| 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: | 1.14.14.113 |
|---|---|
| Description: | Alpha-humulene 10-hydroxylase. |
| Alternative Name: |
CYP71BA1. |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 1.14.14.113 |
| BRENDA Enzyme Link: | BRENDA 1.14.14.113 |
| KEGG Enzyme Link: | KEGG1.14.14.113 |
| BioCyc Enzyme Link: | BioCyc 1.14.14.113 |
| ExPASy Enzyme Link: | ExPASy1.14.14.113 |
| EC2PDB Enzyme Link: | EC2PDB 1.14.14.113 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.14.14.113 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.14.14.113 |
| IntEnz Enzyme Link: | IntEnz 1.14.14.113 |
| MEDLINE Enzyme Link: | MEDLINE 1.14.14.113 |
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:32491 | (1E,4E,8E)-alpha-humulene + O2 + reduced [NADPH--hemoprotein reductase] = 10-hydroxy-alpha-humulene + 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 |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Zingiber zerumbet CYP71BA1 catalyzes the conversion of α-humulene to 8-hydroxy-α-humulene in zerumbone biosynthesis. | Yu F, Okamoto S, Harada H, Yamasaki K, Misawa N, Utsumi R | 2011 Mar | 20730551 |
| Molecular cloning and functional characterization of alpha-humulene synthase, a possible key enzyme of zerumbone biosynthesis in shampoo ginger (Zingiber zerumbet Smith). | Yu F, Okamto S, Nakasone K, Adachi K, Matsuda S, Harada H, Misawa N, Utsumi R | 2008 May | 18273640 |