(S)-coclaurine-N-methyltransferase
| (S)-coclaurine-N-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.140 | ||||||||
| 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, (S)-coclaurine-N-methyltransferase (EC 2.1.1.140) is an enzyme that catalyzes the chemical reaction
S-adenosyl methionine (SAM) provides the methyl group for alkylation of (S)-coclaurine, which is converted to (S)-N-methylcoclaurine, with S-adenosylhomocysteine (SAH) as a by-product.[1][2]
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:(S)-coclaurine-N-methyltransferase. This enzyme participates in alkaloid biosynthesis.[3]
References
- ^ Enzyme 2.1.1.140 at KEGG Pathway Database.
- ^ Loeffler S, Deus-Neumann B, Zenk MH (1995). "S-Adenosyl-L-methionine: (S)-coclaurine-N-methyltransferase from Tinospora cordifolia". Phytochemistry. 38 (6): 1387–1395. Bibcode:1995PChem..38.1387L. doi:10.1016/0031-9422(94)00813-9.
- ^ Tian Y, Kong L, Li Q, Wang Y, Wang Y, An Z, Ma Y, Tian L, Duan B, Sun W, Gao R, Chen S, Xu Z (November 2024). "Structural diversity, evolutionary origin, and metabolic engineering of plant specialized benzylisoquinoline alkaloids". Natural Product Reports. 41 (11): 1787–1810. doi:10.1039/d4np00029c. PMID 39360417.