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(2R)-3-sulfolactate + NAD+
3-sulfopyruvate + NADH + H+
(S)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
1-hydroxy-1,3,4,6-hexanetetracarboxylate + NAD+
1-oxo-1,3,4,6-hexanetetracarboxylate + NADH + H+
-
-
-
r
2-hydroxycaproate + NAD+
2-oxocaproate + NADH + H+
-
-
-
r
2-hydroxyisocaproate + NAD+
2-oxoisocaproate + NADH + H+
the initial rate of the reduction of 2-oxoisocaproate is about seven times faster than the reverse reaction, the dehydrogenation of L-2-hydroxyisocaproate, measured in buffers at the respective pH optima
-
-
r
2-hydroxyisovalerate + NAD+
2-oxoisovalerate + NADH + H+
-
-
-
r
2-hydroxyoctanoate + NAD+
2-oxooctanoate + NADH + H+
-
-
-
?
2-hydroxyvalerate + NAD+
2-oxovalerate + NADH + H+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxocaproate + NADH + H+
2-hydroxycaproate + NAD+
2-oxoglutarate + NADH + H+
(S)-2-hydroxyglutarate + NAD+
-
-
-
?
2-oxoglutarate + NADH + H+
2-hydroxyglutarate + NAD+
2-oxoisocaproate + NADH + H+
2-hydroxyisocaproate + NAD+
2-oxoisovalerate + NADH + H+
2-hydroxyisovalerate + NAD+
-
-
-
r
2-oxooctanoate + NADH + H+
2-hydroxyoctanoate + NAD+
-
-
-
r
2-oxopentanedioic acid + NADH + H+
2-hydroxypentandioic acid + NAD+
-
-
-
?
2-oxovalerate + NADH + H+
2-hydroxyvalerate + NAD+
-
-
-
r
3-phenyllactate + NAD+
pyruvate + NADH + H+
-
-
-
r
3-sulfopyruvate + NADH + H+
(S)-3-sulfolactate + NAD+
3-sulfopyruvate + NADH + H+
3-sulfolactate + NAD+
4-methyl-2-oxopentanoate + NADH + H+
(S)-2-hydroxy-4-methylpentanoate + NAD+
-
-
-
r
a 2-oxocarboxylate + NADH + H+
(2S)-2-hydroxycarboxylate + NAD+
glyoxylate + NADH + H+
2-hydroxypropanoate + NAD+
-
-
-
?
L-lactate + NAD+
pyruvate + NADH + H+
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
oxaloacetate + NADH + H+
malate + NAD+
oxo-tert-leucine + NADH + H+
? + NAD+
-
-
-
r
oxopropandioic acid + NADH + H+
2-hydroxypropanedioic acid + NAD+
-
-
-
?
phenylglyoxylate + NADH + H+
? + NAD+
-
-
-
r
phenylpyruvate + NADH + H+
3-phenyllactate + NAD+
pyruvate + NADH + H+
(S)-lactate + NAD+
-
-
-
?
pyruvate + NADH + H+
L-lactate + NAD+
sulfopyruvate + NADH + H+
sulfo-2-hydroxypropanoate + NAD+
additional information
?
-
(2R)-3-sulfolactate + NAD+
3-sulfopyruvate + NADH + H+
-
-
-
r
(2R)-3-sulfolactate + NAD+
3-sulfopyruvate + NADH + H+
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
-
-
r
2-oxocaproate + NADH + H+
2-hydroxycaproate + NAD+
-
-
-
r
2-oxocaproate + NADH + H+
2-hydroxycaproate + NAD+
-
-
-
-
r
2-oxocaproate + NADH + H+
2-hydroxycaproate + NAD+
2-oxocaproate is the best substrate for the wild-type enzyme
-
-
r
2-oxoglutarate + NADH + H+
2-hydroxyglutarate + NAD+
0.2% activity compared to sulfopyruvate
-
-
r
2-oxoglutarate + NADH + H+
2-hydroxyglutarate + NAD+
0.2% activity compared to sulfopyruvate
-
-
r
2-oxoisocaproate + NADH + H+
2-hydroxyisocaproate + NAD+
-
-
-
r
2-oxoisocaproate + NADH + H+
2-hydroxyisocaproate + NAD+
2-oxoisocaproate is the best substrate with the lowest KM-valus of 0.065 mM. Tthe initial rate of the reduction of 2-oxoisocaproate is about seven times faster than the reverse reaction, the dehydrogenation of L-2-hydroxyisocaproate, measured in buffers at the respective pH optima
-
-
r
3-sulfopyruvate + NADH + H+
(S)-3-sulfolactate + NAD+
-
-
-
r
3-sulfopyruvate + NADH + H+
(S)-3-sulfolactate + NAD+
-
-
-
r
3-sulfopyruvate + NADH + H+
3-sulfolactate + NAD+
-
-
-
?
