四川广播电视台招聘公告
| (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, a (S)-coclaurine-N-methyltransferase (EC 2.1.1.140) is an enzyme that catalyzes the chemical reaction
- S-adenosyl-L-methionine + (S)-coclaurine S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
Thus, the two substrates of this enzyme are S-adenosyl methionine and (S)-coclaurine, whereas its two products are S-adenosylhomocysteine and (S)-N-methylcoclaurine.
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.
References
[edit]- 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.
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