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0.59 - 2.6
(2R,3S)-3-isopropylmalate
0.013 - 0.255
(2R,3S)-3-isopropylmalate
0.002 - 0.0133
DL-3-isopropylmalate
0.000017 - 0.316
isopropylmalate
0.0061 - 0.0161
threo-D,L-isopropylmalate
0.08
threo-Ds-3-Isopropylmalate
-
60°C
0.59
(2R,3S)-3-isopropylmalate
mutant H15Y/E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M, pH 8.0, 37°C
0.9
(2R,3S)-3-isopropylmalate
mutant E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M, pH 8.0, 37°C
0.9
(2R,3S)-3-isopropylmalate
mutant E57V/S72I/R85M/Y86A/M208T/V238M/R310M, pH 8.0, 37°C
1
(2R,3S)-3-isopropylmalate
mutant S72I/R85M/Y86A/M208T/F217Y/V238M/R310M, pH 8.0, 37°C
1
(2R,3S)-3-isopropylmalate
wild-type (2R,3S)-3-isopropylmalate dehydrogenase, pH 8.0, 37°C
1
(2R,3S)-3-isopropylmalate
wild-type HICDH, pH 8.0, 37°C
1.5
(2R,3S)-3-isopropylmalate
mutant E57V/S72I/R85M/Y86A/M208T/F217Y/V238M, pH 8.0, 37°C
1.9
(2R,3S)-3-isopropylmalate
mutant E57V/S72I/R85M/Y86A/M208T/F217Y/R310M, pH 8.0, 37°C
2.6
(2R,3S)-3-isopropylmalate
mutant R85V/Y86A, pH 8.0, 37°C
0.9
NAD+
mutant E57V/S72I/R85M/Y86A/M208T/V238M/R310M, pH 8.0, 37°C
1.2
NAD+
mutant E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M, pH 8.0, 37°C
1.2
NAD+
mutant H15Y/E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M, pH 8.0, 37°C
1.6
NAD+
mutant E57V/S72I/R85M/Y86A/M208T/F217Y/V238M, pH 8.0, 37°C
1.6
NAD+
mutant S72I/R85M/Y86A/M208T/F217Y/V238M/R310M, pH 8.0, 37°C
1.7
NAD+
mutant E57V/S72I/R85M/Y86A/M208T/F217Y/R310M, pH 8.0, 37°C
1.7
NAD+
mutant R85V/Y86A, pH 8.0, 37°C
1.9
NAD+
wild-type (2R,3S)-3-isopropylmalate dehydrogenase, pH 8.0, 37°C
1.9
NAD+
wild-type HICDH, pH 8.0, 37°C
0.013
(2R,3S)-3-isopropylmalate
-
pH 7.6, 20°C, stopped flow experiment
0.013
(2R,3S)-3-isopropylmalate
mutant enzyme D217A, at pH 7.6 and 20°C
0.014
(2R,3S)-3-isopropylmalate
mutant enzyme N102A, at pH 7.6 and 20°C
0.016
(2R,3S)-3-isopropylmalate
wild type enzyme, at pH 7.6 and 20°C
0.016
(2R,3S)-3-isopropylmalate
wild type enzyme, in the presence of 25 mM K+, at pH 7.6 and 20°C
0.0169
(2R,3S)-3-isopropylmalate
-
55°C, mutant enzyme A172D
0.0169
(2R,3S)-3-isopropylmalate
-
mutant enzyme A172D, at 55°C, pH not specified in the publication
0.02
(2R,3S)-3-isopropylmalate
mutant enzyme D245A, at pH 7.6 and 20°C
0.022
(2R,3S)-3-isopropylmalate
60°C, pH 7.6, mutant enzyme A172V
0.0221
(2R,3S)-3-isopropylmalate
-
55°C, wild-type enzyme
0.0221
(2R,3S)-3-isopropylmalate
-
wild type enzyme, at 55°C, pH not specified in the publication
0.0234
(2R,3S)-3-isopropylmalate
-
55°C, mutant enzyme A172N
0.0234
(2R,3S)-3-isopropylmalate
-
mutant enzyme A172N, at 55°C, pH not specified in the publication
0.0257
(2R,3S)-3-isopropylmalate
-
55°C, mutant enzyme A172E
0.0257
(2R,3S)-3-isopropylmalate
-
mutant enzyme A172E, at 55°C, pH not specified in the publication
0.0267
(2R,3S)-3-isopropylmalate
-
55°C, mutant enzyme A172Q
0.0267
(2R,3S)-3-isopropylmalate
-
mutant enzyme A172Q, at 55°C, pH not specified in the publication
0.031
(2R,3S)-3-isopropylmalate
60°C, pH 7.6, wild-type enzyme
0.032
(2R,3S)-3-isopropylmalate
mutant enzyme E270A, at pH 7.6 and 20°C
0.032
(2R,3S)-3-isopropylmalate
mutant enzyme E270A, in the presence of 25 mM K+, at pH 7.6 and 20°C
0.04
(2R,3S)-3-isopropylmalate
mutant enzyme Y139A, at pH 7.6 and 20°C
0.145
(2R,3S)-3-isopropylmalate
mutant enzyme K185A, at pH 7.6 and 20°C
0.255
(2R,3S)-3-isopropylmalate
mutant enzyme D241A, at pH 7.6 and 20°C
0.002
DL-3-isopropylmalate
-
pH 8.0, 60°C, mutant V126G
0.0026
DL-3-isopropylmalate
-
pH 8.0, 60°C, mutant V126A
0.0027
DL-3-isopropylmalate
-
pH 8.0, 60°C, mutant V126T
0.0032
DL-3-isopropylmalate
-
pH 8.0, 60°C, mutant V126S
0.0044
DL-3-isopropylmalate
-
pH 8.0, 60°C, wild-type
0.005
DL-3-isopropylmalate
-
pH 8.0, 60°C, mutant V126M
0.0061
DL-3-isopropylmalate
-
pH 8.0, 60°C, mutant V126E
0.0084
DL-3-isopropylmalate
-
pH 8.0, 60°C, mutant V126I
0.0121
DL-3-isopropylmalate
-
pH 8.0, 60°C, mutant V126L
0.0133
DL-3-isopropylmalate
-
pH 8.0, 60°C, mutant V126F
0.000017
isopropylmalate
-
pH 7.3, 21°C, cofactor: NAD+, wild-type enzyme
0.00048
isopropylmalate
-
pH 7.3, 21°C, cofactor: NAD+, mutant enzyme E87G
0.001
isopropylmalate
-
pH 8.0, 40°C, mutant enzyme C275T
0.0012
isopropylmalate
-
pH 8.0, 40°C, mutant enzyme G376A
0.00125
isopropylmalate
-
pH 8.0, 40°C, wild-type enzyme
0.0013
isopropylmalate
-
pH 8.0, 40°C, mutant enzyme A31G/G43A/A709G
0.0024
isopropylmalate
-
pH 8.0, 40°C, mutant enzyme G43A
0.00298
isopropylmalate
-
pH 7.3, 21°C, cofactor: NADP+, wild-type enzyme
0.0053
isopropylmalate
-
pH 7.3, 21°C, cofactor: NAD+, mutant enzyme E87Q
0.0078
isopropylmalate
-
pH 8.0, 70°C, mutant enzyme C275T
0.0089
isopropylmalate
-
pH 8.0, 70°C, wild-type enzyme
0.0096
