EC number:1.14.14.17
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: | 1.14.14.17 |
|---|---|
| Description: | Squalene monooxygenase. |
| Alternative Name: |
Squalene-2,3-epoxidase. Squalene hydroxylase. Squalene epoxidase. |
3D structure
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.References
External Links
| UniProtKB Enzyme Link: | UniProtKB 1.14.14.17 |
| BRENDA Enzyme Link: | BRENDA 1.14.14.17 |
| KEGG Enzyme Link: | KEGG1.14.14.17 |
| BioCyc Enzyme Link: | BioCyc 1.14.14.17 |
| ExPASy Enzyme Link: | ExPASy1.14.14.17 |
| EC2PDB Enzyme Link: | EC2PDB 1.14.14.17 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.14.14.17 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.14.14.17 |
| IntEnz Enzyme Link: | IntEnz 1.14.14.17 |
| MEDLINE Enzyme Link: | MEDLINE 1.14.14.17 |
EC number:1.14.14.17
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:25282 | O2 + reduced [NADPH--hemoprotein reductase] + squalene = (S)-2,3-epoxysqualene + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](-[*:3])=[CH;+0:4]-[*:5].[*:6]-[N;H0;+0:7]1-[*:8]:[*:9]-[NH;+0:10]-[c;H0;+0:11](:[*:12]):[c;H0;+0:13]-1:[nH;+0:14]:[*:15].[O;H0;+0:16]=[O;H0;+0:17]>>[*:1]-[C;H0;+0:2]1(-[*:3])-[O;H0;+0:16]-[CH;+0:4]-1-[*:5].[*:6]-[n;H0;+0:7]1:[*:8]:[*:9]:[n;H0;+0:10]:[c;H0;+0:11](:[*:12])-[c;H0;+0:13]:1:[n;H0;+0:14]:[*:15].[OH2;+0:17] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| A comprehensive machine-readable view of the mammalian cholesterol biosynthesis pathway. | Mazein A, Watterson S, Hsieh WY, Griffiths WJ, Ghazal P | 2013 Jul 1 | 23583456 |
| Purification and properties of a soluble protein activator of rat liver squalene epoxidase. | Ferguson JB, Bloch K | 1977 Aug 10 | 885856 |
| Enzymatic properties of squalene epoxidase from Saccharomyces cerevisiae. | Satoh T, Horie M, Watanabe H, Tsuchiya Y, Kamei T | 1993 Apr | 8358382 |
| Solubilization and partial characterization of rat liver squalene epoxidase. | Ono T, Bloch K | 1975 Feb 25 | 234459 |
| Arabidopsis thaliana squalene epoxidase 1 is essential for root and seed development. | Rasbery JM, Shan H, LeClair RJ, Norman M, Matsuda SP, Bartel B | 2007 Jun 8 | 17426032 |
| Site-directed mutagenesis of conserved aromatic residues in rat squalene epoxidase. | Abe I, Abe T, Lou W, Masuoka T, Noguchi H | 2007 Jan 5 | 17112472 |
| Cytochrome P450 17alpha hydroxylase/17,20 lyase (CYP17) function in cholesterol biosynthesis: identification of squalene monooxygenase (epoxidase) activity associated with CYP17 in Leydig cells. | Liu Y, Yao ZX, Papadopoulos V | 2005 Jul | 15761033 |
| Photoaffinity labeling identifies the substrate-binding site of mammalian squalene epoxidase. | Lee HK, Zheng YF, Xiao XY, Bai M, Sakakibara J, Ono T, Prestwich GD | 2004 Feb 27 | 15013417 |
| Cloning, heterologous expression, and enzymological characterization of human squalene monooxygenase. | Laden BP, Tang Y, Porter TD | 2000 Feb 15 | 10666321 |