In enzymology, a demethylmacrocin O-methyltransferase (EC 2.1.1.102) is an enzyme that catalyzes the chemical reaction
| demethylmacrocin O-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.102 | ||||||||
| CAS no. | 120313-64-6 | ||||||||
| 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 | ||||||||
| |||||||||
- S-adenosyl-L-methionine + demethylmacrocin S-adenosyl-L-homocysteine + macrocin
Thus, the two substrates of this enzyme are S-adenosyl methionine and demethylmacrocin, whereas its two products are S-adenosylhomocysteine and macrocin.
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:demethylmacrocin 2"'-O-methyltransferase. This enzyme is also called demethylmacrocin methyltransferase. This enzyme participates in biosynthesis of 12-, 14- and 16-membered macrolides.
References
edit- Kreuzman AJ, Turner JR, Yeh WK (1988). "Two distinctive O-methyltransferases catalyzing penultimate and terminal reactions of macrolide antibiotic (tylosin) biosynthesis Substrate specificity, enzyme inhibition, and kinetic mechanism". J. Biol. Chem. 263 (30): 15626–33. PMID 3170602.