isopropylmalate
-
pH 8.0, 70°C, mutant enzyme A31G/G43A/A709G
0.01
isopropylmalate
-
pH 8.0, 70°C, mutant enzyme G376A
0.011
isopropylmalate
-
pH 8.0, 70°C, mutant enzyme G43A
0.044
isopropylmalate
-
pH 7.6, 60°C
0.316
isopropylmalate
-
pH 7.6, 40°C
0.0326
malate
-
pH 7.3, 21°C, cofactor: NAD+, isopropylmalate dehydrogenase mutant E87Q
1.51
malate
-
pH 7.3, 21°C, cofactor: NAD+, wild-type enzyme
31.56
malate
-
pH 7.3, 21°C, cofactor: NADP+, wild-type enzyme
35.59
malate
-
pH 7.3, 21°C, cofactor: NAD+, isopropylmalate dehydrogenase mutant E87G
0.0022
NAD+
pH 8.0, 25°C, wild-type enzyme
0.00321
NAD+
-
pH 7.3, 21°C, reaction with isopropylmalate, wild-type enzyme
0.0091
NAD+
-
pH 8.0, 40°C, mutant V126S
0.0092
NAD+
-
pH 8.0, 40°C, mutant V126A
0.012
NAD+
pH 8.0, 40°C, wild-type enzyme
0.012
NAD+
-
pH 7.3, 21°C, wild-type enzyme
0.0149
NAD+
-
pH 8.0, 40°C, reaction with 3-D-isopropylmalate, mutant enzyme C275T
0.022
NAD+
-
pH 8.0, 40°C, mutant V126T
0.024
NAD+
-
pH 8.0, 40°C, mutant V126G
0.025
NAD+
-
pH 8.0, 40°C, wild-type
0.0258
NAD+
-
pH 8.0, 40°C, isopropylmalate dehydrogenase wild-type
0.031
NAD+
-
pH 7.3, 21°C, mutant enzyme S226R
0.0454
NAD+
-
pH 7.3, 21°C, reaction with tartrate, wild-type enzym
0.0515
NAD+
-
pH 8.0, 40°C, mutant V126E
0.059
NAD+
-
pH 8.0, 60°C, mutant V126A
0.06
NAD+
mutant enzyme Y139A, at pH 7.6 and 20°C
0.062
NAD+
-
pH 8.0, 40°C, mutant V126I
0.064
NAD+
mutant enzyme K185A, at pH 7.6 and 20°C
0.0725
NAD+
-
pH 8.0, 60°C, mutant V126G
0.076
NAD+
-
55°C, mutant enzyme A172D
0.094
NAD+
-
55°C, mutant enzyme A172Q
0.095
NAD+
-
pH 8.0, 60°C, mutant V126S
0.1
NAD+
-
55°C, mutant enzyme A172E
0.103
NAD+
-
pH 8.0, 60°C, mutant V126T
0.105
NAD+
-
55°C, mutant enzyme A172N
0.1065
NAD+
-
pH 7.3, 21°C, reaction with malate, wild-type enzyme
0.109
NAD+
-
pH 8.0, 60°C, mutant V126E
0.111
NAD+
-
pH 8.0, 40°C, mutant V126L
0.116
NAD+
-
55°C, wild-type enzyme
0.13
NAD+
60°C, pH 7.6, pH 7.6, mutant enzyme A172V
0.131
NAD+
-
pH 7.3, 21°C, isopropylmalate dehydrogenase mutant E87G
0.139
NAD+
-
pH 7.6, 60°C
0.14
NAD+
60°C, pH 7.6, wild-type enzyme
0.144
NAD+
-
pH 8.0, 40°C, mutant V126F
0.157
NAD+
-
pH 8.0, 40°C, mutant enzyme A31G/G43A/A709G
0.157
NAD+
-
pH 7.6, 40°C
0.16
NAD+
-
pH 8.0, 40°C, mutant enzyme G43A
0.166
NAD+
-
pH 8.0, 60°C, wild-type
0.172
NAD+
pH 7.6, 70°C, recombinant mutant L134N
0.181
NAD+
-
pH 7.3, 21°C, isopropylmalate dehydrogenase mutant E87Q
0.198
NAD+
-
pH 8.0, 60°C, mutant V126I
0.21
NAD+
pH 8.0, 70°C, wild-type enzyme
0.225
NAD+
-
pH 8.0, 40°C, isopropylmalate dehydrogenase cold-adapted mutant T1155
0.25
NAD+
-
pH 7.6, 20°C, stopped flow experiment
0.255
NAD+
pH 7.6, 70°C, recombinant mutant L134N/V181T/P324T/A335E
0.26
NAD+
mutant enzyme N102A, at pH 7.6 and 20°C
0.29
NAD+
wild type enzyme, at pH 7.6 and 20°C
0.29
NAD+
wild type enzyme, in the presence of 25 mM K+, at pH 7.6 and 20°C
0.305
NAD+
mutant enzyme D217A, at pH 7.6 and 20°C
0.32
NAD+
mutant enzyme D241A, at pH 7.6 and 20°C
0.336
NAD+
pH 7.6, 70°C, recombinant mutant H197K
0.341
NAD+
-
pH 8.0, 70°C, isopropylmalate wild-type
0.359
NAD+
pH 7.6, 70°C, recombinant mutant A335E
0.371
NAD+
pH 7.6, 70°C, recombinant mutant P324T
0.375
NAD+
mutant enzyme D245A, at pH 7.6 and 20°C
0.378
NAD+
-
pH 8.0, 60°C, mutant V126F
0.386
NAD+
-
pH 7.3, 21°C, isopropylmalate dehydrogenase mutant E87G
0.391
NAD+
-
pH 8.0, 60°C, mutant V126L
0.401
NAD+
pH 7.6, 70°C, recombinant mutant R58L
0.428
NAD+
pH 7.6, 70°C, recombinant mutant P56E
0.468
NAD+
pH 7.6, 70°C, recombinant mutant F53L
0.514
NAD+
pH 7.6, 70°C, recombinant wild-type enzyme
0.52
NAD+
pH 7.6, 70°C, recombinant mutant V61I
0.567
NAD+
pH 7.6, 70°C, recombinant mutant V181T/P324T/A335E
0.625
NAD+
pH 7.6, 70°C, recombinant mutant S261N
0.642
NAD+
pH 7.6, 70°C, recombinant mutant V181T
0.66
NAD+
mutant enzyme E270A, at pH 7.6 and 20°C
0.66
NAD+
mutant enzyme E270A, in the presence of 25 mM K+, at pH 7.6 and 20°C
0.673
NAD+
pH 7.6, 70°C, recombinant mutant D184H
0.778
NAD+
-
pH 7.3, 21°C, isopropylmalate dehydrogenase mutant E87Q
0.82
NAD+
-
at 70°C, mutant enzyme G43A
0.917
NAD+
-
at 70°C, mutant enzyme A31G/G43A/A709G
1.01
NAD+
-
at 40°C, isopropylmalate dehydrogenase cold-adapted mutant P215
1.01
NAD+
-
pH 8.0, 40°C, mutant V126M
1.836
NAD+
-
pH 7.3, 21°C, mutant enzyme S226R/D278K/I279Y
1.853
NAD+
-
pH 7.3, 21°C, reaction with malate, mutant enzyme E87Q
1.97
NAD+
-
pH 8.0, 60°C, mutant V126M
2.584
NAD+
-
pH 7.3, 21°C, reaction with malate, mutant enzyme E87G
3.56
NAD+
-
70°C, isopropylmalate dehydrogenase cold-adapted mutant P215
0.014
NADP+
-
pH 7.3, 21°C, mutant enzyme S226R/D278K/I279Y
0.02
NADP+
-
pH 7.3, 21°C, mutant enzyme D278K, I279T, P325Y and 395-Arg
0.722
NADP+
-
pH 7.3, 21°C, mutant enzyme S226R
1.573
NADP+