3-sulfopyruvate + NADH + H+
3-sulfolactate + NAD+
-
-
-
-
?
3-sulfopyruvate + NADH + H+
3-sulfolactate + NAD+
-
-
-
-
?
a 2-oxocarboxylate + NADH + H+
(2S)-2-hydroxycarboxylate + NAD+
-
-
-
r
a 2-oxocarboxylate + NADH + H+
(2S)-2-hydroxycarboxylate + NAD+
various 2-oxocarboxylic acids are stereospecifically reduced to the corresponding (S)-2-hydroxycarboxylic acids. In the reverse reaction the NAD+-dependent dehydrogenation of L-2-hydroxycarboxylic acids is observed
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
?
oxaloacetate + NADH + H+
(S)-malate + NAD+
transfer of pro-4S hydrogen from the reduced coenzyme to the 2-oxoacid substrate
-
-
?
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
?
oxaloacetate + NADH + H+
(S)-malate + NAD+
transfer of pro-4S hydrogen from the reduced coenzyme to the 2-oxoacid substrate
-
-
?
oxaloacetate + NADH + H+
malate + NAD+
31% activity compared to sulfopyruvate
-
-
r
oxaloacetate + NADH + H+
malate + NAD+
31% activity compared to sulfopyruvate
-
-
r
oxaloacetate + NADH + H+
malate + NAD+
-
-
-
?
phenylpyruvate + NADH + H+
3-phenyllactate + NAD+
-
-
-
r
phenylpyruvate + NADH + H+
3-phenyllactate + NAD+
-
-
-
-
r
phenylpyruvate + NADH + H+
3-phenyllactate + NAD+
-
-
-
r
pyruvate + NADH + H+
L-lactate + NAD+
-
-
-
r
pyruvate + NADH + H+
L-lactate + NAD+
-
-
-
-
r
pyruvate + NADH + H+
L-lactate + NAD+
-
-
-
r
sulfopyruvate + NADH + H+
sulfo-2-hydroxypropanoate + NAD+
-
-
-
r
sulfopyruvate + NADH + H+
sulfo-2-hydroxypropanoate + NAD+
preferred substrate
-
-
r
sulfopyruvate + NADH + H+
sulfo-2-hydroxypropanoate + NAD+
-
-
-
r
sulfopyruvate + NADH + H+
sulfo-2-hydroxypropanoate + NAD+
preferred substrate
-
-
r
additional information
?
-
enzyme additionally functions as malate dehydrogenase, reducing oxalacetate to (S)-malate using either NADH or NADPH as a reductant. No substrate: pyruvate
-
-
?
additional information
?
-
-
enzyme additionally functions as malate dehydrogenase, reducing oxalacetate to (S)-malate using either NADH or NADPH as a reductant. No substrate: pyruvate
-
-
?
additional information
?
-
enzyme catalyzes the NADH-dependent reduction of oxaloacetate, 2-oxoglutarate, and pyruvate to the corresponding (S)-2-hydroxyacids with pro-S NADH-stereospecificity
-
-
?
additional information
?
-
no substrates: pyruvate, 2-oxobutanoate, 2-oxovalerate, ketoisovalerate, 2-oxohexanedioate, 2-ketohexanedioate, 3-methyl 2-oxovalerate and 4-methyl-2-oxovalerate
-
-
?
additional information
?
-
-
no substrates: pyruvate, 2-oxobutanoate, 2-oxovalerate, ketoisovalerate, 2-oxohexanedioate, 2-ketohexanedioate, 3-methyl 2-oxovalerate and 4-methyl-2-oxovalerate
-
-
?
additional information
?
-
enzyme additionally functions as malate dehydrogenase, reducing oxalacetate to (S)-malate using either NADH or NADPH as a reductant. No substrate: 2-oxoglutarate, pyruvate, 1-oxo-1,3,4,6-hexanetetracarboxylate
-
-
?
additional information
?
-
-
enzyme additionally functions as malate dehydrogenase, reducing oxalacetate to (S)-malate using either NADH or NADPH as a reductant. No substrate: 2-oxoglutarate, pyruvate, 1-oxo-1,3,4,6-hexanetetracarboxylate
-
-
?
additional information
?
-
broad substrate specificity, utilizes a wide range of 2-oxo acids branched at the C4 atom
-
-
?
additional information
?
-
-
broad substrate specificity, utilizes a wide range of 2-oxo acids branched at the C4 atom
-
-
?
