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0.29
-
mutant D238A, pH 7, 30°C
2.3
-
mutant D238E, pH 7, 30°C
6.7
-
wild-type, pH 7, 30°C
0.11
-
pH 7.5, 25°C, recombinant mutant S469A, ornithine hydroxylation assay
0.15
-
pH 7.5, 25°C, recombinant mutant S469A, O2 consumption assay
0.5
-
pH 7.5, 25°C, recombinant mutant N323A, ornithine hydroxylation assay
0.53
-
pH 7.5, 25°C, recombinant mutant N293A, ornithine hydroxylation assay
0.59
-
pH 7.5, 25°C, recombinant wild-type enzyme, O2 consumption assay
0.62
-
pH 7.5, 25°C, recombinant wild-type enzyme, ornithine hydroxylation assay
0.88
-
pH 7.5, 25°C, recombinant mutant N293A, O2 consumption assay
1.06
-
pH 7.5, 25°C, recombinant mutant N323A, O2 consumption assay
0.03
-
pH 7.6, 25°C, mutant enzyme S257A, cofactor: NADPH
0.03
-
pH 7.6, 25°C, wild-type enzyme, cofactor: NADPH
0.2
-
recombinant FAD-reconstituted enzyme-enzyme, pH 7.5, temperature not specified in the publication
0.34
-
recombinant holo-enzyme, pH 7.5, temperature not specified in the publication
0.48
-
pH 7.5, 25°C, cosubstrate: NADPH, following the formation of hydroxylated ornithine
0.5
-
pH 7.5, 25°C, cosubstrate: NADH, following the formation of hydroxylated ornithine
0.68
-
pH 7.5, 25°C, cosubstrate: NADH, oxygen consumption assay
0.87
-
pH 7.5, 25°C, cosubstrate: NADPH, oxygen consumption assay
0.0198
-
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25°C
0.1
-
at pH 8.5 and 30°C
0.37
-
mutant D238A, pH 7, 30°C
0.58
-
mutant D238E, pH 7, 30°C
1.5
-
wild-type, pH 7, 30°C
0.7
-
mutant enzyme D231A, at pH 8.5 and 20°C
4.3
-
mutant enzyme H272L, at pH 8.5 and 20°C
5.1
-
mutant enzyme E299Q, at pH 8.5 and 20°C
8.2
-
mutant enzyme R57A, at pH 8.5 and 20°C
52
-
mutant enzyme Q104L, at pH 8.5 and 20°C
95
-
mutant enzyme H272N, at pH 8.5 and 20°C
110
-
mutant enzyme Y160F, at pH 8.5 and 20°C
130
-
mutant enzyme Y229F, at pH 8.5 and 20°C
170
-
mutant enzyme C273A, at pH 8.5 and 20°C
170
-
mutant enzyme E299D, at pH 8.5 and 20°C
240
-
mutant enzyme S61A, at pH 8.5 and 20°C
350
-
mutant enzyme Y229S, at pH 8.5 and 20°C
410
-
mutant enzyme Y160S, at pH 8.5 and 20°C
440
-
wild type enzyme, at pH 8.5 and 20°C
460
-
mutant enzyme D140N, at pH 8.5 and 20°C
2200
-
Y227C/E277G double mutant, at 30°C
2900
-
A240D/E277G double mutant, at 30°C
3500
-
Y227C/E277G double mutant, at 55°C
4300
-
A240D/E277G double mutant, at 55°C
0.37
-
recombinant mutant R180Tenzyme, pH 8.0, 25°C
2.1
-
pH 8.0, 37°C, recombinant wild-type enzyme
20.7
-
pH 8.0, 15°C, recombinant mutant R217A, 0.001 mM enzyme
22.6
-
pH 8.0, 15°C, recombinant wild-type enzyme, 0.001 mM enzyme
34.5
-
recombinant wild-type enzyme, pH 8.0, 25°C
34.9
-
pH 8.0, 25°C, recombinant wild-type enzyme, 60 nM enzyme
38.4
-
pH 8.0, 25°C, recombinant mutant R217A, 60 nM enzyme
3.5
-
pH 8.0, temperature not specified in the publication
0.003
-
recombinant PfODC domain
0.006
-
recombinant Pf-Hinge-ODC
0.015
-
mutant enzyme D364E, at pH 7.5 and 37°C
3.3
-
CO2 assay, pH 7.8, 25°C
3.4
-
wild-type, pH 7.0, temperature not specified in the publication
3.5
-
mutant K294A, pH 8.0, 37°C
3.6
-
mutant I163A, pH 7.0, temperature not specified in the publication
4.2
-
circular dichroism assay, pH 7.8, 25°C
4.2
-
mutant I163G, pH 7.0, temperature not specified in the publication
4.4
-
mutant I163V, pH 7.0, temperature not specified in the publication
