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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-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+
3-lactate + 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-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
-
-
?
phenylpyruvate + NADH + H+

3-phenyllactate + NAD+
-
-
-
r
phenylpyruvate + NADH + H+
3-phenyllactate + NAD+
-
-
-
-
r
pyruvate + NADH + H+

3-lactate + NAD+
-
-
-
r
pyruvate + NADH + H+
3-lactate + NAD+
-
-
-
-
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-stereospecifity
-
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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
0.071
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

-
cosubstrate NADH, pH 8.0, 70°C
0.04
3-sulfopyruvate
-
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
-
cosubstrate NADH, pH 8.0, 70°C
0.13
oxaloacetate
-
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; 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
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
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
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
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
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; 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
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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
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii (Q58820), Methanothermus fervidus, Methanothermus fervidus (P16142)
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
Methanocaldococcus jannaschii (Q58820), Methanothermus fervidus (P16142)
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, Methanocaldococcus jannaschii (Q58820)
brenda
Schütte, 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