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
ec00401  Novobiocin biosynthesis
ec01100  Metabolic pathways
ec01130  Biosynthesis of antibiotics
Orthology
K12712  demethyldecarbamoylnovobiocin O-methyltransferase
Genes
NGV: CDO52_02225
Taxonomy
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 43:67-70 (2004)
DOI:10.1002/anie.200352626
  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 395:390-407 (2010)
DOI:10.1016/j.jmb.2009.10.045
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 2.1.1.285
IUBMB Enzyme Nomenclature: 2.1.1.285
ExPASy - ENZYME nomenclature database: 2.1.1.285
BRENDA, the Enzyme Database: 2.1.1.285

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