-
pH 7.3, 21°C, reaction with tartrate, wild-type enzyme
1.75
NADP+
-
wild-type enzyme
1.836
NADP+
-
pH 7.3, 21°C, reaction with isopropylmalate, wild-type enzyme
6.579
NADP+
-
pH 7.3, 21°C, recation with malate, wild-type enzyme
0.0407
Tartrate
-
pH 7.3, 21°C, cofactor: NAD+, wild-type enzyme
0.761
Tartrate
-
pH 7.3, 21°C, cofactor: NAD+, isopropylmalate dehydrogenase mutant E87Q
0.817
Tartrate
-
pH 7.3, 21°C, cofactor: NADP+, wild-type enzyme
1.21
Tartrate
-
pH 7.3, 21°C, cofactor: NAD+, mutant enzyme E87G
0.0061
threo-D,L-isopropylmalate
pH 7.6, 70°C, recombinant wild-type enzyme
0.0063
threo-D,L-isopropylmalate
pH 7.6, 70°C, recombinant mutant V181T/P324T/A335E
0.007
threo-D,L-isopropylmalate
pH 7.6, 70°C, recombinant mutant L134N
0.0161
threo-D,L-isopropylmalate
pH 7.6, 70°C, recombinant mutant L134N/V181T/P324T/A335E
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.08 - 5.7
(2R,3S)-3-isopropylmalate
0.0025 - 220
(2R,3S)-3-isopropylmalate
0.09 - 19
isopropylmalate
additional information
additional information
-
the cold adaption results from the destabilization of the ternary complex caused by increase in the volume of the residue at position 126
-
0.08
(2R,3S)-3-isopropylmalate
wild-type HICDH, pH 8.0, 37°C
0.3
(2R,3S)-3-isopropylmalate
mutant E57V/S72I/R85M/Y86A/M208T/V238M/R310M, pH 8.0, 37°C
0.4
(2R,3S)-3-isopropylmalate
mutant R85V/Y86A, pH 8.0, 37°C
0.6
(2R,3S)-3-isopropylmalate
mutant E57V/S72I/R85M/Y86A/M208T/F217Y/V238M, pH 8.0, 37°C
1.6
(2R,3S)-3-isopropylmalate
mutant S72I/R85M/Y86A/M208T/F217Y/V238M/R310M, pH 8.0, 37°C
1.8
(2R,3S)-3-isopropylmalate
mutant E57V/S72I/R85M/Y86A/M208T/F217Y/R310M, pH 8.0, 37°C
2.9
(2R,3S)-3-isopropylmalate
mutant H15Y/E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M, pH 8.0, 37°C
5.1
(2R,3S)-3-isopropylmalate
mutant E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M, pH 8.0, 37°C
5.7
(2R,3S)-3-isopropylmalate
wild-type (2R,3S)-3-isopropylmalate dehydrogenase, pH 8.0, 37°C
0.0025
(2R,3S)-3-isopropylmalate
mutant enzyme D241A, at pH 7.6 and 20°C
0.0025
(2R,3S)-3-isopropylmalate
mutant enzyme K185A, at pH 7.6 and 20°C
0.033
(2R,3S)-3-isopropylmalate
mutant enzyme E270A, at pH 7.6 and 20°C
0.033
(2R,3S)-3-isopropylmalate
mutant enzyme E270A, in the presence of K+, at pH 7.6 and 20°C
0.045
(2R,3S)-3-isopropylmalate
mutant enzyme D217A, at pH 7.6 and 20°C
0.108
(2R,3S)-3-isopropylmalate
mutant enzyme Y139A, at pH 7.6 and 20°C
0.433
(2R,3S)-3-isopropylmalate
mutant enzyme D245A, at pH 7.6 and 20°C
0.55
(2R,3S)-3-isopropylmalate
mutant enzyme N102A, at pH 7.6 and 20°C
2.36
(2R,3S)-3-isopropylmalate
-
pH 8.0, 40°C, wild-type enzyme
2.41
(2R,3S)-3-isopropylmalate
-
pH 8.0, 40°C, mutant enzyme C275T
2.9
(2R,3S)-3-isopropylmalate
-
pH 7.6, 20°C, quenched flow experiment
3.4
(2R,3S)-3-isopropylmalate
-
pH 7.6, 20°C, stopped flow experiment
3.97
(2R,3S)-3-isopropylmalate
wild type enzyme, in the presence of K+, at pH 7.6 and 20°C
7.2
(2R,3S)-3-isopropylmalate
-
pH 8.0, 40°C, mutant enzyme A31G/G43A/A709G
10.7
(2R,3S)-3-isopropylmalate
-
pH 8.0, 40°C, mutant enzyme G43A
17.7
(2R,3S)-3-isopropylmalate
-
pH 8.0, 40°C, mutant enzyme G376A
40
(2R,3S)-3-isopropylmalate
wild type enzyme, at pH 7.6 and 20°C
44.7
(2R,3S)-3-isopropylmalate
-
pH 8.0, 70°C, mutant enzyme C275T
45.8
(2R,3S)-3-isopropylmalate
-
pH 8.0, 70°C, wild-type enzyme
50.1
(2R,3S)-3-isopropylmalate
-
pH 8.0, 70°C, mutant enzyme A31G/G43A/A709G
63.6
(2R,3S)-3-isopropylmalate
-
pH 8.0, 70°C, mutant enzyme G43A
100
(2R,3S)-3-isopropylmalate
-
pH 8.0, 70°C, mutant enzyme G376A
100
(2R,3S)-3-isopropylmalate
-
55°C, mutant enzyme A172D
107
(2R,3S)-3-isopropylmalate
-
55°C, wild-type enzyme
111
(2R,3S)-3-isopropylmalate
-
55°C, mutant enzyme A172Q
117
(2R,3S)-3-isopropylmalate
-
55°C, mutant enzyme A172E and A172N
163
(2R,3S)-3-isopropylmalate
60°C, pH 7.6, wild-type enzyme
220
(2R,3S)-3-isopropylmalate
60°C, pH 7.6, mutant enzyme A172V
0.09
isopropylmalate
-
pH 7.3, 21°C, reaction with NADP+, mutant enzyme S226R/D278K/I279Y
0.15
isopropylmalate
-
pH 7.3, 21°C, reaction with NAD+, wild-type enzyme
0.2
isopropylmalate
-
pH 7.3, 21°C, reaction with NAD+, mutant enzyme E87G
0.21
isopropylmalate
-
pH 7.3, 21°C, reaction with NAD+, mutant enzyme E87Q
0.24
isopropylmalate
-
pH 7.3, 21°C, reaction with NAD+, wild-type enzyme
0.26
isopropylmalate
-
pH 7.3, 21°C, reaction with NADP+, wild-type enzyme
0.48
isopropylmalate
-
pH 7.3, 21°C, reaction with NAD+, mutant enzyme S226R
0.88
isopropylmalate
-
pH 7.3, 21°C, reaction with NADP+, mutant enzyme S226R
1.66
isopropylmalate
-
pH 7.3, 21°C, reaction with NADP+, wild-type enzyme
1.91
isopropylmalate
-
pH 7.3, 21°C, reaction with NAD+, mutant enzyme S226R/D278K/I279Y
8
isopropylmalate
-
pH 7.6, 70°C
19
