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0.28
thiamine diphosphate
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additional information
additional information
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1
2-oxobutanoate
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at 1.5 mM pyruvate
1.37
2-oxobutanoate
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pH 7.5, 37°C
5
2-oxobutanoate
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at 2 mM pyruvate
5.6
2-oxobutanoate
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wild-type, pH 7.3, 37°C
6.9
2-oxobutanoate
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mutant with a deleted C-terminal domain in the regulatory subunit IlvN, pH 7.3, 37°C
9.1
2-oxobutanoate
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mutant V375A, pH 7.6, 37°C
300
2-oxobutanoate
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wild-type, pH 7.6, 37°C
0.0028
pyruvate
wild type enzyme, at pH 7.5 and 37°C
0.0028
pyruvate
pH 7.5, 37°C, recombinant His6-tagged mutant H84A
0.0028
pyruvate
pH 7.5, 37°C, recombinant His6-tagged mutant H84T
0.0028
pyruvate
pH 7.5, 37°C, recombinant His6-tagged mutant Q86A
0.0028
pyruvate
pH 7.5, 37°C, recombinant His6-tagged wild-type enzyme
0.0117
pyruvate
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wild-type enzyme
0.0289
pyruvate
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mutant R372S/F373P/D374V/D375E
0.0757
pyruvate
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mutant R372S/F373P/D374V/D375E/R376Y
0.141
pyruvate
mutant enzyme Q86A, at pH 7.5 and 37°C
0.15
pyruvate
mutant enzyme H84A, at pH 7.5 and 37°C
0.213
pyruvate
mutant enzyme H84T, at pH 7.5 and 37°C
0.33
pyruvate
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mutant C83T, pH 7.6, 37°C
1
pyruvate
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pH 7.6, isoenzyme AHAS I
1.08
pyruvate
mutant F147R, pH 7.5, 37°C
1.09
pyruvate
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mutant enzyme W574L, at pH 7.5 and 37°C
1.1
pyruvate
mutant Q487S, pH 7.0, 37°C
1.18
pyruvate
wild-type, pH 7.5, 37°C
1.19
pyruvate
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mutant enzyme P197T, at pH 7.5 and 37°C
1.2
pyruvate
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mutant C83S, pH 7.6, 37°C
1.3
pyruvate
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isoenzyme I
1.37
pyruvate
pH 7.5, 37°C, recombinant wild-type enzyme
1.37
pyruvate
pH 6.8, 37°C, recombinant enzyme
1.37
pyruvate
at pH 6.8 and 37°C
1.37
pyruvate
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wild type enzyme, pH and temperature not specified in the publication
1.37
pyruvate
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recombinant wild-type enzyme, pH and temperature not specified in the publication
1.37
pyruvate
wild type enzyme, at pH 6.8 and 37°C
1.37
pyruvate
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mutant enzyme P197L, at pH 7.5 and 37°C
1.38
pyruvate
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mutant S539R, pH not specified in the publication, temperature not specified in the publication
1.38
pyruvate
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mutant enzyme P197H, at pH 7.5 and 37°C
1.46
pyruvate
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mutant enzyme P197S, at pH 7.5 and 37°C
1.5
pyruvate
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mutant C83A, pH 7.6, 37°C
1.5 - 2
pyruvate
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mutant enzyme D376E, at pH 7.5 and 37°C
1.56
pyruvate
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pH 7.0, 37°C, holoenzyme
1.6
pyruvate
mutant Q487G, pH 7.0, 37°C
1.7
pyruvate
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recombinant mutant E49D, pH and temperature not specified in the publication
1.7
pyruvate
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mutant enzyme E49D, pH and temperature not specified in the publication
1.74
pyruvate
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wild type enzyme, at pH 7.5 and 37°C
1.89
pyruvate
mutant L141A, pH 7.5, 37°C
2.2
pyruvate
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pH 7.0, 30°C, sulfonylurea-resistant biotype
2.49
pyruvate
wild-type, pH 7.5, 37°C
2.6
pyruvate
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native protein
2.76
pyruvate
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catalytic subunit
2.76
pyruvate
pH 7.5, 37°C, recombinant wild-type enzyme
2.76
pyruvate
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pH 7.0, 37°C, catalytic subunit
2.76
pyruvate
wild type enzyme, at pH 7.5 and 37°C
2.9
pyruvate
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fusion protein containing an N-terminal oligohistidine sequence on the large subunit
3.33
pyruvate
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mutant S539A, pH not specified in the publication, temperature not specified in the publication
3.35
pyruvate
mutant L89A, pH 7.5, 37°C
3.36
pyruvate
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mutant S167A, pH not specified in the publication, temperature not specified in the publication
3.6
pyruvate
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mutant D375E, pH 7.5, 37°C
3.6
pyruvate
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mutant L476M/Q480W, pH 7.6, 37°C
3.66
