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Information on EC 1.13.11.80 - (3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase
for references in articles please use BRENDA:EC1.13.11.80
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EC Tree 1 Oxidoreductases
1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
1.13.11 With incorporation of two atoms of oxygen
1.13.11.80 (3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase
IUBMB Comments
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.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
DpgC, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DpgC
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(3,5-dihydroxyphenyl)acetyl-CoA + O2 = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA
Arg254 and Glu189 join to form a specific contact with one of the phenolic hydroxyls of the substrate, and this interaction plays a key role in both substrate recognition and catalysis
(3,5-dihydroxyphenyl)acetyl-CoA + O2 = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA
proposed catalytic mechanism
(3,5-dihydroxyphenyl)acetyl-CoA + O2 = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA
Arg254 and Glu189 join to form a specific contact with one of the phenolic hydroxyls of the substrate, and this interaction plays a key role in both substrate recognition and catalysis
-
-
(3,5-dihydroxyphenyl)acetyl-CoA + O2 = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA
proposed catalytic mechanism
-
-
(3,5-dihydroxyphenyl)acetyl-CoA + O2 = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(3,5-dihydroxyphenyl)acetyl-CoA:oxygen oxidoreductase
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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
Substrates: -
Products: -
Products: -
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
Substrates: the enzyme from the Actinobacterium Streptomyces toyocaensis is involved in the biosynthesis of (3,5-dihydroxyphenyl)glycine, a nonproteinogenic amino acid monomer in the glycopeptide antibiotic vancomycin
Products: -
Products: -
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
Substrates: -
Products: -
Products: -
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
Substrates: the enzyme is involved in the biosynthesis of vancomycin and teicoplanin antibiotics. (3,5-dihydroxyphenyl)acetyl-CoA i.e. 2-(3,5-dihydroxyphenyl)acetyl-CoA
Products: -
Products: -
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
Substrates: (3,5-dihydroxyphenyl)acetyl-CoA i.e. 2-(3,5-dihydroxyphenyl)acetyl-CoA
Products: -
Products: -
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
Substrates: -
Products: -
Products: -
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
Substrates: the enzyme is involved in the biosynthesis of vancomycin and teicoplanin antibiotics. (3,5-dihydroxyphenyl)acetyl-CoA i.e. 2-(3,5-dihydroxyphenyl)acetyl-CoA
Products: -
Products: -
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
Substrates: (3,5-dihydroxyphenyl)acetyl-CoA i.e. 2-(3,5-dihydroxyphenyl)acetyl-CoA
Products: -
Products: -
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA
Substrates: -
Products: -
Products: -
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA
Substrates: -
Products: -
Products: -
?
(3-hydroxyphenyl)acetyl-CoA + O2
(3-hydroxyphenyl)glyoxylate + CoA
Substrates: -
Products: -
Products: -
?
(3-hydroxyphenyl)acetyl-CoA + O2
(3-hydroxyphenyl)glyoxylate + CoA
Substrates: -
Products: -
Products: -
?
(4-hydroxyphenyl)acetyl-CoA + O2
(4-hydroxyphenyl)glyoxylate + CoA
Substrates: -
Products: -
Products: -
?
(4-hydroxyphenyl)acetyl-CoA + O2
(4-hydroxyphenyl)glyoxylate + CoA
Substrates: -
Products: -
Products: -
?
(5-hydroxyphenyl)acetyl-CoA + O2
2-(5-hydroxyphenyl)glyoxylate + CoA
Substrates: -
Products: -
Products: -
r
(5-hydroxyphenyl)acetyl-CoA + O2
2-(5-hydroxyphenyl)glyoxylate + CoA
Substrates: -
Products: -
Products: -
r
phenylacetyl-CoA + O2
phenylglyoxylate + CoA
Substrates: -
Products: -
Products: -
?
phenylacetyl-CoA + O2
phenylglyoxylate + CoA
Substrates: -
Products: -
Products: -
?