4.8
-
mutant E165A, pH 7.0, temperature not specified in the publication
5.6
-
mutant E165G, pH 7.0, temperature not specified in the publication
7
-
wild type enzyme, at pH 7.5 and 37°C
7.4
-
mutant I163S, pH 7.0, temperature not specified in the publication
10
-
mutant enzyme S396A, at pH 7.5 and 37°C
10.1
-
mutant E165S, pH 7.0, temperature not specified in the publication
10.1
-
mutant I163T, pH 7.0, temperature not specified in the publication
10.9
-
mutant E165V, pH 7.0, temperature not specified in the publication
15.4
-
wild-type, pH 8.0, 37°C
24.8
-
mutant E165T, pH 7.0, temperature not specified in the publication
25.7
-
mutant I163V/E165V, pH 7.0, temperature not specified in the publication
38.5
-
mutant I163T/E165T, pH 7.0, temperature not specified in the publication
3
6
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322T/I326L
4.7
-
pH 6.0, 30°C, mutant enzyme M50V/A52C/P54D/T55S
4.8
-
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322A
7
-
pH 6.0, 30°C, mutant enzyme A52C
7.2
-
pH 6.0, 30°C, mutant enzyme A52C/P54D
7.2
-
pH 6.0, 30°C, mutant enzyme G319W
8.4
-
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P
8.6
-
pH 6.0, 30°C, wild type enzyme
13
-
pH 6.0, 30°C, mutant enzyme P54D
14
-
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D
20
-
pH 6.0, 30°C, mutant enzyme S322A
24
-
pH 6.0, 30°C, mutant enzyme S322T/I326L
0.54
-
DABA AT/DC fusion protein
0.29
-
mutant M341L, pH 7.5, 37°C
0.4
-
mutant F344Y, pH 7.5, 37°C
0.91
-
wild-type, pH 7.5, 37°C
2.3
-
mutant F344H, pH 7.5, 37°C
2.78
-
pH 7.5, 37°C, recombinant enzyme
980
-
pH 8.5, room temperature
1.83
-
pH 8.0, 30°C, recombinant wild-type enzyme
68.8
-
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
-
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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0.033
-
wild-type, pH 7, 30°C
0.061
-
mutant D238E, pH 7, 30°C
0.31
-
mutant D238A, pH 7, 30°C
0.42
-
dehydrogenation with phenazine methosulfate
0.058
-
pH 8.0, 25°C, recombinant detagged enzyme
1
-
pH 7.5, 25°C, recombinant wild-type enzyme, ornithine hydroxylation assay
1.1
-
pH 7.5, 25°C, recombinant wild-type enzyme, O2 consumption assay
12
-
pH 7.5, 25°C, recombinant mutant N323A, ornithine hydroxylation assay
15
-
pH 7.5, 25°C, recombinant mutant N323A, O2 consumption assay
16
-
pH 7.5, 25°C, recombinant mutant N293A, ornithine hydroxylation assay
18
-
pH 7.5, 25°C, recombinant mutant N293A, O2 consumption assay
18
-
pH 7.5, 25°C, recombinant mutant S469A, ornithine hydroxylation assay
21
-
pH 7.5, 25°C, recombinant mutant S469A, O2 consumption assay
0.107
-
recombinant FAD-reconstituted enzyme-enzyme, pH 7.5, temperature not specified in the publication
0.21
-
pH 7.6, 25°C, mutant enzyme S257A, cofactor: NADPH
0.3
-
pH 7.6, 25°C, wild-type enzyme, cofactor: NADPH
0.305
-
recombinant holo-enzyme, pH 7.5, temperature not specified in the publication
0.5
-
pH 7.5, 25°C, cosubstrate: NADH, oxygen consumption assay
1.7
-
pH 7.5, 25°C, cosubstrate: NADH, following the formation of hydroxylated ornithine
1.7
-
pH 7.5, 25°C, cosubstrate: NADPH, following the formation of hydroxylated ornithine
2
-
pH 7.5, 25°C, cosubstrate: NADPH, oxygen consumption assay
0.33
-
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25°C
0.017
-
at pH 8.0 and 20°C, measured at the rate of H2O2 production
0.022
-