pyruvate
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pH 7.5, 37°C
3.7
pyruvate
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pH 7.0, 30°C, sulfonylurea-susceptible biotype
3.89
pyruvate
mutant F147A, pH 7.5, 37°C
3.96
pyruvate
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at pH 6.5 and 37°C
4
pyruvate
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37°C, reconstituted, recombinant holoenzyme
4.15
pyruvate
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pH 7.6, 37°C
4.34
pyruvate
pH 7.5, 37°C, recombinant mutant Q411N
4.34
pyruvate
mutant enzyme Q411N, at pH 6.8 and 37°C
4.58
pyruvate
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wild-type, pH not specified in the publication, temperature not specified in the publication
4.7
pyruvate
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mutant with a deleted C-terminal domain in the regulatory subunit IlvN, pH 7.3, 37°C
4.7
pyruvate
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mutant Q480W, pH 7.6, 37°C
4.8
pyruvate
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wild-type, pH 7.6, 37°C
4.8
pyruvate
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pH 7.4, 37°C, recombinant enzyme
4.8
pyruvate
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37°C, recombinant holoenzyme
4.94
pyruvate
mutant W516R, pH 7.5, 37°C
5
pyruvate
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wild-type, 37°C, pH 7.6
5.2
pyruvate
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wild-type, pH 7.6, 37°C
5.7
pyruvate
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mutant D374A, pH 7.5, 37°C
5.8
pyruvate
mutant R101A, pH 7.5, 37°C
6
pyruvate
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wild-type with His-tag, pH 7.6, 37°C
6.04
pyruvate
pH 7.5, 37°c, recombinant mutant P126A
6.04
pyruvate
mutant enzyme P126A, at pH 7.5 and 37°C
6.53
pyruvate
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pH 7.5, 37°C, recombinant wild-type enzyme
6.6
pyruvate
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wild-type, pH 7.6, 37°C
7
pyruvate
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enzyme form II
7
pyruvate
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pH 7.6, isoenzyme AHAS III
7
pyruvate
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mutant D428N, 37°C, pH 7.6
7.1
pyruvate
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mutant E47A, pH 7.6, 37°C
7.3
pyruvate
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mutant E47Q, 37°C, pH 7.6
7.3
pyruvate
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mutant V375I, pH 7.6, 37°C
7.6
pyruvate
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isoenzyme III
7.7
pyruvate
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mutant E47A, 37°C, pH 7.6
7.7
pyruvate
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mutant E47Q, pH 7.6, 37°C
7.8
pyruvate
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wild-type, pH 7.3, 37°C
7.82
pyruvate
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mutant S539F, pH not specified in the publication, temperature not specified in the publication
8
pyruvate
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enzyme form I
8
pyruvate
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30°C, 120 ng protein in assay
8
pyruvate
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mutant V477I, pH 7.6, 37°C
8.01
pyruvate
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Km-value of the first active site
8.36
pyruvate
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mutant S506R, pH not specified in the publication, temperature not specified in the publication
8.5
pyruvate
wild type enzyme, at pH 7.5 and 20°C
8.7
pyruvate
mutant Q487A, pH 7.0, 37°C
8.8
pyruvate
holoenzyme, pH 8.0, 60°C
8.8
pyruvate
mutant enzyme S627N, at pH 7.5 and 20°C
8.9
pyruvate
mutant S27A, pH 7.5, 37°C
9
pyruvate
mutant enzyme S627N, in the presence of imazamox, at pH 7.5 and 20°C
9.2
pyruvate
pH 7.5, 37°C, recombinant enzyme
10
pyruvate
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30°C, 60 ng protein in assay
10
pyruvate
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pH 7.0, 37°C, isoform ALS I
10.54
pyruvate
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mutant S506A, pH not specified in the publication, temperature not specified in the publication
10.6
pyruvate
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pH 7.6, isoenzyme AHAS II
11
pyruvate
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pH 7.0, 37°C, isoform ALS II
11.2
pyruvate
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mutant W464L with His-tag, pH 7.6, 37°C
11.4
pyruvate
mutant enzyme S627N, in the presence of imazethapyr, at pH 7.5 and 20°C
11.48
pyruvate
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mutant S167R, pH not specified in the publication, temperature not specified in the publication
11.7
pyruvate
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wild-type, pH 7.5, 37°C
11.7
pyruvate
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pH 7.5, wild-type enzyme
11.9
pyruvate
pH 7.5, 37°C
12
pyruvate
large subunit, pH 8.0, 60°C
12.1
pyruvate
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wild-type recombinant enzyme
13
pyruvate
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mutant L476M, pH 7.6, 37°C
13.6
pyruvate
wild-type, pH 7.0, 37°C