isopropylmalate
-
pH 7.6, 40°C
0.19
malate
-
pH 7.3, 21°C, reaction with NAD+, mutant enzyme E87Q
0.26
malate
-
pH 7.3, 21°C, reaction with NAD+, mutant enzyme E87G
4.69
malate
-
pH 7.3, 21°C, reaction with NADP+, wild-type enzyme
10.6
malate
-
pH 7.3, 21°C, reaction with NAD+, wild-type enzyme
0.15
NAD+
-
pH 7.3, 21°C, reaction with isopropylmalate, wild-type enzyme
0.19
NAD+
-
pH 7.3, 21°C, reaction with tartrate, wild-type enzyme or reaction with malate, mutant enzyme E87Q
0.2
NAD+
-
pH 7.3, 21°C, reaction with isopropylmalate, mutant enzyme E87G
0.21
NAD+
-
pH 7.3, 21°C, reaction with tartrate, mutant enzyme E87G
0.21
NAD+
-
pH 7.3, 21°C, reaction with isopropylmalate, mutant enzyme E87Q
0.24
NAD+
-
pH 7.3, 21°C, reaction with isopropylmalate, wild-type enzyme
0.26
NAD+
-
pH 7.3, 21°C, reaction with malate, mutant enzyme E87G or reaction with tartrate, mutant enzyme E87Q
0.37
NAD+
pH 8.0, 25°C, wild-type enzyme
0.48
NAD+
-
pH 7.3, 21°C, reaction with isopropylmalate, mutant enzyme S226R
1.2
NAD+
-
pH 8.0, 40°C, mutant V126A
1.5
NAD+
-
pH 8.0, 40°C, mutant V126S
1.7
NAD+
-
pH 8.0, 40°C, mutant V126G
1.9
NAD+
-
pH 8.0, 40°C, mutant V126T
1.91
NAD+
-
pH 7.3, 21°C, reaction with isopropylmalate, mutant enzyme S226R/D278K/I279Y
2.36
NAD+
-
pH 8.0, 40°C, wild-type enzyme
2.4
NAD+
pH 8.0, 40°C, wild-type enzyme
2.4
NAD+
-
pH 8.0, 40°C, wild-type
2.41
NAD+
-
pH 8.0, 40°C, mutant enzyme C275T
3.5
NAD+
-
pH 8.0, 40°C, mutant V126E
6
NAD+
-
pH 8.0, 40°C, mutant V126I
7.2
NAD+
-
pH 8.0, 40°C, mutant enzyme A31G/G43A/A709G
8
NAD+
-
pH 7.6, 70°C, reaction with isopropylmalate
8.5
NAD+
-
pH 8.0, 40°C, mutant V126L
9
NAD+
-
pH 8.0, 60°C, mutant V126A
10
NAD+
-
pH 8.0, 60°C, V126G
10.2
NAD+
pH 7.6, 70°C, recombinant mutant V181T
10.6
NAD+
-
pH 7.3, 21°C, reaction with malate, wild-type enzyme
10.7
NAD+
-
pH 8.0, 40°C, mutant enzyme G43A
11
NAD+
-
pH 8.0, 40°C, mutant V126F
11.2
NAD+
pH 7.6, 70°C, recombinant mutant D184H
13
NAD+
-
pH 8.0, 60°C, mutant V126S
13.2
NAD+
pH 7.6, 70°C, recombinant mutant V181T/P324T/A335E
13.4
NAD+
pH 7.6, 70°C, recombinant wild-type enzyme
13.8
NAD+
pH 7.6, 70°C, recombinant mutant P324T
14.6
NAD+
pH 7.6, 70°C, recombinant mutant P56E
15
NAD+
-
pH 8.0, 60°C, mutant V126T
15
NAD+
pH 7.6, 70°C, recombinant mutants F53L and V61I
17.7
NAD+
-
pH 8.0, 40°C, mutant enzyme G376A
17.7
NAD+
pH 7.6, 70°C, recombinant mutant R58L
18
NAD+
-
pH 8.0, 40°C, mutant V126M
18.2
NAD+
pH 7.6, 70°C, recombinant mutants S261N and A335E
19
NAD+
-
pH 7.6, 40°C, reaction with isopropylmalate
20
NAD+
-
pH 8.0, 60°C, wild-type
21
NAD+
-
pH 8.0, 60°C, mutant V126E
21.3
NAD+
pH 7.6, 70°C, recombinant mutant H197K
25.2
NAD+
pH 7.6, 70°C, recombinant mutant L134N/V181T/P324T/A335E
29.9
NAD+
pH 7.6, 70°C, recombinant mutant L134N
30.5
NAD+
-
pH 8.0, 60°C, mutant V126I
42
NAD+
-
pH 8.0, 60°C, mutant V126F
44.5
NAD+
-
pH 8.0, 60°C, mutant V126L
44.7
NAD+
-
pH 8.0, 70°C, mutant enzyme C275T
45.8
NAD+
-
pH 8.0, 70°C, wild-type enzyme
50.1
NAD+
-
pH 8.0, 70°C, mutant enzyme A31G/G43A/A709G
54
NAD+
-
pH 8.0, 60°C, mutant V126M
63.6
NAD+
-
pH 8.0, 70°C, mutant enzyme G43A
79
NAD+
pH 8.0, 70°C, wild-type enzyme
100
NAD+
-
pH 8.0, 70°C, mutant enzyme G376A
100
NAD+
-
55°C, mutant enzyme A172D
107
NAD+
-
55°C, wild-type enzyme
111
NAD+
-
55°C, mutant enzyme A172Q
117
NAD+
-
55°C, mutant enzyme A172E and A172N
163
NAD+
60°C, pH 7.6, wild-type enzyme
220
NAD+
60°C, pH 7.6, pH 7.6, mutant enzyme A172V
0.09
NADP+
-
pH 7.3, 21°C, reaction with isopropylmalate, mutant enzyme S226R/D278K/I279Y
0.1
NADP+
-
pH 7.3, 21°C, reaction with tartrate, wild-type enzyme
0.26
NADP+
-
pH 7.3, 21°C, reaction with isopropylmalate, wild-type enzyme
0.88
NADP+
-
pH 7.3, 21°C, reaction with isopropylmalate, mutant enzyme S226R
1.66
NADP+
-
pH 7.3, 21°C, reaction with isopropylmalate, wild-type enzyme
4.69
NADP+
-
pH 7.3, 21°C, reaction with malate, wild-type enzyme
0.1
Tartrate
-
pH 7.3, 21°C, reaction with NADP+, wild-type enzyme
0.19
Tartrate
-
pH 7.3, 21°C, reaction with NAD+, wild-type enzyme
0.21
Tartrate
-
pH 7.3, 21°C, reaction with NAD+, mutant enzyme E87G
0.26
Tartrate
-
pH 7.3, 21°C, reaction with NAD+, mutant enzyme E87Q
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E57V/R85M/Y86A/M208T/F217Y/V238M/R310M
no (2R,3S)-3-isopropylmalate dehydrogenase activity detected
E57V/S72I/R85M/Y86A/F217Y/V238M/R310M
no (2R,3S)-3-isopropylmalate dehydrogenase activity detected
E57V/S72I/R85M/Y86A/M208T/F217Y/R310M
in comparison to mutant H15Y/E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M this mutant shows a significant decrease in kcat ((2R,3S)-3-isopropylmalate), alteration of Km value only moderate
E57V/S72I/R85M/Y86A/M208T/F217Y/V238M