wild-type, pH 7, 30°C
0.041
-
mutant D238E, pH 7, 30°C
0.45
-
mutant D238A, pH 7, 30°C
5.6
-
at pH 8.5 and 30°C
0.7
-
with pyruvate and NADPH as cosubstrates
29.5
-
pH 7.5, temperature not specified in the publication
0.001
-
liver enzyme, presence of putrescine, pH 7.0
0.00232
-
liver enzyme, pH 7.0
0.05
-
mutant K268A, pH 8.0, 30°C
0.33
-
mutant enzyme E299Q, at pH 8.5 and 20°C
0.36
-
wild-type, pH 7.7, 37°C
0.4
-
mutant enzyme H272N, at pH 8.5 and 20°C
0.42
-
mutant K88R, pH 7.7, 37°C
0.44
-
mutant enzyme R57A, at pH 8.5 and 20°C
0.45
-
mutant enzyme Y229F, at pH 8.5 and 20°C
0.53
-
mutant enzyme S61A, at pH 8.5 and 20°C
0.53
-
wild type enzyme, at pH 8.5 and 20°C
0.55
-
mutant K88Q, pH 7.7, 37°C
0.59
-
mutant enzyme D231A, at pH 8.5 and 20°C
0.61
-
mutant enzyme Y229S, at pH 8.5 and 20°C
0.68
-
mutant enzyme H272L, at pH 8.5 and 20°C
0.73
-
mutant enzyme C273A, at pH 8.5 and 20°C
0.81
-
mutant enzyme Q104L, at pH 8.5 and 20°C
0.85
-
pH 8.5, 10 mM fixed substrate
0.9
-
mutant enzyme E299D, at pH 8.5 and 20°C
1
-
mutant enzyme Y160F, at pH 8.5 and 20°C
1
-
mutant K260A, pH 8.0, 30°C
1.1
-
mutant K265R, pH 8.0, 30°C
1.1
-
mutant K268R, pH 8.0, 30°C
1.2
-
mutant E256Q, pH 8.0, 30°C
1.2
-
mutant K260R, pH 8.0, 30°C
1.2
-
mutant K265A, pH 8.0, 30°C
1.3
-
mutant Q294P, pH 8.0, 30°C
1.6
-
wild-type, pH 8.0, 30°C
1.8
-
mutant arcB6254, pH 7.25
1.85
-
mutant arcB6240, pH 7.25
2
-
mutant L290Q, pH 8.0, 30°C
2
-
mutant L290S, pH 8.0, 30°C
2.1
-
mutant E123S, pH 8.0, 30°C
2.6
-
mutant E123A, pH 8.0, 30°C
2.8
-
mutant C191M/C194N/F197V, pH 8.0, 30°C
3.4
-
mutant T68G, pH 8.0, 30°C
7.3
-
mutant enzyme Y160S, at pH 8.5 and 20°C
10
-
mutant E256A, pH 8.0, 30°C
10
-
mutant K289S, pH 8.0, 30°C
17
-
mutant enzyme D140N, at pH 8.5 and 20°C
20
-
mutant K263R, pH 8.0, 30°C
30
-
mutant K263A, pH 8.0, 30°C
32
-
recombinant enzyme mutant Y230V/G231S/L232M/Y233G, pH 8.5, 37°C
34
-
mutant N184Q, pH 8.0, 30°C
36.4
-
recombinant wild-type enzyme, pH 8.5, 37°C
49
-
mutant D182N, pH 8.0, 30°C
350
-
mutant N185Q, pH 8.0, 30°C
0.56
2.8
pH and temperature not specified in the publication, liver enzyme
0.59
-
pH and temperature not specified in the publication, kidney enzyme
0.6
-
pH and temperature not specified in the publication, small intestine enzyme
0.8
-
pH and temperature not specified in the publication, enzyme from cortical interneurons
0.9
-
wild-type with PfTrx, pH 7.4, 37°C
1.1
-
pH and temperature not specified in the publication, brain enzyme
1.2
4.8
pH and temperature not specified in the publication, liver enzyme
1.282
-
well differentiated gastroadenocarcinoma, pH 7.5
1.5
-
wild-type with PfGrx, pH 7.4, 37°C
1.6
-
wild-type, pH 7.4, 37°C
1.7
-
rhinopharyngeal tumor, pH 7.5
1.7
-
with pyruvate as cosubstrate, pH 7.1, 37°C
2
-
pH and temperature not specified in the publication
2
37
recombinant mutant R180Tenzyme, pH 8.0, 25°C
2.089
-
in rat brain mitochondrial fraction, in absence of pyridoxal 5'-phosphate
2.3
-
wild-type (OAT in parasite cell extract), pH 7.4, 37°C
2.8
-
with 2-oxoglutarate as cosubstrate, pH 7.1, 37°C
2.9
-
with glyoxylate as cosubstrate, pH 7.1, 37°C
3.275
-
poorly differentiated gastroadenocarcinoma, pH 7.5
3.7
-
pH and temperature not specified in the publication, eye retina enzyme
3.95
-
pH and temperature not specified in the publication
4
-
pH and temperature not specified in the publication, liver isolated mitochondria