13.68
pyruvate
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mutant C607S, pH 7.5, 37°C
13.71
pyruvate
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mutant H392M, 37°C, pH 7.5
13.8
pyruvate
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mutant V375A, pH 7.6, 37°C
14.68
pyruvate
pH 7.5, 37°C, recombinant mutant Q112N
14.68
pyruvate
mutant enzyme Q112N, at pH 6.8 and 37°C
15.05
pyruvate
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wild-type, pH 7.5, 37°C
16.09
pyruvate
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wild-type, 37°C, pH 7.5
16.24
pyruvate
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recombinant mutant E49Q, pH and temperature not specified in the publication
16.24
pyruvate
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mutant enzyme E49Q, pH and temperature not specified in the publication
16.4
pyruvate
pH 7.0, 80°C
16.4
pyruvate
pH 7.0, 85°C, recombinant catalytic subunit
16.4
pyruvate
at pH 7.0 and 80°C
16.43
pyruvate
pH 7.5, 37°C, recombinant mutant Q411E
16.43
pyruvate
mutant enzyme Q411E, at pH 6.8 and 37°C
17.06
pyruvate
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wild-type, pH 7.5, 37°C
17.3
pyruvate
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mutant F109M, pH 7.6, 37°C
17.5
pyruvate
pH 7.5, 37°C
17.9
pyruvate
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mutant V391A, pH 7.6, 37°C
19.78
pyruvate
pH 7.5, 37°C, recombinant mutant Q112E
19.78
pyruvate
mutant enzyme Q112E, at pH 6.8 and 37°C
21
pyruvate
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mutant E60Q, pH 7.6, 37°C
21.55
pyruvate
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mutant C411S, pH 7.5, 37°C
24.6
pyruvate
pH 7.5, 37°C, recombinant mutant H111R
24.6
pyruvate
mutant enzyme H111R, at pH 6.8 and 37°C
25.5
pyruvate
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pH 7.5, 37°C, in the presence of 3.5 M KCl
26
pyruvate
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mutant M263A, pH 7.6, 37°C
26.23
pyruvate
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mutant K299Q pH 7.5, 37°C
28
pyruvate
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mutant E60A, pH 7.6, 37°C
29.5
pyruvate
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mutant Q110N, pH 7.6, 37°C
30.2
pyruvate
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mutant Q110A, pH 7.6, 37°C
30.58
pyruvate
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recombinant mutant E49A, pH and temperature not specified in the publication
30.58
pyruvate
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mutant enzyme E49A, pH and temperature not specified in the publication
31.2
pyruvate
pH 7.5, 37°C, recombinant mutant Q112V
31.2
pyruvate
mutant enzyme Q112V, at pH 6.8 and 37°C
36
pyruvate
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mutant D428E, 37°C, pH 7.6
36
pyruvate
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mutant M250A with His-tag, pH 7.6, 37°C
36.6
pyruvate
pH 7.5, 37°C, recombinant mutant H111F
36.6
pyruvate
mutant enzyme H111F, at pH 6.8 and 37°C
38
pyruvate
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mutant R276K with His-tag, pH 7.6, 37°C
40.4
pyruvate
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mutant Q110H pH 7.6, 37°C
50
pyruvate
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wild-type, pH 7.3, 37°C, presence of 10 mM L-valine
50
pyruvate
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mutant R289K, pH 7.6, 37°C
54
pyruvate
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wild-type, pH 7.3, 37°C, presence of 10 mM L-isoleucine
55.8
pyruvate
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mutant D374A/D375A, pH 7.5, 37°C
65
pyruvate
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wild-type, pH 7.3, 37°C, presence of 10 mM L-leucine
70
pyruvate
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pH 6.5, 37°C
76.63
pyruvate
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mutantH351F, 37°C, pH 7.5
100
pyruvate
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Km-value of the second active site
104
pyruvate
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mutant with a deleted C-terminal domain in the regulatory subunit IlvN, pH 7.3, 37°C, presence of 10 mM L-isoleucine
104
pyruvate
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mutant with a deleted C-terminal domain in the regulatory subunit IlvN, pH 7.3, 37°C, presence of 10 mM L-leucine
104
pyruvate
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mutant with a deleted C-terminal domain in the regulatory subunit IlvN, pH 7.3, 37°C, presence of 10 mM L-valine
109.3
pyruvate
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mutant D375A, pH 7.5, 37°C
109.4
pyruvate
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mutant K255F, pH 7.5, 37°C
110.6
pyruvate
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mutant Q110E, pH 7.6, 37°C
113.9
pyruvate
-
pH 7.5, mutant R141K
115.5
pyruvate
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mutant K255Q, pH 7.5, 37°C
116.8
pyruvate
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pH 7.5, mutant R141F
124
pyruvate
-
mutant R289Q, pH 7.6, 37°C
148
pyruvate
-
pH 7.5, 37°C, recombinant mutant W573F
167.4
pyruvate
-
pH 7.5, mutant R372F
266.7
pyruvate
-
mutant D374E/D375E, pH 7.5, 37°C
287.8
pyruvate
