alpha,7 alpha, 12 alpha-triol into 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoic acid by cytochrome P-450(26) from rabbit liver mitochondria. | Dahlbäck H, Holmberg I | 1990 Mar 16 | 2322231 |
| Purification, characterization, and directed evolution study of a vitamin D3 hydroxylase from Pseudonocardia autotrophica. | Fujii Y, Kabumoto H, Nishimura K, Fujii T, Yanai S, Takeda K, Tamura N, Arisawa A, Tamura T | 2009 Jul 24 | 19450562 |
| Characterization of human sterol 27-hydroxylase. A mitochondrial cytochrome P-450 that catalyzes multiple oxidation reaction in bile acid biosynthesis. | Cali JJ, Russell DW | 1991 Apr 25 | 1708392 |
| Identification of ligands for DAF-12 that govern dauer formation and reproduction in C. elegans. | Motola DL, Cummins CL, Rottiers V, Sharma KK, Li T, Li Y, Suino-Powell K, Xu HE, Auchus RJ, Antebi A, Mangelsdorf DJ | 2006 Mar 24 | 16529801 |
| Putative helix F contributes to regioselectivity of hydroxylation in mitochondrial cytochrome P450 27A1. | Pikuleva IA, Puchkaev A, Björkhem I | 2001 Jun 26 | 11412116 |