| Squalene methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.262 | ||||||||
| 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 methyltransferase ( EC 2.1.1.262, TMT-1, TMT-2) is an enzyme with systematic name S-adenosyl-L-methionine:squalene C-methyltransferase. [1] This enzyme catalyses the following chemical reaction
- 2 S-adenosyl-L-methionine + squalene 2 S-adenosyl-L-homocysteine + 3,22-dimethyl-1,2,23,24-tetradehydro-2,3,22,23-tetrahydrosqualene (overall reaction)
- (1a) S-adenosyl-L-methionine + squalene S-adenosyl-L-homocysteine + 3-methyl-1,2-didehydro-2,3-dihydrosqualene
- (1b) S-adenosyl-L-methionine + 3-methyl-1,2-didehydro-2,3-dihydrosqualene S-adenosyl-L-homocysteine + 3,22-dimethyl-1,2,23,24-tetradehydro-2,3,22,23-tetrahydrosqualene
There are two isoforms in the green alga Botryococcus braunii BOT22 that differ in their specificity .
References
- ^ Niehaus TD, Kinison S, Okada S, Yeo YS, Bell SA, Cui P, Devarenne TP, Chappell J (March 2012). "Functional identification of triterpene methyltransferases from Botryococcus braunii race B". The Journal of Biological Chemistry. 287 (11): 8163–73. doi: 10.1074/jbc.m111.316059. PMC 3318757. PMID 22241476.
External links
- Squalene+methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
