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

EC NUMBER
COMMENTARY hide
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 hide
ORGANISM
UNIPROT
LITERATURE
(3,5-dihydroxyphenyl)acetyl-CoA + O2 = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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Biosynthesis of vancomycin group antibiotics
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
show the reaction diagram
(3-hydroxyphenyl)acetyl-CoA + O2
(3-hydroxyphenyl)glyoxylate + CoA
show the reaction diagram
(4-hydroxyphenyl)acetyl-CoA + O2
(4-hydroxyphenyl)glyoxylate + CoA
show the reaction diagram
phenylacetyl-CoA + O2
phenylglyoxylate + CoA
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
IMAGE
0.0025 - 0.217
(3,5-dihydroxyphenyl)acetyl-CoA
0.851
(3-hydroxyphenyl)acetyl-CoA
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pH 7.5, 24°C, wild-type enzyme
0.0044
(5-hydroxyphenyl)acetyl-CoA
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pH 7.5, 24°C, wild-type enzyme
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0.0017 - 0.0026
O2
0.102 - 0.3
phenylacetyl-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.019 - 0.172
(3,5-dihydroxyphenyl)acetyl-CoA
0.222
(3-hydroxyphenyl)acetyl-CoA
Streptomyces toyocaensis
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pH 7.5, 24°C, wild-type enzyme
0.125
(5-hydroxyphenyl)acetyl-CoA
Streptomyces toyocaensis
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pH 7.5, 24°C, wild-type enzyme
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0.017 - 0.064
phenylacetyl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4 - 44
(3,5-dihydroxyphenyl)acetyl-CoA
197618
0.26
(3-hydroxyphenyl)acetyl-CoA
Streptomyces toyocaensis
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pH 7.5, 24°C, wild-type enzyme
197620
28.4
(5-hydroxyphenyl)acetyl-CoA
Streptomyces toyocaensis
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pH 7.5, 24°C, wild-type enzyme
197619
0.06 - 0.62
phenylacetyl-CoA
1147
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
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pH 7.4, 24°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
354000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homohexamer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop method at 20°C
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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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli BL21
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E189Q
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kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 3% compared to the wild-type activity
E255Q
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kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 96% compared to the wild-type activity
L237T
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kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 2% compared to the wild-type activity
Q299N
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kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 63% compared to the wild-type activity
R254K
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kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 1% compared to the wild-type activity
V425T
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kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 6% compared to the wild-type activity
V429T
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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
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E255Q
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kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 96% compared to the wild-type activity
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L237T
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kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 2% compared to the wild-type activity
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Q299N
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kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 63% compared to the wild-type activity
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R254K
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kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 1% compared to the wild-type activity
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V425T
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kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 6% compared to the wild-type activity
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V429T
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kcat/KM for (3,5-dihydroxyphenyl)acetyl-CoA is 3% compared to the wild-type activity
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