Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.3 Carboxy- and carbamoyltransferases
ID:2.1.3.12
Description:Decarbamoylnovobiocin carbamoyltransferase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.3.12
BRENDA Enzyme Link: BRENDA 2.1.3.12
KEGG Enzyme Link: KEGG2.1.3.12
BioCyc Enzyme Link: BioCyc 2.1.3.12
ExPASy Enzyme Link: ExPASy2.1.3.12
EC2PDB Enzyme Link: EC2PDB 2.1.3.12
ExplorEnz Enzyme Link: ExplorEnz 2.1.3.12
PRIAM enzyme-specific profiles Link: PRIAM 2.1.3.12
IntEnz Enzyme Link: IntEnz 2.1.3.12
MEDLINE Enzyme Link: MEDLINE 2.1.3.12
MSA:

2.1.3.12;

Phylogenetic Tree:

2.1.3.12;

Uniprot:
M-CSA:
RHEA:36659 carbamoyl phosphate + descarbamoylnovobiocin = novobiocin + phosphate
RULE(radius=1) [*:1]-[C;H0;+0:2](=[*:3])-[O;H0;+0:4]-[*:5].[*:6]-[OH;+0:7]>>[*:1]-[C;H0;+0:2](=[*:3])-[O;H0;+0:7]-[*:6].[*:5]-[OH;+0:4]
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