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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:EC1.13.11.80Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The enzyme appears in viruses and cellular organisms
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(3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase
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(3,5-dihydroxyphenyl)acetyl-CoA + O2 = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA
(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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Biosynthesis of vancomycin group antibiotics
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Biosynthesis of antibiotics
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(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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DpgC
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UniProt
brenda
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UniProt
brenda
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UniProt
brenda
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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
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the enzyme is involved in the biosynthesis of vancomycin and teicoplanin antibiotics
physiological function
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the enzyme is involved in the biosynthesis of vancomycin and teicoplanin antibiotics
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(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
(3-hydroxyphenyl)acetyl-CoA + O2
(3-hydroxyphenyl)glyoxylate + CoA
(4-hydroxyphenyl)acetyl-CoA + O2
(4-hydroxyphenyl)glyoxylate + CoA
phenylacetyl-CoA + O2
phenylglyoxylate + CoA
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
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(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
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(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
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(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
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(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
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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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(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
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?
(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
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(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
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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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(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
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(3-hydroxyphenyl)acetyl-CoA + O2
(3-hydroxyphenyl)glyoxylate + CoA
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(3-hydroxyphenyl)acetyl-CoA + O2
(3-hydroxyphenyl)glyoxylate + CoA
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(4-hydroxyphenyl)acetyl-CoA + O2
(4-hydroxyphenyl)glyoxylate + CoA
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(4-hydroxyphenyl)acetyl-CoA + O2
(4-hydroxyphenyl)glyoxylate + CoA
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phenylacetyl-CoA + O2
phenylglyoxylate + CoA
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phenylacetyl-CoA + O2
phenylglyoxylate + CoA
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phenylacetyl-CoA + O2
phenylglyoxylate + CoA
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(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
(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
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(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
Q8KLK7
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(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
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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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(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
Q8KLK7
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(3,5-dihydroxyphenyl)acetyl-CoA + O2
(3,5-dihydroxyphenyl)glyoxylate + CoA
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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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additional information
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cofactor-free enzyme
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additional information
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no cofactor detected
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additional information
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metal-free enzyme
additional information
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not dependent on a metal ion
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[(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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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
0.102 - 0.3
phenylacetyl-CoA
0.0025
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.5, 24°C, mutant enzyme Q299N
0.0036
(3,5-dihydroxyphenyl)acetyl-CoA
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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
0.0039
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.4, 24°C
0.006
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.5, 24°C
0.0138
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.4, 24°C
0.0147
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.4, 24°C
0.058
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.4, 24°C
0.064
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.5, 24°C, mutant enzyme E189Q
0.217
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.5, 24°C, mutant enzyme R254K
0.0017
O2
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pH 7.4, 24°C
0.102
phenylacetyl-CoA
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pH 7.5, 24°C, wild-type enzyme
0.3
phenylacetyl-CoA
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pH 7.5, 24°C
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0.019 - 0.172
(3,5-dihydroxyphenyl)acetyl-CoA
0.222
(3-hydroxyphenyl)acetyl-CoA
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pH 7.5, 24°C, wild-type enzyme
0.125
(5-hydroxyphenyl)acetyl-CoA
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pH 7.5, 24°C, wild-type enzyme
0.017 - 0.064
phenylacetyl-CoA
0.019
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.4, 24°C
0.037
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.4, 24°C
0.05
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.4, 24°C
0.069
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.5, 24°C, mutant enzyme Q299N
0.085
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.5, 24°C, mutant enzyme E189Q
0.086
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.5, 24°C, mutant enzyme R254K
0.153
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.5, 24°C, mutant enzyme E255Q
0.17
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.5, 24°C
0.172
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.5, 24°C, wild-type enzyme
0.172
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.4, 24°C
0.017
phenylacetyl-CoA
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pH 7.5, 24°C
0.064
phenylacetyl-CoA
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pH 7.5, 24°C, wild-type enzyme
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0.4 - 44
(3,5-dihydroxyphenyl)acetyl-CoA
0.26
(3-hydroxyphenyl)acetyl-CoA
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pH 7.5, 24°C, wild-type enzyme
28.4
(5-hydroxyphenyl)acetyl-CoA
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pH 7.5, 24°C, wild-type enzyme
0.06 - 0.62
phenylacetyl-CoA
0.4
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.5, 24°C, mutant enzyme R254K
0.86
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.4, 24°C
1.3
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.5, 24°C, mutant enzyme E189Q
1.3
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.4, 24°C
2.7
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.4, 24°C
27.6
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.5, 24°C, mutant enzyme Q299N
28.3
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.5, 24°C
42.5
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.5, 24°C, mutant enzyme E255Q
44
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.5, 24°C, wild-type enzyme
44
(3,5-dihydroxyphenyl)acetyl-CoA
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pH 7.4, 24°C
0.06
phenylacetyl-CoA
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pH 7.5, 24°C
0.62
phenylacetyl-CoA
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pH 7.5, 24°C, wild-type enzyme
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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
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7.5
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assay at
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24
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assay at
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Streptomyces toyocaensis;
Q8KLK7
Streptomyces toyocaensis;
Q8KLK7
Streptomyces toyocaensis;
Q8KLK7
Streptomyces toyocaensis;
Q8KLK7
Streptomyces toyocaensis;
Q8KLK7
Streptomyces toyocaensis;
Q8KLK7
Streptomyces toyocaensis;
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homohexamer
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crystallographic data
homohexamer
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crystallographic data
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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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expression in Escherichia coli
expression in Escherichia coli BL21
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expression in Escherichia coli
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expression in Escherichia coli
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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
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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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DPGC_AMYOR
434
47089
Swiss-Prot
DPGC_STRTO
438
48174
Swiss-Prot
A0A2S6QW08_9PROT
466
51489
TrEMBL
A0A2S6RG61_9PROT
468
53821
TrEMBL
A0A2S6RC95_9PROT
460
53182
TrEMBL
A0A2P8AQS0_9ACTN
310
33878
TrEMBL
A0A2S6RXG2_9PROT
482
52939
TrEMBL
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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
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