EC number:2.1.1.285

Enzyme

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EC Tree
     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.285
Description:Demethyldecarbamoylnovobiocin O-methyltransferase.
Cath: 3.40.50.150;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.285
BRENDA Enzyme Link: BRENDA 2.1.1.285
KEGG Enzyme Link: KEGG2.1.1.285
BioCyc Enzyme Link: BioCyc 2.1.1.285
ExPASy Enzyme Link: ExPASy2.1.1.285
EC2PDB Enzyme Link: EC2PDB 2.1.1.285
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.285
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.285
IntEnz Enzyme Link: IntEnz 2.1.1.285
MEDLINE Enzyme Link: MEDLINE 2.1.1.285

EC number:2.1.1.285

MSA:

2.1.1.285;
Phylogenetic Tree:

2.1.1.285;
Uniprot:
M-CSA:
RHEA:36655 desmethyldescarbamoylnovobiocin + S-adenosyl-L-methionine = descarbamoylnovobiocin + H(+) + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[O;H0;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The crystal structure of the novobiocin biosynthetic enzyme NovP: the first representative structure for the TylF O-methyltransferase superfamily.Gómez García I, Stevenson CE, Usón I, Freel Meyers CL, Walsh CT, Lawson DM2010 Jan 1519857499
Characterization of NovP and NovN: completion of novobiocin biosynthesis by sequential tailoring of the noviosyl ring.Freel Meyers CL, Oberthür M, Xu H, Heide L, Kahne D, Walsh CT2004 Jan14694473