| macrocin O-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.101 | ||||||||
| CAS no. | 79468-52-3 | ||||||||
| 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 macrocin O-methyltransferase (EC 2.1.1.101) is an enzyme that catalyzes the chemical reaction
- S-adenosyl-L-methionine + macrocin S-adenosyl-L-homocysteine + tylosin
Thus, the two substrates of this enzyme are S-adenosyl methionine and macrocin, whereas its two products are S-adenosylhomocysteine and tylosin.
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:macrocin 3"'-O-methyltransferase. Other names in common use include macrocin methyltransferase, and S-adenosyl-L-methionine-macrocin O-methyltransferase.
References
- Bauer NJ, Kreuzman AJ, Dotzlaf JE, Yeh WK (1988). "Purification, characterization, and kinetic mechanism of S-adenosyl-L-methionine:macrocin O-methyltransferase from Streptomyces fradiae". J. Biol. Chem. 263 (30): 15619–25. PMID 3170601.
- 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.
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