phenylacetyl-CoA + O2
phenylglyoxylate + CoA
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
Substrates: the enzyme from the Actinobacterium Streptomyces toyocaensis is involved in the biosynthesis of (3,5-dihydroxyphenyl)glycine, a nonproteinogenic amino acid monomer in the glycopeptide antibiotic vancomycin
Products: -
Products: -
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
Substrates: -
Products: -
Products: -
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
Substrates: the enzyme is involved in the biosynthesis of vancomycin and teicoplanin antibiotics. (3,5-dihydroxyphenyl)acetyl-CoA i.e. 2-(3,5-dihydroxyphenyl)acetyl-CoA
Products: -
Products: -
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
Substrates: -
Products: -
Products: -
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
Substrates: the enzyme is involved in the biosynthesis of vancomycin and teicoplanin antibiotics. (3,5-dihydroxyphenyl)acetyl-CoA i.e. 2-(3,5-dihydroxyphenyl)acetyl-CoA
Products: -
Products: -
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA
Substrates: -
Products: -
Products: -
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]methyl (3R)-4-([3-[(2-[[(2,5-dihydroxyphenyl)acetyl]amino]ethyl)amino]-3-oxopropyl]amino)-3-hydroxy-2,2-dimethyl-4-oxobutyl dihydrogen diphosphate
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.851
(3-hydroxyphenyl)acetyl-CoA
pH 7.5, 24°C, wild-type enzyme
0.0044
(5-hydroxyphenyl)acetyl-CoA
pH 7.5, 24°C, wild-type enzyme
0.0025
(3,5-dihydroxyphenyl)acetyl-CoA
pH 7.5, 24°C, mutant enzyme Q299N
0.0036
(3,5-dihydroxyphenyl)acetyl-CoA
pH 7.5, 24°C, mutant enzyme E255Q
0.0039
(3,5-dihydroxyphenyl)acetyl-CoA
pH 7.5, 24°C, wild-type enzyme
0.064
(3,5-dihydroxyphenyl)acetyl-CoA
pH 7.5, 24°C, mutant enzyme E189Q
0.125
(3,5-dihydroxyphenyl)acetyl-CoA
mutant enzyme A319C, at pH 7.5 and 24°C
0.217
(3,5-dihydroxyphenyl)acetyl-CoA
pH 7.5, 24°C, mutant enzyme R254K
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.222
(3-hydroxyphenyl)acetyl-CoA
pH 7.5, 24°C, wild-type enzyme
0.125
(5-hydroxyphenyl)acetyl-CoA
pH 7.5, 24°C, wild-type enzyme
0.069
(3,5-dihydroxyphenyl)acetyl-CoA
pH 7.5, 24°C, mutant enzyme Q299N
0.085
(3,5-dihydroxyphenyl)acetyl-CoA
pH 7.5, 24°C, mutant enzyme E189Q
0.086
(3,5-dihydroxyphenyl)acetyl-CoA
pH 7.5, 24°C, mutant enzyme R254K
0.095
(3,5-dihydroxyphenyl)acetyl-CoA
mutant enzyme A319C, at pH 7.5 and 24°C
0.153
(3,5-dihydroxyphenyl)acetyl-CoA
pH 7.5, 24°C, mutant enzyme E255Q
0.172
(3,5-dihydroxyphenyl)acetyl-CoA
pH 7.5, 24°C, wild-type enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.26
(3-hydroxyphenyl)acetyl-CoA
pH 7.5, 24°C, wild-type enzyme
28.4
(5-hydroxyphenyl)acetyl-CoA
pH 7.5, 24°C, wild-type enzyme
0.4
(3,5-dihydroxyphenyl)acetyl-CoA
pH 7.5, 24°C, mutant enzyme R254K
1.3
(3,5-dihydroxyphenyl)acetyl-CoA
pH 7.5, 24°C, mutant enzyme E189Q
27.6
(3,5-dihydroxyphenyl)acetyl-CoA
pH 7.5, 24°C, mutant enzyme Q299N
42.5
(3,5-dihydroxyphenyl)acetyl-CoA
pH 7.5, 24°C, mutant enzyme E255Q
44
(3,5-dihydroxyphenyl)acetyl-CoA
pH 7.5, 24°C, wild-type enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0027
[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]methyl (3R)-4-([3-[(2-[[(2,5-dihydroxyphenyl)acetyl]amino]ethyl)amino]-3-oxopropyl]amino)-3-hydroxy-2,2-dimethyl-4-oxobutyl dihydrogen diphosphate
pH 7.4, 24°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
the enzyme from the actinobacterium Streptomyces toyocaensis is involved in the biosynthesis of (3,5-dihydroxyphenyl)glycine, a nonproteinogenic amino acid monomer in the glycopeptide antibiotic vancomycin
physiological function
the enzyme is involved in the biosynthesis of vancomycin and teicoplanin antibiotics
physiological function
-
the enzyme is involved in the biosynthesis of vancomycin and teicoplanin antibiotics
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A2S6QW08_9PROT
