EC number:1.14.14.154
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: | 1.14.14.154 | ||
|---|---|---|---|
| Description: | Sterol 14-alpha-demethylase. | ||
| Alternative Name: |
Obtusufoliol 14-demethylase. Lanosterol 14-demethylase. Lanosterol 14-alpha-demethylase. Cytochrome P450 51. CYP51. | ||
| Prosite: | PDOC00081; | ||
| PDB: |
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3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.14.14.154 |
| BRENDA Enzyme Link: | BRENDA 1.14.14.154 |
| KEGG Enzyme Link: | KEGG1.14.14.154 |
| BioCyc Enzyme Link: | BioCyc 1.14.14.154 |
| ExPASy Enzyme Link: | ExPASy1.14.14.154 |
| EC2PDB Enzyme Link: | EC2PDB 1.14.14.154 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.14.14.154 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.14.14.154 |
| IntEnz Enzyme Link: | IntEnz 1.14.14.154 |
| MEDLINE Enzyme Link: | MEDLINE 1.14.14.154 |
EC number:1.14.14.154
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:54028 | a 14alpha-methyl steroid + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase] |
| RULE(radius=1) | [*:1]-[C;H0;+0:2]1=[CH;+0:3]-[N;H0;+0:4](-[*:5])-[CH;+0:6]=[CH;+0:7]-[CH2;+0:8]-1.[*:9]-[CH2;+0:10]-[C;H0;+0:11](-[*:12])(-[*:13])-[CH3;+0:14].[*:15]-[N;H0;+0:16]1-[CH;+0:17]=[C;H0;+0:18](-[*:19])-[CH2;+0:20]-[CH;+0:21]=[CH;+0:22]-1.[*:23]-[N;H0;+0:24]1-[CH;+0:25]=[C;H0;+0:26](-[*:27])-[CH2;+0:28]-[CH;+0:29]=[CH;+0:30]-1.[H+;H0:31].[H+;H0:32].[O;H0;+0:33]=[O;H0;+0:34].[O;H0;+0:35]=[O;H0;+0:36].[O;H0;+0:37]=[O;H0;+0:38]>>[*:9]-[CH;+0:10]=[C;H0;+0:11](-[*:12])-[*:13].[*:1]-[c;H0;+0:2]1:[cH;+0:3]:[n+;H0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[*:15]-[n+;H0:16]1:[cH;+0:17]:[c;H0;+0:18](-[*:19]):[cH;+0:20]:[cH;+0:21]:[cH;+0:22]:1.[*:23]-[n+;H0:24]1:[cH;+0:25]:[c;H0;+0:26](-[*:27]):[cH;+0:28]:[cH;+0:29]:[cH;+0:30]:1.[O;H0;+0:37]=[CH;+0:14]-[OH;+0:38].[OH2;+0:33].[OH2;+0:34].[OH2;+0:35].[OH2;+0:36] |
| Reaction |  |
| Core-to-Core | |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Identification, modeling and ligand affinity of early deuterostome CYP51s, and functional characterization of recombinant zebrafish sterol 14α-demethylase. | Morrison AM, Goldstone JV, Lamb DC, Kubota A, Lemaire B, Stegeman JJ | 2014 Jun | 24361620 |
| CYP51 from Trypanosoma cruzi: a phyla-specific residue in the B' helix defines substrate preferences of sterol 14alpha-demethylase. | Lepesheva GI, Zaitseva NG, Nes WD, Zhou W, Arase M, Liu J, Hill GC, Waterman MR | 2006 Feb 10 | 16321980 |
| Arabidopsis cyp51 mutant shows postembryonic seedling lethality associated with lack of membrane integrity. | Kim HB, Schaller H, Goh CH, Kwon M, Choe S, An CS, Durst F, Feldmann KA, Feyereisen R | 2005 Aug | 16040657 |
| Obtusifoliol 14alpha-demethylase (CYP51) antisense Arabidopsis shows slow growth and long life. | Kushiro M, Nakano T, Sato K, Yamagishi K, Asami T, Nakano A, Takatsuto S, Fujioka S, Ebizuka Y, Yoshida S | 2001 Jul 6 | 11437378 |
| The ubiquitously expressed human CYP51 encodes lanosterol 14 alpha-demethylase, a cytochrome P450 whose expression is regulated by oxysterols. | Strömstedt M, Rozman D, Waterman MR | 1996 May 1 | 8619637 |
