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EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
arginine racemase,
more
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Racemase, arginine
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-
-
ArgR
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-
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L-arginine = D-arginine
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-
-
-
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arginine racemase
A pyridoxal-phosphate protein.
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D-lysine
L-lysine
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103% activity compared to D-arginine
-
-
?
D-ornithine
L-ornithine
-
42% activity compared to D-arginine
-
-
?
L-2,3-Diaminopropionate
D-2,3-Diaminopropionate
Pseudomonas graveolens
-
-
-
?
L-2,4-Diaminobutyrate
D-2,4-Diaminobutyrate
Pseudomonas graveolens
-
-
-
?
L-Citrulline
D-Citrulline
L-Homoarginine
D-Homoarginine
L-Homocitrulline
D-Homocitrulline
L-lysine
D-lysine
-
104% activity compared to L-arginine
-
-
?
L-Orn
D-Orn
Pseudomonas graveolens
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-
-
?
L-Theanine
D-Theanine
Pseudomonas graveolens
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-
-
?
N5-Acetyl-L-Orn
N4-Acetyl-L-Orn
Pseudomonas graveolens
-
-
-
?
N6-Acetyl-L-Lys
N6-AcetylD-Lys
Pseudomonas graveolens
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-
-
?
additional information
?
-
Pseudomonas graveolens
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the enzyme catylzes transamination between L-Orn or D-Orn and pyruvate with the formation of racemic Ala and DELTA1-pyrroline-2-carboxylic acid. The rate of transamination is very low as compared to that of racemization
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-
?
D-alanine
L-alanine
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11% activity compared to D-arginine
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-
?
D-alanine
L-alanine
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11% activity compared to D-arginine
-
-
?
D-arginine
L-arginine
-
racemization of arginine is a two-step mechanism, intermediate is 2-keto-arginine, a first enzyme (DauA) catalyzes oxidative deamination of D-arginine into 2-ketoarginine and ammonia, and the second enzyme DauB is able to use 2-ketoarginine and ammonia as substrates and convert them into L-arginine in the presence of NADPH or NADH, DauA and DauB are coupled catabolic and anabolic dehydrogenases to perform D-to-L racemization of arginine, which serves as prerequisite of D-arginine utilization through L-arginine catabolic pathways
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-
ir
D-arginine
L-arginine
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100% activity
-
-
?
D-arginine
L-arginine
-
100% activity
-
-
?
L-alanine
D-alanine
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12% activity compared to L-arginine
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-
?
L-alanine
D-alanine
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12% activity compared to L-arginine
-
-
?
L-Arg
D-Arg
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-
-
?
L-Arg
D-Arg
Pseudomonas graveolens
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-
-
?
L-Arg
D-Arg
Pseudomonas graveolens
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-
-
?
L-Arg
D-Arg
Pseudomonas graveolens
-
-
-
?
L-Arg
D-Arg
Pseudomonas graveolens
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-
-
?
L-Arg
D-Arg
Pseudomonas graveolens
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-
-
?
L-arginine
D-arginine
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100% activity
-
-
?
L-arginine
D-arginine
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100% activity
-
-
?
L-Citrulline
D-Citrulline
Pseudomonas graveolens
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-
-
-
?
L-Citrulline
D-Citrulline
Pseudomonas graveolens
-
13% of the activity relative to L-Arg
-
?
L-Ethionine
D-Ethionine
Pseudomonas graveolens
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-
-
-
?
L-Ethionine
D-Ethionine
Pseudomonas graveolens
-
13% of the activity relative to L-Arg
-
?
L-Glu
D-Glu
Pseudomonas graveolens
-
-
-
-
?
L-Glu
D-Glu
Pseudomonas graveolens
-
7% of the activity relative to L-Arg
-
?
L-Homoarginine
D-Homoarginine
Pseudomonas graveolens
-
-
-
-
?
L-Homoarginine
D-Homoarginine
Pseudomonas graveolens
-
25% of the activity relative to L-Arg
-
?
L-Homocitrulline
D-Homocitrulline
Pseudomonas graveolens
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-
-
-
?
L-Homocitrulline
D-Homocitrulline
Pseudomonas graveolens
-
12% of the activity relative to L-Arg
-
?
L-Lys
D-Lys
Pseudomonas graveolens
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-
-
-
?
L-Lys
D-Lys
Pseudomonas graveolens
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110% of the activity relative to L-Arg
-
?
L-Met
D-Met
Pseudomonas graveolens
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-
-
-
?
L-Met
D-Met
Pseudomonas graveolens
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4% of the activity relative to L-Arg
-
?
L-Ornithine
D-Ornithine
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44% activity compared to L-arginine
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-
?
L-Ornithine
D-Ornithine
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44% activity compared to L-arginine
-
-
?