4.3
-
pH and temperature not specified in the publication, enzyme from astrocytes
4.7
-
pH and temperature not specified in the publication, enzyme from cerebellar granule cells
5.089
-
in rat brain mitochondrial fraction, in presence of 0.05 mM pyridoxal 5'-phosphate
5.1
-
pH 8.0, 25°C, recombinant mutant R217A, 60 nM enzyme
5.6
-
pH and temperature not specified in the publication, eye enzyme
6.5
-
pH 8.0, 25°C, recombinant wild-type enzyme, 60 nM enzyme
6.5
-
recombinant wild-type enzyme, pH 8.0, 25°C
6.9
-
pH 8.0, 15°C, recombinant mutant R217A, 0.001 mM enzyme
6.9
-
pH 8.0, 37°C, recombinant wild-type enzyme
7
-
pH 8.0, 15°C, recombinant wild-type enzyme, 0.001 mM enzyme
7.5
-
pH and temperature not specified in the publication, liver enzyme
8.97
-
assay based on detection of L-glutamate, pH 8.0, 37°C
10.5
-
assay based on reduction of DELTA1-pyrroline-5-carboxylate, pH 8.0, 37°C
13.94
-
wild-type, pH 7.5, 37°C
15
-
pH and temperature not specified in the publication
15.32
-
transgenic mouse, pH 7.5, 37°C
87
-
salt stress conditions
4.391
-
pH 8.0, temperature not specified in the publication
0.03
-
mutant enzyme C360A
0.041
-
recombinant PfODC
0.047
-
recombinant Pf-Hinge-ODC
0.06
-
in 10 mM sodium phosphate buffer, pH 7.0
0.07
-
enzyme from epidermis
0.081
-
mutant enzyme K69A
0.09
-
in presence of 2.9 mM dithiothreitol
0.122
-
CO2 assay, pH 7.8, 25°C
0.15
-
mutant enzyme C70S
0.16
-
recombinant PfODC domain
0.214
-
circular dichroism assay, pH 7.8, 25°C
0.27
-
mutant enzyme S396A, at pH 7.5 and 37°C
0.33
-
recombinant enzyme
0.37
-
wild type enzyme, at pH 7.5 and 37°C
0.37
-
wild-type, pH 8.0, 37°C
0.4
-
apparent value, at 37°C
0.6
-
in presence of 0.25 M NaCl
0.6
-
mutant I163T, pH 7.0, temperature not specified in the publication
0.6
-
mutant I163T/E165T, pH 7.0, temperature not specified in the publication
0.7
-
in presence of 0.25 M NaCl
0.7
-
mutant E165T, pH 7.0, temperature not specified in the publication
1
-
enzyme from chromatin
1.1
-
mutant I163V/E165V, pH 7.0, temperature not specified in the publication
1.3
-
mutant I163V, pH 7.0, temperature not specified in the publication
1.4
-
mutant E165V, pH 7.0, temperature not specified in the publication
1.5
-
mutant I163A, pH 7.0, temperature not specified in the publication
1.5
-
mutant I163S, pH 7.0, temperature not specified in the publication
1.7
-
mutant I163G, pH 7.0, temperature not specified in the publication
1.9
-
mutant E165S, pH 7.0, temperature not specified in the publication
2.4
-
mutant E165A, pH 7.0, temperature not specified in the publication
3
-
mutant E165G, pH 7.0, temperature not specified in the publication
3.3
-
wild-type, pH 7.0, temperature not specified in the publication
3.6
-
degradative ornithine decarboxylase
5.6
-
biosynthetic ornithine decarboxylase
43
-
mutant K294A, pH 8.0, 37°C
55.2
-
mutant enzyme D364E, at pH 7.5 and 37°C
207
-
pupa, 37°C, pH 7.1
438
-
larva, 37°C, pH 7.1
1660
-
ovaries of young females, 37°C, pH 7.1
0.96
-
pH 6.0, 30°C, wild type enzyme
0.98
-
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P
1.2
-
pH 6.0, 30°C, mutant enzyme S322A
1.3
-
pH 6.0, 30°C, mutant enzyme A52C
1.3
-
pH 6.0, 30°C, mutant enzyme G319W
1.5
-
pH 6.0, 30°C, mutant enzyme S322T/I326L
1.6
-
pH 6.0, 30°C, mutant enzyme A52C/P54D
2.1
-
pH 6.0, 30°C, mutant enzyme P54D