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15
1-oxo-1,3,4,6-hexanetetracarboxylate
cosubstrate NADH, pH 8.0, 70°C
2.2
2-hydroxycaproate
pH 8.0, 30°C
0.62
2-hydroxyisocaproate
pH 8.0, 30°C
0.6
2-Hydroxyisovalerate
pH 8.0, 30°C
1.9
2-Hydroxyoctanoate
pH 8.0, 30°C
1.8
2-hydroxyvalerate
pH 8.0, 30°C
0.45
2-oxobutyrate
pH 7.0, 30°C
1.9
2-oxoglutarate
cosubstrate NADH, pH 8.0, 70°C
0.06
2-oxoisocaproate
pH 7.0, 30°C
0.065
2-oxoisovalerate
pH 7.0, 30°C
0.17
2-oxooctanoate
pH 7.0, 30°C
1.9
2-oxopentanedioic acid
pH 8.0, 70°C
0.1
2-oxovalerate
pH 7.0, 30°C
0.64
3-Phenyllactate
pH 8.0, 30°C
0.04 - 0.21
3-sulfopyruvate
0.067 - 110
4-methyl-2-oxopentanoate
46
glyoxylate
pH 8.0, 70°C
100
L-lactate
pH 8.0, 30°C
3.4
oxopropandioic acid
pH 8.0, 70°C
0.026 - 19
phenylpyruvate
0.196
sulfopyruvate
pH 6.5, 37°C
additional information
additional information
typical Michaelis-Menten kinetics, comparison to ComC enzymes from other rumen methanogens from Methanobrevibacter
-
0.071
2-oxocaproate
pH 7.0, 30°C, mutant enzyme delP88
0.1 - 1
2-oxocaproate
pH 7.0, 30°C, wild-type enzyme
0.1 - 2
2-oxocaproate
pH 7.0, 30°C
0.62
2-oxocaproate
pH 7.0, 30°C, mutant enzyme delN87/delP88
2
2-oxocaproate
pH 7.0, 30°C, mutant enzyme delN87
5
2-oxocaproate
pH 7.0, 30°C, mutant enzyme delK82
6.4
2-oxocaproate
pH 7.0, 30°C, mutant enzyme del L83
18
2-oxocaproate
pH 7.0, 30°C, mutant enzyme del I81
19
2-oxocaproate
pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88
62
2-oxocaproate
pH 7.0, 30°C, mutant enzyme del I81/delK82
0.04
3-sulfopyruvate
pH 8.0, 70°C
0.04
3-sulfopyruvate
cosubstrate NADH, pH 8.0, 70°C
0.07
3-sulfopyruvate
cosubstrate NADH, pH 8.0, 70°C
0.21
3-sulfopyruvate
cosubstrate NADPH, pH 8.0, 70°C
0.21
3-sulfopyruvate
cosubstrate NADPH, pH 8.0, 70°C
0.067
4-methyl-2-oxopentanoate
pH 7.0, 30°C, wild-type enzyme
0.17
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme delP88
0.9 - 1
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme delN87
1 - 4
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme del I81/delK82
2.8
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme delN87/delP88
11
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme del L83
18
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme del I81
43
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88
110
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme delK82
0.11
oxaloacetate
cosubstrate NADH, pH 8.0, 70°C
0.13
oxaloacetate
pH 8.0, 70°C
0.13
oxaloacetate
cosubstrate NADH, pH 8.0, 70°C
0.95
oxaloacetate
cosubstrate NADPH, pH 8.0, 70°C
5.32
oxaloacetate
cosubstrate NADPH, pH 8.0, 70°C
0.026
phenylpyruvate
pH 7.0, 30°C, wild-type enzyme
0.1 - 2
phenylpyruvate
pH 7.0, 30°C
0.1 - 2
phenylpyruvate
pH 7.0, 30°C, mutant enzyme delP88
0.33
phenylpyruvate
pH 7.0, 30°C, mutant enzyme delN87/delP88
0.41
phenylpyruvate
pH 7.0, 30°C, mutant enzyme delN87
2.8
phenylpyruvate
pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88
2.8
phenylpyruvate
pH 7.0, 30°C, mutant enzyme del L83
3.3
phenylpyruvate
pH 7.0, 30°C, mutant enzyme del I81/delK82
5.8
phenylpyruvate
pH 7.0, 30°C, mutant enzyme del I81
19
phenylpyruvate
pH 7.0, 30°C, mutant enzyme delK82
2 - 5
pyruvate
pH 7.0, 30°C, mutant enzyme delN87
3.5
pyruvate
pH 7.0, 30°C, wild-type enzyme
4.5
pyruvate
pH 7.0, 30°C
9.3
pyruvate
pH 7.0, 30°C, mutant enzyme del I81
27
pyruvate
pH 7.0, 30°C, mutant enzyme delN87/delP88
30
pyruvate
pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88
50
pyruvate
pH 7.0, 30°C, mutant enzyme delP88
140
pyruvate
pH 7.0, 30°C, mutant enzyme del I81/delK82
200
pyruvate
pH 7.0, 30°C, mutant enzyme delK82
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.63 - 360000
2-oxocaproate
2 - 13000
2-oxoisocaproate
1.7 - 520000
4-methyl-2-oxopentanoate
0.07 - 52
oxo-tert-leucine
0.1 - 18000
