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(R)-2-hydroxy-4-methylpentanoate + NAD+
4-methyl-2-oxopentanoate + NADH + H+
-
i.e. (R)-2-hydroxyisocaproate
i.e. 2-oxoisocaproate
-
r
(R)-2-hydroxycarboxylate + NAD+
a 2-oxocarboxylate + NADH + H+
(R)-mandelate + NAD+
phenylglyoxylate + NADH + H+
2-formylbutanethioate + NADH + H+
?
2-hydroxyhexanoate + NAD+
2-oxohexanoate + NADH + H+
-
-
-
-
r
2-hydroxyoctanoate + NAD+
2-oxooctanoate + NADH + H+
-
-
-
-
r
2-hydroxypentanoate + NAD+
2-oxopentanoate + NADH + H+
-
-
-
-
r
2-oxo-3-phenylpropanoate + NADH + H+
2-hydroxy-3-phenylpropanoate + NAD+
2-oxobutanoate + NADH + H+
2-hydroxybutanoate + NAD+
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
2-oxobutyrate + NADH + H+
?
2-oxobutyrate + NADH + H+
? + NAD+
2-oxobutyrate + NADH + H+
D-2-hydroxybutyrate + NAD+
2-oxocaproate + NADH + H+
?
2-oxocaproate + NADH + H+
? + NAD+
2-oxocarboxylate + NADH + H+
(R)-2-hydroxycarboxylate + NAD+
2-oxohexanoate + NADH + H+
2-hydroxyhexanoate + NAD+
2-oxoisocaproate + NADH + H+
?
2-oxoisocaproate + NADH + H+
? + NAD+
2-oxoisocaproate + NADH + H+
L-2-hydroxyisocaproate + NAD+
2-oxoisovalerate + NADH + H+
?
2-oxoisovalerate + NADH + H+
? + NAD+
-
-
-
-
r
2-oxomethylthiobutyrate + NADH + H+
? + NAD+
-
-
-
-
r
2-oxomethylvalerate + NADH + H+
? + NAD+
-
-
-
-
r
2-oxooctanoate + NADH + H+
2-hydroxyoctanoate + NAD+
-
-
-
-
r
2-oxopentanoate + NADH + H+
2-hydroxypentanoate + NAD+
2-oxovalerate + NADH + H+
?
-
-
-
-
?
2-oxovalerate + NADH + H+
? + NAD+
-
-
-
-
r
3-(4-hydroxyphenyl)-2-oxopropanoate + NADH + H+
2-hydroxy-3-(4-hydroxyphenyl)propanoate + NAD+
-
-
-
-
?
3-hydroxypyruvate + NADH + H+
?
-
-
-
-
?
3-methyl-2-oxobutanoate + NADH + H+
2-hydroxy-3-methylbutanoate + NAD+
3-methyl-2-oxobutanoate + NADH + H+
3-methyl-2-hydroxybutanoate + NAD+
3-methyl-2-oxopentanoate + NADH + H+
2-hydroxy-3-methylpentanoate + NAD+
4-methyl-2-oxopentanoate + NADH + H+
(R)-2-hydroxy-4-methylpentanoate + NAD+
4-methyl-2-oxopentanoate + NADH + H+
4-methyl-2-hydroxypentanoate + NAD+
-
highest Vmax/Km value of all substrates tested
-
-
?
benzoylformate + NADH + H+
?
benzoylformate + NADH + H+
? + NAD+
-
-
-
-
r
D-2-hydroxybutyrate + NAD+
2-oxobutyrate + NADH + H+
D-lactate + NAD+
pyruvate + NADH + H+
-
-
-
-
r
D-malate + NAD+
oxaloacetate + NADH + H+
D-mandelate + NADH + H+
? + NAD+
-
-
-
-
r
DL-2-hydroxyisocaproate + NADH + H+
? + NAD+
-
-
-
-
r
L-2-hydroxycaproate + NAD+
2-oxocaproate + NADH + H+
-
-
-
-
r
oxaloacetate + NADH + H+
D-malate + NAD+
phenylglyoxylate + NADH + H+
hydroxy(phenyl)acetic acid + NAD+
phenylpyruvate + NADH + H+
?
-
-
-
-
?
phenylpyruvate + NADH + H+
? + NAD+
phenylpyruvate + NADH + H+
phenyl-D-lactate + NAD+
phenylpyruvate + NADH + H+
phenyllactate + NAD+
pyruvate + NADH + H+
D-lactate + NAD+
pyruvate + NADH + H+
lactate + NAD+
additional information
?
-
(R)-2-hydroxycarboxylate + NAD+