in comparison to mutant H15Y/E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M this mutant shows a significant decrease in kcat ((2R,3S)-3-isopropylmalate), alteration of Km value only moderate
E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M
in comparison to mutant H15Y/E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M this mutant shows a larger kcat ((2R,3S)-3-isopropylmalate) and a larger Km((2R,3S)-3-isopropylmalate) or (NAD+) temperatures giving half of the initial activity is 87.8 °C
E57V/S72I/R85M/Y86A/M208T/V238M/R310M
in comparison to mutant H15Y/E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M this mutant shows a significant decrease in kcat ((2R,3S)-3-isopropylmalate), alteration of Km value only moderate
E57V/S72I/R85V/Y86A/M208T/F217Y/V238M/R310M
no (2R,3S)-3-isopropylmalate dehydrogenase activity detected
H15Y/E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M
TtHICDH variant with considerably higher IPMDH activity than double mutant R85V/Y86A, Km ((2R,3S)-3-isopropylmalate) or (NAD+) lower than wild-type HICDH but still considerably higher than wild-type (2R,3S)-3-isopropylmalate dehydrogenase, kcat ((2R,3S)-3-isopropylmalate) much higher than wild-type HICDH but still considerably lower than wild-type (2R,3S)-3-isopropylmalate dehydrogenase, temperatures giving half of the initial activity is 79.9 °C, crystal structure determined at 2.4 A, mutant is a homotetramer
R85V/Y86A
TtHICDH variant with high IPMDH activity, Km ((2R,3S)-3-isopropylmalate) or (NAD+) lower than wild-type HICDH but still considerably higher than wild-type (2R,3S)-3-isopropylmalate dehydrogenase, kcat ((2R,3S)-3-isopropylmalate) higher than wild-type HICDH but still considerably lower than wild-type (2R,3S)-3-isopropylmalate dehydrogenase, temperatures giving half of the initial activity is 92.5 °C
S72I/R85M/Y86A/M208T/F217Y/V238M/R310M
in comparison to mutant H15Y/E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M this mutant shows a significant decrease in kcat ((2R,3S)-3-isopropylmalate), alteration of Km value only moderate
A172E
-
enhanced thermostability compared to wild-type enzyme
A172G
-
melting temperature is reduced by 0.3°C compared to wild-type enzyme, crystal structure is similar to that of the wild-type enzyme
A172I
-
melting temperature is increased by 2°C compared to wild-type enzyme
A172N
-
enhanced thermostability compared to wild-type enzyme
A172Q
-
enhanced thermostability compared to wild-type enzyme
A31G/G43A/A709G
-
optimum temperature is shifted to lower temperatures compared to wild-type enzyme, activity is less temperature dependent than that of the wild-type, resulting in higher activity at temperatures below 60°C, improved turnover-numbers at 40°Cm increase in Km-values, slight loss of thermal stability
C275T
-
similar pH-dependence to that of the wild-type enzyme, improved binding affinities for both D-3-isopropylmalate and NAD+ result in an improved catalytic efficiency, mutant enzyme retains thermal stability
D217A
the mutant retains 1.1% of the catalytic activity of the wild type enzyme
D241A
the mutant shows a drastic decrease in the kcat value (0.06% compared to that of the wild type enzyme)
D245A
the mutant retains 10.5% of the catalytic activity of the wild type enzyme
E87G
-
mutation does not affect the dissociation constant from the binary complex, but does greatly increase the KM-values
E87Q
-
mutation does not affect the dissociation constant from the binary complex, but does greatly increase the KM-values
G240A
-
decreased thermostability
G376A
-
optimum temperature is shifted to lower temperatures compared to wild-type enzyme, activity is less temperature dependent than that of the wild-type, resulting in higher activity at temperatures below 60°C, improved turnover-numbers at 40°C, increase in Km-values, mutant enzyme retains thermal stability
G43A
-
optimum temperature is shifted to lower temperatures compared to wild-type enzyme, activity is less temperature dependent than that of the wild-type, resulting in higher activity at temperatures below 60°C, improved turnover-numbers at 40°C, increase ion Km-values, slight loss of thermal stability
K185A
the mutant shows a drastic decrease in the kcat value (0.06% compared to that of the wild type enzyme)
L134N/V181T/P324T/A335E
site-directed mutagenesis, exchange of residues for those of ancestral mutants, the mutant shows increased thermal stability compared to the wild-type enzyme, the mutant shows increased thermal stability compared to the wild-type enzyme
L204F
-
higher thermostability compared to wild-type enzyme, denaturation rates at 68°C and 70°C are slower
L246E/V249M
-
decreased thermostability
N102A
the mutant retains 13% of the catalytic activity of the wild type enzyme