3.1
-
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D
3.3
-
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322T/I326L
4
-
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322A
4.5
-
pH 6.0, 30°C, mutant enzyme M50V/A52C/P54D/T55S
11.1
-
DABA AT/DC fusion protein
1.04
-
mutant M341L, pH 7.5, 37°C
1.05
-
wild-type, pH 7.5, 37°C
1.43
-
pH 7.5, 37°C, recombinant enzyme
1.53
-
mutant F344H, pH 7.5, 37°C
1.59
-
mutant F344Y, pH 7.5, 37°C
0.25
-
0.5 mM NAD+, in the presence of L-arginine
0.25
-
OCD, Ach5, in the absence of L-arginine
0.25
-
OCD, C58, in the presence of L-arginine
1.7
-
0.5 mM NAD+, in the absence of L-arginine
1.7
-
in the absence of L-arginine , OCD, C58
2
-
0.5 mM NAD+ and 0.1 mM L-arginine, strain GR4
5.5
-
in the absence of ADP
6.2
-
in the presence of ADP
0.77
-
pH 8.5, room temperature
27
-
pH 8.0, 30°C, recombinant wild-type enzyme
3
-
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
-
wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Control of arginine biosynthesis in Escherichia coli: inhibition of arginyl-transfer ribonucleic acid synthetase activity
1973
Williams, A.L.; Yem, D.W.; McGinnis, E.; Williams, L.S.
J. Bacteriol.
115
228-234
Purification and characterization of histidyl-transfer RNA synthetase from Neurospora crassa
1980
Chen, C.C.; Somberg, E.W.
Biochim. Biophys. Acta
613
514-525
-
Carnosine synthetase (chick muscle)
1971
Kalyankar, G.D.; Meister, A.
Methods Enzymol.
17
102-105
Enzymatic synthesis of carnosine and related beta-alanyl and gamma-aminobutyryl peptides
1959
Kalyankar, G.D.; Meister, A.
J. Biol. Chem.
234
3210-3218
Enzymes of arginine and urea synthesis
1973
Ratner, S.
Adv. Enzymol. Relat. Areas Mol. Biol.
39
1-90
Mechanism and regulation of the glutamine-dependent carbamyl phosphate synthetase of Escherichia coli
1989
Meister, A.
Adv. Enzymol. Relat. Areas Mol. Biol.
62
315-374
Carbamoyl-phosphate synthetase: an example of effects on enzyme properties of shifting an equilibrium between active monomer and active oligomer
1986
Anderson, P.M.
Biochemistry
25
5576-5582
carbamyl phosphate synthetase (glutamine-utilizing) from Escherichia coli
1985
Kaseman, D.S.; Meister, A.
Methods Enzymol.
113
305-326
Carbamoylphosphate synthetase from Pseudomonas aeruginosa. Subunit composition, kinetic analysis and regulation
1983
Abdelal, A.T.; Bussey, L.; Vickers, L.
Eur. J. Biochem.
129
697-702
Carbamoyl-phosphate synthetase (glutamine): Salmonella
1978
Ingraham, J.L.; Abdelal, A.T.H.
Methods Enzymol.
51
29-35
-
Purification and characterization of amino acid racemase with very broad substrate specificity from Aeromonas caviae
1987
Inagaki, K.; Tanizawa, K.; Tanaka, H.; Soda, K.
Agric. Biol. Chem.
51
173-180
A new amino acid racemase with threonine alpha-epimerase activity from Pseudomonas putida: purification and characterization
1993
Lim, Y.H.; Yokoigawa, K.; Esaki, N.; Soda, K.
J. Bacteriol.
175
4213-4217
Nonstereospecific transamination catalyzed by pyridoxal phosphate-dependent amino acid racemases of broad substrate specificity
1988
Lim, Y.H.; Yoshimura, T.; Kurokawa, Y.; Esaki, N.; Soda, K.
J. Biol. Chem.
273
4001-4005
Purification and properties of amino acid racemase from Aeromonas punctata subsp. caviae
1984
Inagaki, K.; Tanizawa, K.; Tanaka, H.; Soda, K.
Prog. Clin. Biol. Res.
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