a 2-oxocarboxylate + NADH + H+
-
-
-
r
(R)-2-hydroxycarboxylate + NAD+
a 2-oxocarboxylate + NADH + H+
-
-
-
r
(R)-mandelate + NAD+

phenylglyoxylate + NADH + H+
-
Vmax/Km is 0.4% compared to 4-methyl-2-oxopentanoate
-
-
?
(R)-mandelate + NAD+
phenylglyoxylate + NADH + H+
-
Vmax/Km is 1% compared to 4-methyl-2-oxopentanoate
-
-
?
(R)-mandelate + NAD+
phenylglyoxylate + NADH + H+
-
Vmax/KM is less than 1% compared to 4-methyl-2-oxopentanoate
-
-
?
2-formylbutanethioate + NADH + H+

?
-
i.e. 2-ketomethylthiobutyrate
-
-
?
2-formylbutanethioate + NADH + H+
?
-
i.e. 2-ketomethylthiobutyrate
-
-
?
2-oxo-3-phenylpropanoate + NADH + H+

2-hydroxy-3-phenylpropanoate + NAD+
-
Vmax/KM is 1.9% compared to 4-methyl-2-oxopentanoate
-
-
?
2-oxo-3-phenylpropanoate + NADH + H+
2-hydroxy-3-phenylpropanoate + NAD+
-
Vmax/Km is 2.7% compared to 4-methyl-2-oxopentanoate
-
-
?
2-oxobutanoate + NADH + H+

2-hydroxybutanoate + NAD+
-
Vmax/Km is 0.25% compared to 4-methyl-2-oxopentanoate
-
-
?
2-oxobutanoate + NADH + H+
2-hydroxybutanoate + NAD+
-
Vmax/KM is less than 1% compared to 4-methyl-2-oxopentanoate
-
-
?
2-oxobutyrate + NADH + H+

2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+

?
-
-
-
-
?
2-oxobutyrate + NADH + H+
?
-
-
-
-
?
2-oxobutyrate + NADH + H+

? + NAD+
-
-
-
-
r
2-oxobutyrate + NADH + H+
? + NAD+
-
-
-
-
r
2-oxobutyrate + NADH + H+

D-2-hydroxybutyrate + NAD+
-
55% activity compared to pyruvate
-
-
r
2-oxobutyrate + NADH + H+
D-2-hydroxybutyrate + NAD+
-
55% activity compared to pyruvate
-
-
r
2-oxocaproate + NADH + H+

?
-
-
-
-
?
2-oxocaproate + NADH + H+
?
-
-
-
-
?
2-oxocaproate + NADH + H+

? + NAD+
-
-
-
-
r
2-oxocaproate + NADH + H+
? + NAD+
-
-
-
-
r
2-oxocarboxylate + NADH + H+

(R)-2-hydroxycarboxylate + NAD+
-
-
-
-
r
2-oxocarboxylate + NADH + H+
(R)-2-hydroxycarboxylate + NAD+
-
-
-
-
r
2-oxohexanoate + NADH + H+

