EC number:1.14.11.52

Enzyme

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EC Tree
     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
ID:1.14.11.52
Description:Validamycin A dioxygenase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.11.52
BRENDA Enzyme Link: BRENDA 1.14.11.52
KEGG Enzyme Link: KEGG1.14.11.52
BioCyc Enzyme Link: BioCyc 1.14.11.52
ExPASy Enzyme Link: ExPASy1.14.11.52
EC2PDB Enzyme Link: EC2PDB 1.14.11.52
ExplorEnz Enzyme Link: ExplorEnz 1.14.11.52
PRIAM enzyme-specific profiles Link: PRIAM 1.14.11.52
IntEnz Enzyme Link: IntEnz 1.14.11.52
MEDLINE Enzyme Link: MEDLINE 1.14.11.52

EC number:1.14.11.52

MSA:

1.14.11.52;
Phylogenetic Tree:

1.14.11.52;
Uniprot:
M-CSA:
RHEA:48752 2-oxoglutarate + O2 + validamycin A = CO2 + H(+) + succinate + validamycin B
RULE(radius=1) [*:1]-[CH2;+0:2]-[*:3].[*:4]=[C;H0;+0:5](-[OH;+0:6])-[C;H0;+0:7](=[*:8])-[*:9].[O;H0;+0:10]=[O;H0;+0:11]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:10].[*:8]=[C;H0;+0:7](-[*:9])-[OH;+0:11].[*:4]=[C;H0;+0:5]=[O;H0;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The α-ketoglutarate/Fe(II)-dependent dioxygenase VldW is responsible for the formation of validamycin B.Almabruk KH, Asamizu S, Chang A, Varghese SG, Mahmud T2012 Oct 1522961651