| cycloartenol 24-C-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.142 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a cycloartenol 24-C-methyltransferase (EC 2.1.1.142) is an enzyme that catalyzes the chemical reaction
- S-adenosyl-L-methionine + cycloartenol S-adenosyl-L-homocysteine + (24R)-24-methylcycloart-25-en-3beta-ol
Thus, the two substrates of this enzyme are S-adenosyl methionine and cycloartenol, whereas its two products are S-adenosylhomocysteine and (24R)-24-methylcycloart-25-en-3beta-ol.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:cycloartenol 24-C-methyltransferase. This enzyme is also called sterol C-methyltransferase.
References
- Mangla AT, Nes WD (2000). "Sterol C-methyl transferase from Prototheca wickerhamii mechanism, sterol specificity and inhibition". Bioorg. Med. Chem. 8 (5): 925–36. doi:10.1016/S0968-0896(00)00040-7. PMID 10882005.
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