| EC |
2.1.1.101 |
| Accepted name: |
macrocin O-methyltransferase |
| Reaction: |
S-adenosyl-L-methionine + macrocin = S-adenosyl-L-homocysteine + tylosin |
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For diagram of tylosin biosynthesis, click here |
| Other name(s): |
macrocin methyltransferase; S-adenosyl-L-methionine-macrocin O-methyltransferase; MOMT (ambiguous); tylF (gene name) |
| Systematic name: |
S-adenosyl-L-methionine:macrocin 3′′′-O-methyltransferase |
| Comments: |
Requires Mg2+, Mn2+ or Co2+. The 3-hydroxy group of the 2-O-methyl-6-deoxy-D-allose moiety in the macrolide antibiotic macrosin acts as methyl acceptor, generating tylosin, another macrolide antibiotic. Isolated from the bacterium Streptomyces fradiae. Not identical with EC 2.1.1.102, demethylmacrocin O-methyltransferase. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 79468-52-3 |
| References: |
| 1. |
Bauer, N.J., Kreuzman, A.J., Dotzlaf, J.E. and Yeh, W.-K. Purification, characterization, and kinetic mechanism of S-adenosyl-L-methionine:macrocin O-methyltransferase from Streptomyces fradiae. J. Biol. Chem. 263 (1988) 15619–15625. [PMID: 3170601] |
| 2. |
Kreuzman, A.J., Turner, J.R. and Yeh, W.-K. 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 (1988) 15626–15633. [PMID: 3170602] |
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| [EC 2.1.1.101 created 1992] |
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