Squalene—-hopanol cyclase
| Squalene—hopanol cyclase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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
[edit]- ^ Hoshino T, Nakano S, Kondo T, Sato T, Miyoshi A (May 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". Organic & Biomolecular Chemistry. 2 (10): 1456–70. doi:10.1039/b401172d. PMID 15136801.
- ^ Sato T, Kouda M, Hoshino T (March 2004). "Site-directed mutagenesis experiments on the putative deprotonation site of squalene-hopene cyclase from Alicyclobacillus acidocaldarius". Bioscience, Biotechnology, and Biochemistry. 68 (3): 728–38. doi:10.1271/bbb.68.728. PMID 15056909.
External links
[edit]- Squalene---hopanol+cyclase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