S226R
-
Km-value for NADP+ is about 40% compared to wild-type enzyme, Km-value for NAD+ is 2.6fold higher compared to wild-type enzyme
S226R/D278K/I279Y
-
Km-value for NADP+ is about 0.8% compared to wild-type enzyme, Km-value for NAD+ is 153fold higher compared to wild-type enzyme
T16V
site-directed mutagenesis, exchange of a cofactor binding residue to the residue of the ancestral mutant, the mutant shows increased thermal stability compared to the wild-type enzyme
V126A
-
the mutation decreases the KM value of DL-3-isopropylmalate at 60°C in comparison to wild-type
V126E
-
the mutation increases the KM value of DL-3-isopropylmalate at 60°C in comparison to wild-type
V126F
-
the mutation increases the KM value of DL-3-isopropylmalate at 60°C in comparison to wild-type
V126G
-
the mutation decreases the KM value of DL-3-isopropylmalate at 60°C in comparison to wild-type
V126I
-
the mutation increases the KM value of DL-3-isopropylmalate at 60°C in comparison to wild-type
V126L
-
the mutation increases the KM value of DL-3-isopropylmalate at 60°C in comparison to wild-type
V126M
-
the mutation increases the KM value of DL-3-isopropylmalate at 60°C in comparison to wild-type
V126S
-
the mutation decreases the KM value of DL-3-isopropylmalate at 60°C in comparison to wild-type
V126T
-
the mutation decreases the KM value of DL-3-isopropylmalate at 60°C in comparison to wild-type
V181T/P324T/A335E
site-directed mutagenesis, exchange of residues for those of ancestral mutants, the mutant highly shows increased thermal stability compared to the wild-type enzyme, the mutant shows decreased thermal stability compared to the wild-type enzyme
W152F
site-directed mutagenesis, the W152F mutation causes a significant decrease in the amplitude of only the slow part of refolding, without influencing the amplitude of the burst part, the mutant shows an altered tertiary structure compared to the wild-type enzyme conformation
W152F/W195F
site-directed mutagenesis, the W152F mutation causes a significant decrease in the amplitude of only the slow part of refolding, without influencing the amplitude of the burst part, the mutant shows an altered tertiary structure compared to the wild-type enzyme conformation
W77F/W152F
site-directed mutagenesis, the W152F mutation causes a significant decrease in the amplitude of only the slow part of refolding, without influencing the amplitude of the burst part, the mutant shows an altered tertiary structure compared to the wild-type enzyme conformation
Y139A
the mutant retains 2.9% of the catalytic activity of the wild type enzyme
A172D
-
enhanced thermostability compared to wild-type enzyme
A172D
-
melting temperature is reduced by 2.7°C compared to wild-type enzyme
A172F
-
mutation causes rearrangement in domain structure, which leads to a higher thermostability compared to wild-type enzyme
A172F
-
melting temperature is increased by 1.8°C compared to wild-type enzyme
A172L
-
mutation causes rearrangement in domain structure, which leads to a higher thermostability compared to wild-type enzyme
A172L
-
melting temperature is increased by 3°C compared to wild-type enzyme
A172L
the mutant shows improved thermal stability compared to the wild type enzyme
A172V
-
melting temperature is increased by 1°C compared to wild-type enzyme, crystal structure is similar to that of the wild-type enzyme
A172V
mutation improves thermal stability, without significantly changing its catalytic properties
A335E
site-directed mutagenesis, exchange of a cofactor binding residue to the residue of the ancestral mutant, the mutant shows increased thermal stability compared to the wild-type enzyme
A335E
site-directed mutagenesis, exchange of a residue for that of ancestral mutants, the mutant shows increased thermal stability compared to the wild-type enzyme, the mutant shows increased thermal stability compared to the wild-type enzyme
D184H
site-directed mutagenesis, exchange of a cofactor binding residue to the residue of the ancestral mutant, the mutant shows increased thermal stability compared to the wild-type enzyme
D184H
site-directed mutagenesis, exchange of a residue for that of ancestral mutants, the mutant shows increased catalytic efficiency with NAD+ compared to the wild-type enzyme
E270A
the mutant exhibits largely reduced (about 1%) catalytic activity and negligible activation by K+ compared to the wild type enzyme
E270A
the mutation leads to a significant increase in the Km value for NAD+ compared to the wild type enzyme
F53L
site-directed mutagenesis, exchange of a cofactor binding residue to the residue of the ancestral mutant, the mutant shows decreased thermal stability compared to the wild-type enzyme
F53L
