Squalene—-hopanol cyclase
| Squalene—-hopanol cyclase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.2.1.129 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Squalene—-hopanol cyclase (EC 4.2.1.129, squalene—-hopene cyclase) is an enzyme with systematic name hopan-22-ol hydro-lyase.[1][2] This enzyme catalyses the following chemical reaction
- hopan-22-ol squalene + H2O
The enzyme produces the cyclization products hopene and hopanol.
References
- ↑ Hoshino, T.; Nakano, S.; Kondo, T.; Sato, T.; Miyoshi, A. (2004). "Squalene-hopene cyclase: final deprotonation reaction, conformational analysis for the cyclization of (3R,S)-2,3-oxidosqualene and further evidence for the requirement of an isopropylidene moiety both for initiation of the polycyclization cascade and for the formation of the 5-membered E-ring". Org Biomol Chem. 2: 1456–1470. doi:10.1039/b401172d. PMID 15136801.
- ↑ Sato, T.; Kouda, M.; Hoshino, T. (2004). "Site-directed mutagenesis experiments on the putative deprotonation site of squalene-hopene cyclase from Alicyclobacillus acidocaldarius". Biosci. Biotechnol. Biochem. 68: 728–738. doi:10.1271/bbb.68.728. PMID 15056909.
External links
- Squalene---hopanol+cyclase at the US National Library of Medicine Medical Subject Headings (MeSH)
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