phenylglyoxylate
62.8
sulfopyruvate
pH 6.5, 37°C
0.63
2-oxocaproate
pH 7.0, 30°C, mutant enzyme del I81
6.58
2-oxocaproate
pH 7.0, 30°C, mutant enzyme L239M/T245A
13
2-oxocaproate
pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88
20
2-oxocaproate
pH 7.0, 30°C, mutant enzyme del I81/delK82
27
2-oxocaproate
pH 7.0, 30°C, mutant enzyme T245A
40
2-oxocaproate
pH 7.0, 30°C, mutant enzyme delK82
320
2-oxocaproate
pH 7.0, 30°C, mutant enzyme L239F
620
2-oxocaproate
pH 7.0, 30°C, mutant enzyme delP88
1000
2-oxocaproate
pH 7.0, 30°C, mutant enzyme del L 83
2100
2-oxocaproate
pH 7.0, 30°C, mutant enzyme F236S
2400
2-oxocaproate
pH 7.0, 30°C, mutant enzyme L239W
4400
2-oxocaproate
pH 7.0, 30°C, mutant enzyme delN87
5600
2-oxocaproate
pH 7.0, 30°C, mutant enzyme L239A
6900
2-oxocaproate
pH 7.0, 30°C, mutant enzyme F236V
7600
2-oxocaproate
pH 7.0, 30°C, mutant enzyme G234V/G235D
7900
2-oxocaproate
pH 7.0, 30°C, mutant enzyme L239M
21000
2-oxocaproate
pH 7.0, 30°C, mutant enzyme delN87/delP88
360000
2-oxocaproate
pH 7.0, 30°C, wild-type enzyme
360000
2-oxocaproate
-
pH 7.0, 30°C, wild-type enzyme
2 - 8
2-oxoisocaproate
pH 7.0, 30°C, mutant enzyme L239M/T245A
210
2-oxoisocaproate
pH 7.0, 30°C, mutant enzyme T245A
420
2-oxoisocaproate
pH 7.0, 30°C, mutant enzyme L239F
920
2-oxoisocaproate
pH 7.0, 30°C, mutant enzyme F236S
1000
2-oxoisocaproate
pH 7.0, 30°C, mutant enzyme F236V
2400
2-oxoisocaproate
pH 7.0, 30°C, wild-type enzyme
2500
2-oxoisocaproate
pH 7.0, 30°C, mutant enzyme G234V/G235D
3400
2-oxoisocaproate
pH 7.0, 30°C, mutant enzyme L239W
4400
2-oxoisocaproate
pH 7.0, 30°C, mutant enzyme L239A
13000
2-oxoisocaproate
pH 7.0, 30°C, mutant enzyme L239M
1.7
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme del I81
25
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme del I81/delK82
39
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88
490
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme delP88
920
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme delK82
2400
4-methyl-2-oxopentanoate
pH 7.0, 30°C, wild-type enzyme
4200
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme del L 83
15000
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme delN87
520000
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme delN87/delP88
0.07
oxo-tert-leucine
pH 7.0, 30°C, mutant enzyme F236S
0.075
oxo-tert-leucine
pH 7.0, 30°C, mutant enzyme L239M/T245A
0.2
oxo-tert-leucine
pH 7.0, 30°C, mutant enzyme G234V/G235D
0.3
oxo-tert-leucine
pH 7.0, 30°C, mutant enzyme L239A
0.4
oxo-tert-leucine
pH 7.0, 30°C, mutant enzyme L239M
32
oxo-tert-leucine
pH 7.0, 30°C, mutant enzyme T245A
52
oxo-tert-leucine
pH 7.0, 30°C, wild-type enzyme
0.1
phenylglyoxylate
pH 7.0, 30°C, mutant enzyme L239M/T245A
0.2
phenylglyoxylate
pH 7.0, 30°C, mutant enzyme F236V
1.3
phenylglyoxylate
pH 7.0, 30°C, mutant enzyme T245A
9.5
phenylglyoxylate
pH 7.0, 30°C, mutant enzyme F236S
20
phenylglyoxylate
pH 7.0, 30°C, mutant enzyme L239F
22
phenylglyoxylate
pH 7.0, 30°C, mutant enzyme L239W
92
phenylglyoxylate
pH 7.0, 30°C, mutant enzyme G234V/G235D
150
phenylglyoxylate
pH 7.0, 30°C, mutant enzyme L239M
520
phenylglyoxylate
pH 7.0, 30°C, mutant enzyme L239A
18000
phenylglyoxylate
pH 7.0, 30°C, wild-type enzyme
8
phenylpyruvate
pH 7.0, 30°C, mutant enzyme del I81
25
phenylpyruvate
pH 7.0, 30°C, mutant enzyme L239M/T245A
51
phenylpyruvate
pH 7.0, 30°C, mutant enzyme T245A
280
phenylpyruvate
pH 7.0, 30°C, mutant enzyme delK82
350
phenylpyruvate
pH 7.0, 30°C, mutant enzyme L239F
750
phenylpyruvate
pH 7.0, 30°C, mutant enzyme delP88
1200
phenylpyruvate
pH 7.0, 30°C, mutant enzyme del L 83
2500
phenylpyruvate
pH 7.0, 30°C, mutant enzyme G234V/G235D
2600
phenylpyruvate
pH 7.0, 30°C, mutant enzyme del I81/delK82
3500
phenylpyruvate
pH 7.0, 30°C, mutant enzyme L239A
4100
