KEGG   ENZYME: 2.1.1.101
Entry
EC 2.1.1.101                Enzyme                                 
Name
macrocin O-methyltransferase;
macrocin methyltransferase;
S-adenosyl-L-methionine-macrocin O-methyltransferase;
MOMT (ambiguous);
tylF (gene name)
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
Sysname
S-adenosyl-L-methionine:macrocin 3'''-O-methyltransferase
Reaction(IUBMB)
S-adenosyl-L-methionine + macrocin = S-adenosyl-L-homocysteine + tylosin [RN:R02858]
Reaction(KEGG)
R02858
Substrate
S-adenosyl-L-methionine [CPD:C00019];
macrocin [CPD:C00744]
Product
S-adenosyl-L-homocysteine [CPD:C00021];
tylosin [CPD:C01457]
Comment
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.
History
EC 2.1.1.101 created 1992
Pathway
ec00522  Biosynthesis of 12-, 14- and 16-membered macrolides
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K15996  macrocin O-methyltransferase
Genes
STRM: M444_29905
Reference
1  [PMID:3170601]
  Authors
Bauer NJ, Kreuzman AJ, Dotzlaf JE, Yeh WK.
  Title
Purification, characterization, and kinetic mechanism of S-adenosyl-L-methionine:macrocin O-methyltransferase from Streptomyces fradiae.
  Journal
J Biol Chem 263:15619-25 (1988)
  Sequence
[ag:AAD41819]
Reference
2  [PMID:3170602]
  Authors
Kreuzman AJ, Turner JR, Yeh WK
  Title
Two distinctive O-methyltransferases catalyzing penultimate and terminal reactions of macrolide antibiotic (tylosin) biosynthesis. Substrate specificity, enzyme inhibition, and kinetic mechanism.
  Journal
J Biol Chem 263:15626-33 (1988)
  Sequence
[ag:AAD41819]
Other DBs
ExplorEnz - The Enzyme Database: 2.1.1.101
IUBMB Enzyme Nomenclature: 2.1.1.101
ExPASy - ENZYME nomenclature database: 2.1.1.101
BRENDA, the Enzyme Database: 2.1.1.101
CAS: 79468-52-3
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