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Enzyme Nomenclature
Information on EC 1.13.11.80 - (3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.13.11.80
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RECOMMENDED NAME
GeneOntology No.
(3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase
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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
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(3,5-dihydroxyphenyl)acetyl-CoA + O2 = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA
proposed catalytic mechanism
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(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; proposed catalytic mechanism
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(3,5-dihydroxyphenyl)acetyl-CoA + O2 = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
-
-
-
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
-
-
-
-
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
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
-
-
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
-
-
-
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
-
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
-
-
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
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(3,5-dihydroxyphenyl)acetyl-CoA i.e. 2-(3,5-dihydroxyphenyl)acetyl-CoA
-
-
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
-
-
-
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
-
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
-
-
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
-
(3,5-dihydroxyphenyl)acetyl-CoA i.e. 2-(3,5-dihydroxyphenyl)acetyl-CoA
-
-
?
(3-hydroxyphenyl)acetyl-CoA + O2
(3-hydroxyphenyl)glyoxylate + CoA
-
-
-
?
(3-hydroxyphenyl)acetyl-CoA + O2
(3-hydroxyphenyl)glyoxylate + CoA
-
-
-
?
(4-hydroxyphenyl)acetyl-CoA + O2
(4-hydroxyphenyl)glyoxylate + CoA
-
-
-
?
(4-hydroxyphenyl)acetyl-CoA + O2
(4-hydroxyphenyl)glyoxylate + CoA
-
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
G4V4T6
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
-
-
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
Q8KLK7
-
-
-
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
-
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
-
-
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
Q8KLK7
-
-
-
?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
-
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
-
-
?
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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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INHIBITORS
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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-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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pH 7.5, 24°C, wild-type enzyme
0.064
(3,5-dihydroxyphenyl)acetyl-CoA
-
pH 7.5, 24°C, mutant enzyme E189Q
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
0.069
(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
0.153
(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
0.4
(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
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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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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
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
-
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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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 6% compared to the wild-type activity
V429T
-
kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 3% compared to the wild-type activity
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
-
kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 6% compared to the wild-type activity
-
V429T
-
kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 3% compared to the wild-type activity
-
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LINKS TO OTHER DATABASES (specific for EC-Number 1.13.11.80)
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