phenylpyruvate
pH 7.0, 30°C, mutant enzyme L239W
6400
phenylpyruvate
pH 7.0, 30°C, mutant enzyme F236S
7300
phenylpyruvate
pH 7.0, 30°C, wild-type enzyme
7300
phenylpyruvate
-
pH 7.0, 30°C, wild-type enzyme
11000
phenylpyruvate
pH 7.0, 30°C, mutant enzyme L239M
12000
phenylpyruvate
pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88
15000
phenylpyruvate
pH 7.0, 30°C, mutant enzyme F236V
19000
phenylpyruvate
pH 7.0, 30°C, mutant enzyme delN87
89000
phenylpyruvate
pH 7.0, 30°C, mutant enzyme delN87/delP88
0.004
pyruvate
pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88
0.03
pyruvate
pH 7.0, 30°C, mutant enzyme del I81/delK82
0.1
pyruvate
pH 7.0, 30°C, mutant enzyme F236V
0.2
pyruvate
pH 7.0, 30°C, mutant enzyme L239W
0.23
pyruvate
pH 7.0, 30°C, mutant enzyme del I81
0.76
pyruvate
pH 7.0, 30°C, mutant enzyme delK82
0.9
pyruvate
pH 7.0, 30°C, mutant enzyme L239A
15
pyruvate
pH 7.0, 30°C, mutant enzyme delN87
17
pyruvate
pH 7.0, 30°C, mutant enzyme delN87/delP88
20
pyruvate
pH 7.0, 30°C, mutant enzyme F236S
46
pyruvate
pH 7.0, 30°C, mutant enzyme delP88
90
pyruvate
pH 7.0, 30°C, wild-type enzyme
90
pyruvate
-
pH 7.0, 30°C, wild-type enzyme
100
pyruvate
pH 7.0, 30°C, mutant enzyme L239M
340
pyruvate
pH 7.0, 30°C, mutant enzyme G234V/G235D
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.035 - 3300000
2-oxocaproate
3.84 - 203000
2-oxoisocaproate
0.092 - 190000
4-methyl-2-oxopentanoate
0.0469 - 133
oxo-tert-leucine
0.00526 - 1880
phenylglyoxylate
1.4 - 281000
phenylpyruvate
320.4
sulfopyruvate
pH 6.5, 37°C
0.035
2-oxocaproate
pH 7.0, 30°C, mutant enzyme del I81
0.32
2-oxocaproate
pH 7.0, 30°C, mutant enzyme del I81/delK82
0.411
2-oxocaproate
pH 7.0, 30°C, mutant enzyme L239M/T245A
0.68
2-oxocaproate
pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88
8
2-oxocaproate
pH 7.0, 30°C, mutant enzyme delK82
22.5
2-oxocaproate
pH 7.0, 30°C, mutant enzyme T245A
160
2-oxocaproate
pH 7.0, 30°C, mutant enzyme del L 83
941
2-oxocaproate
pH 7.0, 30°C, mutant enzyme L239F
1920
2-oxocaproate
pH 7.0, 30°C, mutant enzyme F236V
2200
2-oxocaproate
pH 7.0, 30°C, mutant enzyme delN87
2420
2-oxocaproate
pH 7.0, 30°C, mutant enzyme L239W
2670
2-oxocaproate
pH 7.0, 30°C, mutant enzyme L239A
2880
2-oxocaproate
pH 7.0, 30°C, mutant enzyme F236S
8700
2-oxocaproate
pH 7.0, 30°C, mutant enzyme delP88
34000
2-oxocaproate
pH 7.0, 30°C, mutant enzyme delN87/delP88
37600
2-oxocaproate
pH 7.0, 30°C, mutant enzyme L239M
76000
2-oxocaproate
pH 7.0, 30°C, mutant enzyme G234V/G235D
3270000
2-oxocaproate
pH 7.0, 30°C, wild-type enzyme
3300000
2-oxocaproate
pH 7.0, 30°C, wild-type enzyme
3.84
2-oxoisocaproate
pH 7.0, 30°C, mutant enzyme L239M/T245A
117
2-oxoisocaproate
pH 7.0, 30°C, mutant enzyme T245A
400
2-oxoisocaproate
pH 7.0, 30°C, mutant enzyme F236V
677
2-oxoisocaproate
pH 7.0, 30°C, mutant enzyme L239F
1530
2-oxoisocaproate
pH 7.0, 30°C, mutant enzyme F236S
2620
2-oxoisocaproate
pH 7.0, 30°C, mutant enzyme L239W
7330
2-oxoisocaproate
pH 7.0, 30°C, mutant enzyme L239A
35800
2-oxoisocaproate
pH 7.0, 30°C, wild-type enzyme
39100
2-oxoisocaproate
pH 7.0, 30°C, mutant enzyme G234V/G235D
203000
2-oxoisocaproate
pH 7.0, 30°C, mutant enzyme L239M
0.092
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme del I81
0.91
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88
1.8
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme del I81/delK82
8.4
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme delK82
380
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme del L 83
2900
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme delP88
16000
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme delN87
36000
4-methyl-2-oxopentanoate
pH 7.0, 30°C, wild-type enzyme
190000
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme delN87/delP88
0.0469
