Entry |
|
Name |
demethyldecarbamoylnovobiocin O-methyltransferase;
NovP
|
Class |
Transferases;
Transferring one-carbon groups;
Methyltransferases
|
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 |
ec01110 | Biosynthesis of secondary metabolites |
|
Orthology |
K12712 | demethyldecarbamoylnovobiocin O-methyltransferase |
|
Genes |
ACTU: | Actkin_05240(mycF_2) |
|
Reference |
|
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 |
|
Sequence |
|
Reference |
|
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 |
|
Sequence |
|
Other DBs |
ExPASy - ENZYME nomenclature database: | 2.1.1.285 |
|
LinkDB |
|