466
0
51489
TrEMBL
-
A0A2S6RC95_9PROT
460
0
53182
TrEMBL
-
A0A2S6RXG2_9PROT
482
0
52939
TrEMBL
-
A0A2S6RG61_9PROT
468
0
53821
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homohexamer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of the enzyme in complex with a bound substrate mimic, crystallized by the hanging drop method at 20°C, 2.75 A resolution
wild type and mutant enzymes A319C and V425T in complex with substrate, hanging drop vapor diffusion method, using 140 mM ammonium acetate, 14% (w/v) PEG 4000, 100 mM sodium citrate pH 5.6
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A319C
the catalytic efficiency of the mutant is about 1.5% of that of the wild type protein
E189Q
kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 3% compared to the wild-type activity
E255Q
kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 96% compared to the wild-type activity
L237T
kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 2% compared to the wild-type activity
Q299N
kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 63% compared to the wild-type activity
R254K
kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 1% compared to the wild-type activity
V425T
V429T
kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 3% compared to the wild-type activity
A319C
-
the catalytic efficiency of the mutant is about 1.5% of that of the wild type protein
-
E189Q
-
kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 3% compared to the wild-type activity
-
E255Q
-
kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 96% compared to the wild-type activity
-
L237T
-
kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 2% compared to the wild-type activity
-
Q299N
-
kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 63% compared to the wild-type activity
-
R254K
-
kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 1% compared to the wild-type activity
-
V425T
V429T
-
kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 3% compared to the wild-type activity
-
V425T
the mutant shows reduced activity compared to the wild type enzyme
V425T
kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 6% compared to the wild-type activity
V425T
-
kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 6% compared to the wild-type activity
-
V425T
-
the mutant shows reduced activity compared to the wild type enzyme
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fielding, E.N.; Widboom, P.F.; Bruner, S.D.
Substrate recognition and catalysis by the cofactor-independent dioxygenase DpgC
Biochemistry
46
13994-4000
2007
Streptomyces toyocaensis (Q8KLK7), Streptomyces toyocaensis A47934 (Q8KLK7)
brenda
Tseng, C.C.; Vaillancourt, F.H.; Bruner, S.D.; Walsh, C.T.
DpgC is a metal- and cofactor-free 3,5-dihydroxyphenylacetyl-CoA 1,2-dioxygenase in the vancomycin biosynthetic pathway
Chem. Biol.
11
1195-1203
2004
Amycolatopsis orientalis (G4V4T6)
brenda
Widboom, P.F.; Fielding, E.N.; Liu, Y.; Bruner, S.D.
Structural basis for cofactor-independent dioxygenation in vancomycin biosynthesis
Nature
447
342-345
2007
Streptomyces toyocaensis (Q8KLK7), Streptomyces toyocaensis A47934 (Q8KLK7)
brenda
Chen, H.; Tseng, C.C.; Hubbard, B.K.; Walsh, C.T.
Glycopeptide antibiotic biosynthesis: enzymatic assembly of the dedicated amino acid monomer (S)-3,5-dihydroxyphenylglycine
Proc. Natl. Acad. Sci. USA
98
14901-14906
2001
Amycolatopsis orientalis (G4V4T6)
brenda
Li, K.; Fielding, E.N.; Condurso, H.L.; Bruner, S.D.
Probing the structural basis of oxygen binding in a cofactor-independent dioxygenase
Acta Crystallogr. Sect. D
73
573-580
2017
Streptomyces toyocaensis (Q8KLK7), Streptomyces toyocaensis A47934 (Q8KLK7)
brenda
EXTERNAL LINKS (specific for EC-Number 1.13.11.80)
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Release 2023.1 (January 2023)
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