| Cloning and functional expression of the cDNA encoding rat lanosterol 14-alpha demethylase. | Sloane DL, So OY, Leung R, Scarafia LE, Saldou N, Jarnagin K, Swinney DC | 1995 Aug 19 | 7665087 |
| Structural basis of human CYP51 inhibition by antifungal azoles. | Strushkevich N, Usanov SA, Park HW | 2010 Apr 9 | 20149798 |
| RHEA:25286 | lanosterol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase] |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](-[*:3])(-[CH3;+0:4])-[CH2;+0:5]-[*:6].[*:7]-[C;H0;+0:8]1=[CH;+0:9]-[N;H0;+0:10](-[*:11])-[CH;+0:12]=[CH;+0:13]-[CH2;+0:14]-1.[*:15]-[N;H0;+0:16]1-[CH;+0:17]=[C;H0;+0:18](-[*:19])-[CH2;+0:20]-[CH;+0:21]=[CH;+0:22]-1.[*:23]-[N;H0;+0:24]1-[CH;+0:25]=[C;H0;+0:26](-[*:27])-[CH2;+0:28]-[CH;+0:29]=[CH;+0:30]-1.[H+;H0:31].[H+;H0:32].[O;H0;+0:33]=[O;H0;+0:34].[O;H0;+0:35]=[O;H0;+0:36].[O;H0;+0:37]=[O;H0;+0:38]>>[*:1]-[C;H0;+0:2](-[*:3])=[CH;+0:5]-[*:6].[*:7]-[c;H0;+0:8]1:[cH;+0:9]:[n+;H0:10](-[*:11]):[cH;+0:12]:[cH;+0:13]:[cH;+0:14]:1.[*:15]-[n+;H0:16]1:[cH;+0:17]:[c;H0;+0:18](-[*:19]):[cH;+0:20]:[cH;+0:21]:[cH;+0:22]:1.[*:23]-[n+;H0:24]1:[cH;+0:25]:[c;H0;+0:26](-[*:27]):[cH;+0:28]:[cH;+0:29]:[cH;+0:30]:1.[O;H0;+0:37]=[CH;+0:4]-[OH;+0:38].[OH2;+0:33].[OH2;+0:34].[OH2;+0:35].[OH2;+0:36] |
| Reaction |  |
| Core-to-Core | |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Structural basis of human CYP51 inhibition by antifungal azoles. | Strushkevich N, Usanov SA, Park HW | 2010 Apr 9 | 20149798 |
| The amino acid residues affecting the activity and azole susceptibility of rat CYP51 (sterol 14-demethylase P450). | Nitahara Y, Kishimoto K, Yabusaki Y, Gotoh O, Yoshida Y, Horiuchi T, Aoyama Y | 2001 May | 11328599 |
| Purification and characterization of rat sterol 14-demethylase P450 (CYP51) expressed in Escherichia coli. | Nitahara Y, Aoyama Y, Horiuchi T, Noshiro M, Yoshida Y | 1999 Nov | 10544287 |
| RHEA:14917 | 3 O2 + obtusifoliol + 3 reduced [NADPH--hemoprotein reductase] = 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase] |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](-[*:3])(-[CH3;+0:4])-[CH2;+0:5]-[*:6].[*:7]-[C;H0;+0:8]1=[CH;+0:9]-[N;H0;+0:10](-[*:11])-[CH;+0:12]=[CH;+0:13]-[CH2;+0:14]-1.[*:15]-[N;H0;+0:16]1-[CH;+0:17]=[C;H0;+0:18](-[*:19])-[CH2;+0:20]-[CH;+0:21]=[CH;+0:22]-1.[*:23]-[N;H0;+0:24]1-[CH;+0:25]=[C;H0;+0:26](-[*:27])-[CH2;+0:28]-[CH;+0:29]=[CH;+0:30]-1.[H+;H0:31].[H+;H0:32].[O;H0;+0:33]=[O;H0;+0:34].[O;H0;+0:35]=[O;H0;+0:36].[O;H0;+0:37]=[O;H0;+0:38]>>[*:1]-[C;H0;+0:2](-[*:3])=[CH;+0:5]-[*:6].[*:7]-[c;H0;+0:8]1:[cH;+0:9]:[n+;H0:10](-[*:11]):[cH;+0:12]:[cH;+0:13]:[cH;+0:14]:1.[*:15]-[n+;H0:16]1:[cH;+0:17]:[c;H0;+0:18](-[*:19]):[cH;+0:20]:[cH;+0:21]:[cH;+0:22]:1.[*:23]-[n+;H0:24]1:[cH;+0:25]:[c;H0;+0:26](-[*:27]):[cH;+0:28]:[cH;+0:29]:[cH;+0:30]:1.[O;H0;+0:37]=[CH;+0:4]-[OH;+0:38].[OH2;+0:33].[OH2;+0:34].[OH2;+0:35].[OH2;+0:36] |
| Reaction |  |
| Core-to-Core | |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Obtusifoliol 14alpha-demethylase (CYP51) antisense Arabidopsis shows slow growth and long life. | Kushiro M, Nakano T, Sato K, Yamagishi K, Asami T, Nakano A, Takatsuto S, Fujioka S, Ebizuka Y, Yoshida S | 2001 Jul 6 | 11437378 |