KEGG   ENZYME: 2.1.1.285Help
Entry
EC 2.1.1.285                Enzyme                                 

Name
demethyldecarbamoylnovobiocin O-methyltransferase;
NovP
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
BRITE hierarchy
Sysname
S-adenosyl-L-methionine:demethyldecarbamoylnovobiocin 4''-O-methyltransferase
Reaction(IUBMB)
S-adenosyl-L-methionine + demethyldecarbamoylnovobiocin = S-adenosyl-L-homocysteine + decarbamoylnovobiocin [RN:R06771]
Reaction(KEGG)
Substrate
S-adenosyl-L-methionine [CPD:C00019];
demethyldecarbamoylnovobiocin [CPD:C12475]
Product
S-adenosyl-L-homocysteine [CPD:C00021];
decarbamoylnovobiocin [CPD:C12476]
Comment
The enzyme is involved in the biosynthesis of the aminocoumarin antibiotic novobiocin.
History
EC 2.1.1.285 created 2013
Pathway
Novobiocin biosynthesis
Biosynthesis of antibiotics
Orthology
K12712  
demethyldecarbamoylnovobiocin O-methyltransferase
Reference
1  [PMID:14694473]
  Authors
Freel Meyers CL, Oberthur M, Xu H, Heide L, Kahne D, Walsh CT
  Title
Characterization of NovP and NovN: completion of novobiocin biosynthesis by sequential tailoring of the noviosyl ring.
  Journal
Angew. Chem. Int. Ed. Engl. 43 (2004) 67-70.
  Sequence
Reference
2  [PMID:19857499]
  Authors
Gomez Garcia I, Stevenson CE, Uson I, Freel Meyers CL, Walsh CT, Lawson DM
  Title
The crystal structure of the novobiocin biosynthetic enzyme NovP: the first representative structure for the TylF O-methyltransferase superfamily.
  Journal
J. Mol. Biol. 395 (2010) 390-407.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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