Entry
Name
(3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase;
DpgC
Class
Oxidoreductases;
Acting on single donors with incorporation of molecular oxygen (oxygenases);
With incorporation of two atoms of oxygen
BRITE hierarchy
Sysname
(3,5-dihydroxyphenyl)acetyl-CoA:oxygen oxidoreductase
Reaction(IUBMB)
(3,5-dihydroxyphenyl)acetyl-CoA + O2 = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA [RN:
R06624 ]
Reaction(KEGG)
Substrate
Product
2-(3,5-dihydroxyphenyl)-2-oxoacetate [CPD:
C12325 ];
CoA [CPD:
C00010 ]
Comment
The enzyme, characterized from bacteria Streptomyces toyocaensis and Amycolatopsis orientalis, is involved in the biosynthesis of (3,5-dihydroxyphenyl)glycine, a component of the glycopeptide antibiotic vancomycin.
History
EC 1.13.11.80 created 2015
Pathway
ec01055 Biosynthesis of vancomycin group antibiotics
ec01110 Biosynthesis of secondary metabolites
Orthology
K16427 (3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase
Genes
NTP : CRH09_30860 CRH09_31735
NAD : NCTC11293_04863(caiD_11)
SRC : M271_00275 M271_09135
SPRI : SPRI_0192 SPRI_7161
SKA : CP970_02985 CP970_09660
KUT : JJ691_30280 JJ691_70270(dpgC)
AOU : ACTOB_006416 ACTOB_006455
» show all
Taxonomy
Reference
Authors
Chen H, Tseng CC, Hubbard BK, Walsh CT
Title
Glycopeptide antibiotic biosynthesis: enzymatic assembly of the dedicated amino acid monomer (S)-3,5-dihydroxyphenylglycine.
Journal
Reference
Authors
Widboom PF, Fielding EN, Liu Y, Bruner SD.
Title
Structural basis for cofactor-independent dioxygenation in vancomycin biosynthesis.
Journal
Reference
Authors
Fielding EN, Widboom PF, Bruner SD
Title
Substrate recognition and catalysis by the cofactor-independent dioxygenase DpgC.
Journal
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