| Entry |
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| Name |
demethyldecarbamoylnovobiocin O-methyltransferase;
NovP
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| Class |
Transferases;
Transferring one-carbon groups;
Methyltransferases
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| Sysname |
S-adenosyl-L-methionine:demethyldecarbamoylnovobiocin 4''-O-methyltransferase
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| Reaction(IUBMB) |
S-adenosyl-L-methionine + demethyldecarbamoylnovobiocin = S-adenosyl-L-homocysteine + decarbamoylnovobiocin [RN: R06771]
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| Reaction(KEGG) |
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| Substrate |
S-adenosyl-L-methionine [CPD: C00019];
demethyldecarbamoylnovobiocin [CPD: C12475]
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| Product |
S-adenosyl-L-homocysteine [CPD: C00021];
decarbamoylnovobiocin [CPD: C12476]
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| Comment |
The enzyme is involved in the biosynthesis of the aminocoumarin antibiotic novobiocin.
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| History |
EC 2.1.1.285 created 2013
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| Pathway |
| ec01110 | Biosynthesis of secondary metabolites |
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| Orthology |
| K12712 | demethyldecarbamoylnovobiocin O-methyltransferase |
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| Genes |
| ACTU: | Actkin_05240(mycF_2) |
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| Reference |
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| Authors |
Freel Meyers CL, Oberthur M, Xu H, Heide L, Kahne D, Walsh CT |
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| Title |
Characterization of NovP and NovN: completion of novobiocin biosynthesis by sequential tailoring of the noviosyl ring. |
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| Journal |
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| Sequence |
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| Reference |
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| Authors |
Gomez Garcia I, Stevenson CE, Uson I, Freel Meyers CL, Walsh CT, Lawson DM |
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| Title |
The crystal structure of the novobiocin biosynthetic enzyme NovP: the first representative structure for the TylF O-methyltransferase superfamily. |
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| Journal |
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| Sequence |
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| Other DBs |
| ExPASy - ENZYME nomenclature database: | 2.1.1.285 |
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