site-directed mutagenesis, exchange of a residue for that of ancestral mutants, the mutant shows increased catalytic efficiency with NAD+ compared to the wild-type enzyme
H179K
site-directed mutagenesis, exchange of a cofactor binding residue to the residue of the ancestral mutant, the mutant shows decreased thermal stability compared to the wild-type enzyme
H179K
site-directed mutagenesis, exchange of a residue for that of ancestral mutants, the mutant shows increased catalytic efficiency with NAD+ compared to the wild-type enzyme
L134N
site-directed mutagenesis, exchange of a cofactor binding residue to the residue of the ancestral mutant, the mutant shows increased thermal stability compared to the wild-type enzyme
L134N
site-directed mutagenesis, exchange of a residue for that of ancestral mutants, the mutant shows increased thermal stability compared to the wild-type enzyme, the mutant shows highly increased thermal stability compared to the wild-type enzyme
P324T
site-directed mutagenesis, exchange of a cofactor binding residue to the residue of the ancestral mutant, the mutant shows increased thermal stability compared to the wild-type enzyme
P324T
site-directed mutagenesis, exchange of a residue for that of ancestral mutants, the mutant shows increased thermal stability compared to the wild-type enzyme, the mutant shows increased thermal stability compared to the wild-type enzyme
P56E
site-directed mutagenesis, exchange of a cofactor binding residue to the residue of the ancestral mutant, the mutant shows increased thermal stability compared to the wild-type enzyme
P56E
site-directed mutagenesis, exchange of a residue for that of ancestral mutants, the mutant shows increased catalytic efficiency with NAD+ compared to the wild-type enzyme
R58L
site-directed mutagenesis, exchange of a cofactor binding residue to the residue of the ancestral mutant, the mutant shows decreased thermal stability compared to the wild-type enzyme
R58L
site-directed mutagenesis, exchange of a residue for that of ancestral mutants, the mutant shows increased catalytic efficiency with NAD+ compared to the wild-type enzyme
S261N
site-directed mutagenesis, exchange of a cofactor binding residue to the residue of the ancestral mutant, the mutant shows decreased thermal stability compared to the wild-type enzyme
S261N
site-directed mutagenesis, exchange of a residue for that of ancestral mutants, the mutant shows slightly increased catalytic efficiency with NAD+ compared to the wild-type enzyme
V181T
site-directed mutagenesis, exchange of a cofactor binding residue to the residue of the ancestral mutant, the mutant shows increased thermal stability compared to the wild-type enzyme
V181T
site-directed mutagenesis, exchange of a residue for that of ancestral mutants, the mutant shows decreased thermal stability compared to the wild-type enzyme, the mutant shows decreased thermal stability compared to the wild-type enzyme
V61I
site-directed mutagenesis, exchange of a cofactor binding residue to the residue of the ancestral mutant, the mutant shows decreased thermal stability compared to the wild-type enzyme
V61I
site-directed mutagenesis, exchange of a residue for that of ancestral mutants, the mutant shows slightly increased catalytic efficiency with NAD+ compared to the wild-type enzyme
additional information
designing thermostable 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree and ancestral mutant sequences, overview
additional information
-
designing thermostable 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree and ancestral mutant sequences, overview
additional information
one or a combination of amino acid(s) in 3-isopropylmalate dehydrogenase is/are substituted by a residue(s) found in the Escherichia coli enzyme at the same position(s). The best mutant, which contains three amino acid substitutions, shows a 17fold higher specific activity at 25°C compared to the original wild-type enzyme while retaining high thermal stability. The kinetic and thermodynamic parameters of the mutant show similar patterns along the reaction coordinate to those of the mesophilic enzyme
additional information
-
one or a combination of amino acid(s) in 3-isopropylmalate dehydrogenase is/are substituted by a residue(s) found in the Escherichia coli enzyme at the same position(s). The best mutant, which contains three amino acid substitutions, shows a 17fold higher specific activity at 25°C compared to the original wild-type enzyme while retaining high thermal stability. The kinetic and thermodynamic parameters of the mutant show similar patterns along the reaction coordinate to those of the mesophilic enzyme