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mutant H351M, 37°C, pH 7.5
337.3
pyruvate
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pH 7.5, mutant R376K
466.7
pyruvate
pH 7.5, 37°c, recombinant mutant P126V
466.7
pyruvate
mutant enzyme P126V, at pH 7.5 and 37°C
475.9
pyruvate
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pH 7.5, mutant R372K
557.6
pyruvate
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mutant D374E, pH 7.5, 37°C
807.7
pyruvate
pH 7.5, 37°c, recombinant mutant P126T
807.7
pyruvate
mutant enzyme P126T, at pH 7.5 and 37°C
959.5
pyruvate
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mutant H351Q, 37°C, pH 7.5
additional information
additional information
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kinetics
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additional information
additional information
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kinetics
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additional information
additional information
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kinetics
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additional information
additional information
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non-hyperbolic substrate-saturation curve, involving interaction between the active sites of the dimer
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additional information
additional information
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kinetics of wild-type and mutant enzymes
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additional information
additional information
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kinetics of isozymes
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additional information
additional information
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cofactor affinities of wild-type and mutant enzymes, overview
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additional information
additional information
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kinetics or recombinant wild-type and reconstituted isozymes AHAS I, exclusive binding model
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additional information
additional information
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steady-state kinetics at different reaction conditions
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additional information
additional information
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steady-state kinetics of recombinant wild-type and mutant enzymes, cofactor binding parameters, overview
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additional information
additional information
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Michaelis-Menten steady-state kinetic analysis, overview
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additional information
additional information
Michaelis-Menten steady-state kinetic analysis, overview
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additional information
additional information
Michaelis-Menten steady-state kinetic analysis, overview
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additional information
additional information
binding kinetics of Mg2+ and thiamine diphosphate with wild-type enzyme and mutant enzymes, overview
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additional information
additional information
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binding kinetics of Mg2+ and thiamine diphosphate with wild-type enzyme and mutant enzymes, overview
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additional information
additional information
Michaelis-Menten kinetics and optimal reaction conditions, overview
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additional information
additional information
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Michaelis-Menten kinetics and optimal reaction conditions, overview
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additional information
additional information
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substrate and cofactor kinetics of wild-type and mutant enzymes, overview
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additional information
additional information
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activity is dependent on the ionic strength of the buffer and diminishes considerably (approximately 80%) when assayed in buffers with less than 100 mM concentrations. At concentrations higher than 100 mM the activity levels are quite similar (tested up to 500 mM)
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additional information
additional information
activity is dependent on the ionic strength of the buffer and diminishes considerably (approximately 80%) when assayed in buffers with less than 100 mM concentrations. At concentrations higher than 100 mM the activity levels are quite similar (tested up to 500 mM)
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additional information
additional information
activity is dependent on the ionic strength of the buffer and diminishes considerably (approximately 80%) when assayed in buffers with less than 100 mM concentrations. At concentrations higher than 100 mM the activity levels are quite similar (tested up to 500 mM)
-