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D-arginine
L-arginine
-
racemization of arginine is a two-step mechanism, intermediate is 2-keto-arginine, a first enzyme (DauA) catalyzes oxidative deamination of D-arginine into 2-ketoarginine and ammonia, and the second enzyme DauB is able to use 2-ketoarginine and ammonia as substrates and convert them into L-arginine in the presence of NADPH or NADH, DauA and DauB are coupled catabolic and anabolic dehydrogenases to perform D-to-L racemization of arginine, which serves as prerequisite of D-arginine utilization through L-arginine catabolic pathways
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-
ir
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pyridoxal 5'-phosphate
Pseudomonas graveolens
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Km: 0.0004 mM
pyridoxal 5'-phosphate
Pseudomonas graveolens
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contains 1 mol of firmly bound pyridoxal 5'-phosphate per 42000 g of protein
pyridoxal 5'-phosphate
Pseudomonas graveolens
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slighly increases activity
pyridoxal 5'-phosphate
Pseudomonas graveolens
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contains 4 mol of pyridoxal 5'-phosphate per mol of enzyme
pyridoxal 5'-phosphate
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dependent on
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DL-Penicillamine
Pseudomonas graveolens
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hydroxylamine
Pseudomonas graveolens
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-
L-2,4-diaminobutyrate
Pseudomonas graveolens
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-
L-Orn
Pseudomonas graveolens
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inactivated by preliminary incubation at pH 10.0. The inactivation is prevented and the inactivated enzyme is reactivated by addition of pyruvate or oxaloacetate
N4-Acetyl-L-Orn
Pseudomonas graveolens
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inactivated by preliminary incubation at pH 10.0. The inactivation is prevented and the inactivated enzyme is reactivated by addition of pyruvate or oxaloacetate
D-Orn
Pseudomonas graveolens
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-
D-Orn
Pseudomonas graveolens
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inactivated by preliminary incubation at pH 10.0. The inactivation is prevented and the inactivated enzyme is reactivated by addition of pyruvate or oxaloacetate
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1
D-Arg
Pseudomonas graveolens
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-
0.0004
pyridoxal 5'-phosphate
Pseudomonas graveolens
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cofactor pyridoxal 5'-phosphate
8.8
D-alanine
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mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
15
D-alanine
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wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
1
D-arginine
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mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
1.2
D-arginine
-
wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
1.8
D-Lysine
-
mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
2.4
D-Lysine
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wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
3.1
D-ornithine
-
mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
3.6
D-ornithine
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wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
8.4
L-alanine
-
mutant enzyme C74A/C73A ,in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
15.7
L-alanine
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wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
1
L-arginine
-
mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
1.2
L-arginine
-
wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
1.8
L-lysine
-
mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
2.4
L-lysine
-
wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
3
L-ornithine
-
mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
3.7
L-ornithine
-
wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
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2.6
D-alanine
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wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
6.8
D-alanine
-
mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
94.6
D-arginine
-
mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
119
D-arginine
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wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
81.7
D-Lysine
-
mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
104
D-Lysine
-
wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
67.5
D-ornithine
-
mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
83.3
D-ornithine
-
wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
2.4
L-alanine
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wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
6.3
L-alanine
-
mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
93.5
L-arginine
-
mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
119
L-arginine
-
wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
84.9
L-lysine
-
mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
109
L-lysine
-
wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
68.8
L-ornithine
-
mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
87.7
L-ornithine
-
wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
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0.17
D-alanine
-
wild type enzyme,in 0.6 M CHES-NaOH buffer (pH 10.0), 0.1 mM pyridoxal 5'-phosphate, at 37°C
0.77
D-alanine
-
mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0), 0.1 mM pyridoxal 5'-phosphate, at 37°C
94.6
D-arginine
-
mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0), 0.1 mM pyridoxal 5'-phosphate, at 37°C
96
D-arginine
-
wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0), 0.1 mM pyridoxal 5'-phosphate, at 37°C
43.7
D-Lysine
-
wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0), 0.1 mM pyridoxal 5'-phosphate, at 37°C
45.1
D-Lysine
-
mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0), 0.1 mM pyridoxal 5'-phosphate, at 37°C
22.1
D-ornithine
-
mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0), 0.1 mM pyridoxal 5'-phosphate, at 37°C
23
D-ornithine
-
wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0), 0.1 mM pyridoxal 5'-phosphate, at 37°C
0.15
L-alanine
-
wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
0.74
L-alanine
-
mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0), 0.1 mM pyridoxal 5'-phosphate, at 37°C
92.6
L-arginine
-
mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0), 0.1 mM pyridoxal 5'-phosphate, at 37°C
101
L-arginine
-
wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0), 0.1 mM pyridoxal 5'-phosphate, at 37°C
46.2
L-lysine
-
wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0), 0.1 mM pyridoxal 5'-phosphate, at 37°C
47.4
L-lysine
-
mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0), 0.1 mM pyridoxal 5'-phosphate, at 37°C
22.9
L-ornithine
-
mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0), 0.1 mM pyridoxal 5'-phosphate, at 37°C
23.4
L-ornithine
-
wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0), 0.1 mM pyridoxal 5'-phosphate, at 37°C
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10.5
-
periplasmic arginine racemase activity, mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
1250
Pseudomonas graveolens
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-
70.2
-
periplasmic arginine racemase activity, wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
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10 - 10.6
Pseudomonas graveolens
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-
11
Pseudomonas graveolens
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transamination
7 - 10
Pseudomonas graveolens
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theanine
7.5 - 10.6
Pseudomonas graveolens
-
L-Lys
7.5 - 8.5
Pseudomonas graveolens
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Orn
9 - 10.6
Pseudomonas graveolens
-
D-Arg
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-
-
-
brenda
Pseudomonas graveolens
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-
-
brenda
-
-
-
brenda
-
-
-
brenda
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-
an about 30times higher activity of ArgR is detected in the periplasm compared to that in the cytoplasm
brenda
-
an about 30times higher activity of ArgR is detected in the periplasm compared to that in the cytoplasm
-
brenda
-
an about 30times higher activity of ArgR is detected in the periplasm compared to that in the cytoplasm
-
brenda
-
an about 30times higher activity of ArgR is detected in the periplasm compared to that in the cytoplasm
-
-
brenda
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A0A653WMY3_9MICO
388
0
41392
TrEMBL
-
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167000
Pseudomonas graveolens
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sedimentation equilibrium method
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homodimer
-
2 * 42000
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-
Pseudomonas graveolens
-
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C47A/C73A
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the mutant displays about 7fold reduced specific activity compared to the wild type enzyme. The relative activities of C47A/C73AArgR for L-arginine, L-lysine, L-ornithine, D-arginine, D-lysine, and D-ornithine correspond well to those of wild type ArgR, but the relative activities for L-alanine and D-alanine increase to 25 and 26%, respectively
C47A/C73A
-
the mutant displays about 7fold reduced specific activity compared to the wild type enzyme. The relative activities of C47A/C73AArgR for L-arginine, L-lysine, L-ornithine, D-arginine, D-lysine, and D-ornithine correspond well to those of wild type ArgR, but the relative activities for L-alanine and D-alanine increase to 25 and 26%, respectively
-
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pyridoxal 5'-phosphate slighly increases stability
Pseudomonas graveolens
-
the disulfide bond of ArgR is essential for ArgR to fold
-
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3-7°C, as a suspension in 0.02 M potassium phosphate buffer, pH 7.3, containing 0.1 mM pyridoxal 5'-phosphate and 60% saturated ammonium sulfate, stable for 6 months
Pseudomonas graveolens
-
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-
-
-
Pseudomonas graveolens
-
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expressed in Escherichia coli BL21(DE3) cells
-
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Adams, E.
Amino acid racemases and epimerases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
6
479-507
1972
Pseudomonas graveolens
-
brenda
Soda, K.; Yorifuji, T.; Ogata, K.
Occurence of arginine racemase in bacterial extract
Biochim. Biophys. Acta
146
606-608
1967
Pseudomonas graveolens
brenda
Yorifuji, T.; Ogata, K.
Crystalline arginine racemase
Biochem. Biophys. Res. Commun.
34
760-764
1969
Pseudomonas graveolens
brenda
Soda, K.; Yorifuji, T.; Ogata, K.
Arginine racemase (Pseudomonas graveolens)
Methods Enzymol.
17A
341-345
1976
Pseudomonas graveolens
-
brenda
Yorifuji, T.; Ogata, K.
Arginine racemase of Pseudomonas graveolens. I. Purification, crystallization, and properties
J. Biol. Chem.
246
5085-5092
1971
Pseudomonas graveolens
brenda
Yorifuji, T.
Arginine racemase of Pseudomonas graveolens. II. Racemization and transamination of ornithine catalyzed by arginine racemase
J. Biol. Chem.
246
5093-5101
1971
Pseudomonas graveolens
brenda
Jann, A.; Matsumoto, H.; Haas, D.
The fourth arginine catabolic pathway of Pseudomonas aeruginosa [published erratum appears in J Gen Microbiol 1988 Sep;134(Pt 9):2633]
J. Gen. Microbiol.
134
1043-1053
1988
Pseudomonas aeruginosa
brenda
Li, C.; Lu, C.D.
Arginine racemization by coupled catabolic and anabolic dehydrogenases
Proc. Natl. Acad. Sci. USA
106
906-911
2009
Pseudomonas aeruginosa
brenda
Matsui, D.; Oikawa, T.
Detection and function of the intramolecular disulfide bond in arginine racemase: an enzyme with broad substrate specificity
Chem. Biodivers.
7
1591-1602
2010
Pseudomonas taetrolens, Pseudomonas taetrolens NBRC 3460
brenda
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