Squalene monooxygenase
| Squalene monooxygenase | ||
|---|---|---|
| Properties of human protein | ||
| Mass / length primary structure | 574 amino acids | |
| Cofactor | FAD | |
| Identifier | ||
| Gene name | SQLE | |
| External IDs | ||
| Enzyme classification | ||
| EC, category | 1.14.99.7 , monooxygenase | |
| Response type | Addition of an oxygen atom | |
| Substrate | Squalene + red.Acc./H 2 + O 2 | |
| Products | Squalene epoxide + ox.Acc. + H 2 O | |
| Occurrence | ||
| Parent taxon | Eukaryotes , few bacteria | |
The squalene monooxygenase (SE) is the enzyme that the oxidation of squalene to S -squalene-2,3-epoxide catalyzed . This reaction takes place in eukaryotes and some bacteria ; in animals it is part of cholesterol biosynthesis . In humans, SE is localized in the microsomes .
Catalyzed reaction
+ A H 2 + O 2 ⇔ -Squalen-2,3-epoxid.svg)
+ A + H 2 O
Squalene is oxidized to S- squalene-2,3-epoxide and the acceptor is dehydrated.
Individual evidence
- ↑ a b InterPro entry
- ↑ Lamb DC, Jackson CJ, Warrilow AG, Manning NJ, Kelly DE, Kelly SL: Lanosterol biosynthesis in the prokaryote Methylococcus capsulatus: insight into the evolution of sterol biosynthesis . In: Mol. Biol. Evol. . 24, No. 8, August 2007, pp. 1714-21. doi : 10.1093 / molbev / msm090 . PMID 17567593 .
- ↑ UniProt Q14534
Web links
Wikibooks: Biochemistry and Pathobiochemistry: Cholesterol Biosynthesis - Learning and Teaching Materials
- Jassal / reactome: Squalene is oxidized to its epoxide