Squalene methyltransferase
Appearance
Squalene methyltransferase | |||||||||
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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 | ||||||||
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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
[edit]- ^ 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
[edit]- Squalene+methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)