oxo-tert-leucine
pH 7.0, 30°C, mutant enzyme L239A
0.07
oxo-tert-leucine
pH 7.0, 30°C, mutant enzyme F236S
0.357
oxo-tert-leucine
pH 7.0, 30°C, mutant enzyme G234V/G235D
1.08
oxo-tert-leucine
pH 7.0, 30°C, mutant enzyme L239M
15
oxo-tert-leucine
pH 7.0, 30°C, mutant enzyme L239M/T245A
16
oxo-tert-leucine
pH 7.0, 30°C, mutant enzyme T245A
133
oxo-tert-leucine
pH 7.0, 30°C, wild-type enzyme
0.00526
phenylglyoxylate
pH 7.0, 30°C, mutant enzyme F236V
0.0684
phenylglyoxylate
pH 7.0, 30°C, mutant enzyme T245A
2.97
phenylglyoxylate
pH 7.0, 30°C, mutant enzyme L239W
6.06
phenylglyoxylate
pH 7.0, 30°C, mutant enzyme L239F
6.13
phenylglyoxylate
pH 7.0, 30°C, mutant enzyme G234V/G235D
10
phenylglyoxylate
pH 7.0, 30°C, mutant enzyme L239M
13
phenylglyoxylate
pH 7.0, 30°C, mutant enzyme L239M/T245A
32.8
phenylglyoxylate
pH 7.0, 30°C, mutant enzyme F236S
158
phenylglyoxylate
pH 7.0, 30°C, mutant enzyme L239A
1880
phenylglyoxylate
pH 7.0, 30°C, wild-type enzyme
1.4
phenylpyruvate
pH 7.0, 30°C, mutant enzyme del I81
3.09
phenylpyruvate
pH 7.0, 30°C, mutant enzyme L239M/T245A
15
phenylpyruvate
pH 7.0, 30°C, mutant enzyme delK82
66.2
phenylpyruvate
pH 7.0, 30°C, mutant enzyme T245A
790
phenylpyruvate
pH 7.0, 30°C, mutant enzyme del I81/delK82
1460
phenylpyruvate
pH 7.0, 30°C, mutant enzyme L239F
2190
phenylpyruvate
pH 7.0, 30°C, mutant enzyme L239A
4300
phenylpyruvate
pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88
4300
phenylpyruvate
pH 7.0, 30°C, mutant enzyme del L 83
5060
phenylpyruvate
pH 7.0, 30°C, mutant enzyme L239W
6300
phenylpyruvate
pH 7.0, 30°C, mutant enzyme delP88
10000
phenylpyruvate
pH 7.0, 30°C, mutant enzyme F236V
28700
phenylpyruvate
pH 7.0, 30°C, mutant enzyme G234V/G235D
46000
phenylpyruvate
pH 7.0, 30°C, mutant enzyme delN87
49200
phenylpyruvate
pH 7.0, 30°C, mutant enzyme F236S
224000
phenylpyruvate
pH 7.0, 30°C, mutant enzyme L239M
270000
phenylpyruvate
pH 7.0, 30°C, mutant enzyme delN87/delP88
280000
phenylpyruvate
pH 7.0, 30°C, wild-type enzyme
281000
phenylpyruvate
pH 7.0, 30°C, wild-type enzyme
0.00013
pyruvate
pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88
0.00021
pyruvate
pH 7.0, 30°C, mutant enzyme del I81/delK82
0.0038
pyruvate
pH 7.0, 30°C, mutant enzyme delK82
0.01
pyruvate
pH 7.0, 30°C, mutant enzyme F236V
0.012
pyruvate
pH 7.0, 30°C, mutant enzyme L239A
0.025
pyruvate
pH 7.0, 30°C, mutant enzyme del I81
0.0465
pyruvate
pH 7.0, 30°C, mutant enzyme L239W
0.6
pyruvate
pH 7.0, 30°C, mutant enzyme delN87
0.63
pyruvate
pH 7.0, 30°C, mutant enzyme delN87/delP88
0.654
pyruvate
pH 7.0, 30°C, mutant enzyme G234V/G235D
0.92
pyruvate
pH 7.0, 30°C, mutant enzyme delP88
1.82
pyruvate
pH 7.0, 30°C, mutant enzyme F236S
5.88
pyruvate
pH 7.0, 30°C, mutant enzyme L239M
25.7
pyruvate
pH 7.0, 30°C, wild-type enzyme
26
pyruvate
pH 7.0, 30°C, wild-type enzyme
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del I81/delK82
phenylpyruvate is the only substrate which is converted at a significant catalytic rate by the mutant enzyme. In the publication this mutant is referred to as Ile100ADELTA/Lys100BDELTA, according to the numbering system of the dogfish L-lactate dehydrogenase coenzyme loop region
del I81/delK82/delN87/delP88
specific modifications in catalytic rates and substrate recognition
del L 83
deletion mutant shows an altered substrate specificity. In the publication this mutant is referred to as Leu101DELTA, according to the numbering system of the dogfish L-lactate dehydrogenase coenzyme loop region
delI81
drastic reductions in the catalytic activity for all tested substrates. In the publication this mutant is referred to as Ile100ADELTA, according to the numbering system of the dogfish L-lactate dehydrogenase coenzyme loop region
delK82
