KEGG   ORTHOLOGY: K15996
Entry
K15996                      KO                                     
Symbol
tylF
Name
macrocin O-methyltransferase [EC:2.1.1.101]
Pathway
map00522  Biosynthesis of 12-, 14- and 16-membered macrolides
map01100  Metabolic pathways
map01110  Biosynthesis of secondary metabolites
Module
M00773  Tylosin biosynthesis, methylmalonyl-CoA + malonyl-CoA => tylactone => tylosin
Reaction
R02858  S-adenosyl-L-methionine:macrocin 3'''-O-methyltransferase
Brite
KEGG Orthology (KO) [BR:ko00001]
 09100 Metabolism
  09109 Metabolism of terpenoids and polyketides
   00522 Biosynthesis of 12-, 14- and 16-membered macrolides
    K15996  tylF; macrocin O-methyltransferase
 09180 Brite Hierarchies
  09181 Protein families: metabolism
   01008 Polyketide biosynthesis proteins
    K15996  tylF; macrocin O-methyltransferase
Enzymes [BR:ko01000]
 2. Transferases
  2.1  Transferring one-carbon groups
   2.1.1  Methyltransferases
    2.1.1.101  macrocin O-methyltransferase
     K15996  tylF; macrocin O-methyltransferase
Polyketide biosynthesis proteins [BR:ko01008]
 Polyketide tailoring proteins
  Methylase
   K15996  tylF; macrocin O-methyltransferase
Other DBs
GO: 0030769
Genes
STRM: M444_29905
AG: AAD41819(tylF)
Reference
  Authors
Fouces R, Mellado E, Diez B, Barredo JL
  Title
The tylosin biosynthetic cluster from Streptomyces fradiae: genetic organization of the left region.
  Journal
Microbiology 145 ( Pt 4):855-68 (1999)
DOI:10.1099/13500872-145-4-855
Reference
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
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