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Onodera, K.; Moriyama, H.; Takenaka, A.; Tanaka, N.; Akutsu, N.; Muro, M.; Oshima, T.; Imada, K.; Sato, M.; Katsube, Y.
Crystallization and preliminary X-ray studies of a Bacillus subtilis and Thermus thermophilus HB8 chimeric 3-isopropylmalate dehydrogenase
J. Biochem.
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1-2
1991
Bacillus subtilis, Thermus thermophilus
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Purification, catalytic properties, and thermal stability of threo-Ds-3-isopropylmalate dehydrogenase coded by leuB gene from an extreme thermophile, Thermus thermophilus strain HB8
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449-456
1990
Thermus thermophilus
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Kakinuma, K.; Ozawa, K.; Fujimoto, Y.; Akutsu, N.; Oshima, T.
Stereochemistry of the decarboxylation reaction catalysed by 3-isopropylmalate dehydrogenase from the thermophilic bacterium Thermus thermophilus
J. Chem. Soc. Chem. Commun.
1989
1190-1192
1989
Thermus thermophilus
-
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Crystallization and preliminary X-ray data for 3-isopropylmalate dehydrogenase of Thermus thermophilus
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1988
Thermus thermophilus
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Hamasawa, K.; Kobayashi, Y.; Harada, S.; Yoda, K.; Yamasaki, M.; Tamura, G.
Molecular cloning and nucleotide sequence of the 3-isopropylmalate dehydrogenase gene of Candida utilis
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133
1089-1097
1987
Cyberlindnera jadinii, Saccharomyces cerevisiae, Thermus thermophilus
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Cloning and DNA homology of 3-isopropylmalate dehydrogenase genes from thermophilic bacilli
FEMS Microbiol. Lett.
36
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1986
[Bacillus] caldolyticus, [Bacillus] caldotenax, Bacillus subtilis, Saccharomyces cerevisiae, Escherichia coli, Thermus thermophilus
-
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DNA and amino-acid sequences of 3-isopropylmalate dehydrogenase of Bacillus coagulans. Comparison with the enzymes of Saccharomyces cerevisiae and Thermus thermophilus
Biochim. Biophys. Acta
867
36-44
1986
Weizmannia coagulans, Bacillus subtilis, Saccharomyces cerevisiae, Thermus thermophilus
-
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Tanaka, T.; Kawano, N.; Oshima, T.
Cloning of 3-isopropylmalate dehydrogenase gene of an extreme thermophile and partial purification of the gene product
Biochemistry
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Croft, J.E.; Love, D.R.; Bergquist, P.L.
Expression of leucine genes from an extremely thermophilic bacterium in Escherichia coli
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Escherichia coli, Thermus thermophilus, Salmonella enterica subsp. enterica serovar Typhimurium
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Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus
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1997
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Dean, A.M.; Dvorak, L.
The role of glutamate 87 in the kinetic mechanism of Thermus thermophilus isopropylmalate dehydrogenase
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Adaptation of a thermophilic enzyme, 3-isopropylmalate dehydrogenase, to low temperatures
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Redesigning secondary structure to invert coenzyme specificity in isopropylmalate dehydrogenase
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Qu, C.; Akanuma, S.; Tanaka, N.; Moriyama, H.; Oshima, T.
Design, X-ray crystallography, molecular modelling and thermal stability studies of mutant enzymes at site 172 of 3-isopropylmalate dehydrogenase from Thermus thermophilus
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Thermus thermophilus (Q5SIY4), Thermus thermophilus
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Thermus thermophilus (Q5SIY4), Thermus thermophilus
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Thermus thermophilus
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Thermus thermophilus (Q5SIY4), Thermus thermophilus
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Thermus thermophilus (Q5SIY4), Thermus thermophilus
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Thermus thermophilus (Q5SIY4), Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SIY4)
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Thermus thermophilus (Q5SIY4), Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SIY4)
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Thermus thermophilus (Q5SIY4), Thermus thermophilus
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