Botryococcene C-methyltransferase
From Wikipedia the free encyclopedia
| Botryococcene C-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.263 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Botryococcene C-methyltransferase (EC 2.1.1.263, TMT-3) is an enzyme with systematic name S-adenosyl-L-methionine:botryococcene C-methyltransferase.[1]
Function[edit]
This enzyme catalyses the following chemical reaction:
- 2 S-adenosyl-L-methionine + C30 botryococcene 2 S-adenosyl-L-homocysteine + 3,20-dimethyl-1,2,21,22-tetradehydro-2,3,20,21-tetrahydrobotryococcene (overall reaction)
- (1a) S-adenosyl-L-methionine + C30 botryococcene S-adenosyl-L-homocysteine + 3-methyl-1,2-didehydro-2,3-dihydrobotryococcene
- (1b) S-adenosyl-L-methionine + 3-methyl-1,2-didehydro-2,3-dihydrobotryococcene S-adenosyl-L-homocysteine + 3,20-dimethyl-1,2,21,22-tetradehydro-2,3,20,21-tetrahydrobotryococcene
- (2a) S-adenosyl-L-methionine + C30 botryococcene S-adenosyl-L-homocysteine + 20-methyl-21,22-didehydro-20,21-dihydrobotryococcene
- (2b) S-adenosyl-L-methionine + 20-methyl-21,22-didehydro-20,21-dihydrobotryococcene S-adenosyl-L-homocysteine + 3,20-dimethyl-1,2,21,22-tetradehydro-2,3,20,21-tetrahydrobotryococcene
This enzyme is isolated from the green alga Botryococcus braunii BOT22.
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]
- Botryococcene+C-methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