drastic reductions in the catalytic activity for all tested substrates. In the publication this mutant is referred to as Lys100BDELTA, according to the numbering system of the dogfish L-lactate dehydrogenase coenzyme loop region
delN87
deletion mutant shows an altered substrate specificity. In the publication this mutant is referred to as Asn105ADELTA, according to the numbering system of the dogfish L-lactate dehydrogenase coenzyme loop region
delN87/delP88
for the deletion mutant enzyme 2-oxo carboxylic acids branched at C4 are better substrates than 2-oxocaproate, the substrate with the best kcat,/KM ratio known for the wild-type enzyme.The mutation results in a 5.2fold increased catalytic efficiency towards 4-methyl-2-oxopentanoate compared to the wild-type enzyme. In the publication this mutant is referred to as Asn105ADELTA/Pro105BDELTA, according to the numbering system of the dogfish L-lactate dehydrogenase coenzyme loop region
delP88
deletion mutant shows an altered substrate specificity. In the publication this mutant is referred to as Pro105BDELTA, according to the numbering system of the dogfish L-lactate dehydrogenase coenzyme loop region
F236S
phenylpyruvate displays the largest kcat of the tested substrates. All kcat values, with the exception of phenylpyruvate, are reduced, but the relative acceptance of phenylglyoxylate is greatly increased
F236V
decrease in the second-order rate constants for all tested substrates. The kcat values for the smaller substrates decrease drastically. Phenylpyruvate is the favourite substrate (2-oxocaproate is the favourite substrate of the wild-type enzyme)
G234V/G235D
the second-order rate constant decreased for most substrates with the exception of pyruvate, which reacts 2.5times faster in the mutant enzyme than in the wild-type enzyme. The catalysis of 2-oxoisocaproate is unaffected
L239A
shift of enzyme specificity towards the substrates branched at C3 corresponding to an increase in the turnover numbers for 2-oxoisocaproate
L239F
slight decrease in the KM values for phenylglyoxylate combined with a dramatic decrease in the kcat values
L239M
KM values of all substrates of the enzyme variant are very similar to those of the wild-type enzyme, large improvement in the kcat values of the C4-branched substrates 2-oxoisocaproate and phenylpyruvate, decrease in the turnover number of 2-oxocaproate (the substrate favoured by the wild-type enzyme). Whereas in the wild-type enzyme the second-order rate constant for 2-oxoisocaproate is only 1% of that for the unbranched substrate, in the mutant enzyme the rate constant of 2-oxocaproate is only 18% of that for 2-oxoisocaproate
L239M/T245A
the catalytic rates are reduced by several orders of magnitude and the KM values shows at least a 100fold increase for most substrates (with the exception of phenylglyoxylate). With respect to L239M the substrate specificity shifts towards keto-tert-leucine and with respect to T245A 2-oxoisocaproate and phenylpyruvate are more favoured
L239W
slight decrease in the KM values for phenylglyoxylate combined with a dramatic decrease in the kcat values
T245A
the catalytic rates are reduced by several orders of magnitude, relative shift of substrate specificity for keto-tert-leucine of more than 17 000 compared with the 2-oxocaproate (kcat/KM)
additional information
the coenzyme loop, a functional element which is essential for catalysis and substrate specificity, is modified in order to identify the residues involved in the catalytic reaction and substrate specificity
additional information
-
the coenzyme loop, a functional element which is essential for catalysis and substrate specificity, is modified in order to identify the residues involved in the catalytic reaction and substrate specificity
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Graupner, M.; Xu, H.; White, R.H.
Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea
J. Bacteriol.
182
3688-3692
2000
Methanothermus fervidus (P16142), Methanothermus fervidus, Methanocaldococcus jannaschii (Q58820), Methanocaldococcus jannaschii
brenda
Rein, U.; Gueta, R.; Denger, K.; Ruff, J.; Hollemeyer, K.; Cook, A.M.
Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA
Microbiology
151
737-747
2005
Paracoccus pantotrophus, Paracoccus pantotrophus NKNCYSA / DSM 12449
brenda
Graupner, M.; White, R.H.
The first examples of (S)-2-hydroxyacid dehydrogenases catalyzing the transfer of the pro-4S hydrogen of NADH are found in the archaea
Biochim. Biophys. Acta
158
169-173
2001
Methanothermus fervidus (P16142), Methanocaldococcus jannaschii (Q58820)
brenda
Irimia, A.; Madern, D.; Zaccai, G.; Vellieux, F.M.
Methanoarchaeal sulfolactate dehydrogenase: prototype of a new family of NADH-dependent enzymes
EMBO J.
23
1234-1244
2004
Methanocaldococcus jannaschii (Q58820), Methanocaldococcus jannaschii
brenda
Schtte, W.; Hummel, W.; Kula, M.R.
L-2-Hydroxyisocaproate dehydrogenase - A new enzyme from Lactobacillus confusus for the stereospecific reduction of 2-ketocarboxylic acids
Appl. Microbiol. Biotechnol.
19
167-176
1984
Weissella confusa (P14295)
-
brenda
Feil, I.K.; Lerch, H.P.; Schomburg, D.
Deletion variants of L-hydroxyisocaproate dehydrogenase. Probing substrate specificity
Eur. J. Biochem.
223
857-863
1994
Weissella confusa (P14295), Weissella confusa
brenda
Lerch, H.P.; Frank, R.; Collins, J.
Cloning, sequencing and expression of the L-2-hydroxyisocaproate dehydrogenase-encoding gene of Lactobacillus confusus in Escherichia coli
Gene
83
263-270
1989
Weissella confusa (P14295), Weissella confusa
brenda
Niefind, K.; Hecht, H.J.; Schomburg, D.
Crystal structure of L-2-hydroxyisocaproate dehydrogenase from Lactobacillus confusus at 2.2 A resolution. An example of strong asymmetry between subunits
J. Mol. Biol.
251
256-281
1995
Weissella confusa (P14295), Weissella confusa
brenda
Feil, I.K.; Hendle, J.; Schomburg, D.
Modified substrate specificity of L-hydroxyisocaproate dehydrogenase derived from structure-based protein engineering
Protein Eng.
10
255-262
1997
Weissella confusa (P14295), Weissella confusa
brenda
Chatterjee, S.; Schoepe, J.; Lohmer, S.; Schomburg, D.
High level expression and single-step purification of hexahistidine-tagged L-2-hydroxyisocaproate dehydrogenase making use of a versatile expression vector set
Protein Expr. Purif.
39
137-143
2005
Weissella confusa (P14295)
brenda
Bao, L.; Chatterjee, S.; Lohmer, S.; Schomburg, D.
An irreversible and kinetically controlled process: thermal induced denaturation of L-2-hydroxyisocaproate dehydrogenase from Lactobacillus confusus
Protein J.
26
143-151
2007
Weissella confusa (P14295), Weissella confusa
brenda
Zhang, Y.; Schofield, L.R.; Sang, C.; Dey, D.; Ronimus, R.S.
Expression, purification, and characterization of (R)-sulfolactate dehydrogenase (ComC) from the rumen methanogen Methanobrevibacter millerae SM9
Archaea
2017
5793620
2017
Methanobrevibacter millerae (A0A0U3EA38), Methanobrevibacter millerae SM9 (A0A0U3EA38)
brenda