2-hydroxyhexanoate + NAD+
-
Vmax/KM is 3% compared to 4-methyl-2-oxopentanoate
-
-
?
2-oxohexanoate + NADH + H+
2-hydroxyhexanoate + NAD+
-
Vmax/Km is 4.1% compared to 4-methyl-2-oxopentanoate
-
-
?
2-oxohexanoate + NADH + H+
2-hydroxyhexanoate + NAD+
-
Vmax/Km is 5.1% compared to 4-methyl-2-oxopentanoate
-
-
?
2-oxohexanoate + NADH + H+
2-hydroxyhexanoate + NAD+
-
i.e. 2-oxovalerate
-
-
r
2-oxohexanoate + NADH + H+
2-hydroxyhexanoate + NAD+
i.e. 2-oxocaproate
-
-
r
2-oxohexanoate + NADH + H+
2-hydroxyhexanoate + NAD+
i.e. 2-oxocaproate
-
-
?
2-oxoisocaproate + NADH + H+

?
-
-
-
-
?
2-oxoisocaproate + NADH + H+
?
-
-
-
-
?
2-oxoisocaproate + NADH + H+

? + NAD+
-
-
-
-
r
2-oxoisocaproate + NADH + H+
? + NAD+
-
-
-
-
r
2-oxoisocaproate + NADH + H+

L-2-hydroxyisocaproate + NAD+
-
29% activity compared to pyruvate
-
-
r
2-oxoisocaproate + NADH + H+
L-2-hydroxyisocaproate + NAD+
-
29% activity compared to pyruvate
-
-
r
2-oxoisovalerate + NADH + H+

?
-
-
-
-
?
2-oxoisovalerate + NADH + H+
?
-
-
-
-
?
2-oxopentanoate + NADH + H+

2-hydroxypentanoate + NAD+
-
Vmax/KM is 10.6% compared to 4-methyl-2-oxopentanoate
-
-
?
2-oxopentanoate + NADH + H+
2-hydroxypentanoate + NAD+
-
Vmax/Km is 5.8% compared to 4-methyl-2-oxopentanoate
-
-
?
2-oxopentanoate + NADH + H+
2-hydroxypentanoate + NAD+
-
Vmax/Km is 7.6% compared to 4-methyl-2-oxopentanoate
-
-
?
2-oxopentanoate + NADH + H+
2-hydroxypentanoate + NAD+
-
i.e. 2-oxocaproate
-
-
r
2-oxopentanoate + NADH + H+
2-hydroxypentanoate + NAD+
i.e. 2-oxovalerate
-
-
r
2-oxopentanoate + NADH + H+
2-hydroxypentanoate + NAD+
i.e. 2-oxovalerate
-
-
?
3-methyl-2-oxobutanoate + NADH + H+

2-hydroxy-3-methylbutanoate + NAD+
-
i.e.2-oxoisovalerate
-
-
?
3-methyl-2-oxobutanoate + NADH + H+
2-hydroxy-3-methylbutanoate + NAD+
-
i.e.2-oxoisovalerate
-
-
?
3-methyl-2-oxobutanoate + NADH + H+

3-methyl-2-hydroxybutanoate + NAD+
-
Vmax/Km is 51% compared to 4-methyl-2-oxopentanoate
-
-
?
3-methyl-2-oxobutanoate + NADH + H+
3-methyl-2-hydroxybutanoate + NAD+
-
Vmax/KM is 56% compared to 4-methyl-2-oxopentanoate
-
-
?
3-methyl-2-oxobutanoate + NADH + H+
3-methyl-2-hydroxybutanoate + NAD+
-
Vmax/Km is 85.7% compared to 4-methyl-2-oxopentanoate
-
-
?
3-methyl-2-oxopentanoate + NADH + H+

2-hydroxy-3-methylpentanoate + NAD+
-
i.e. 2-oxomethylvalerate
-
-
?
3-methyl-2-oxopentanoate + NADH + H+
2-hydroxy-3-methylpentanoate + NAD+
-
i.e. 2-oxomethylvalerate
-
-
?
4-methyl-2-oxopentanoate + NADH + H+

(R)-2-hydroxy-4-methylpentanoate + NAD+
-
i.e. 2-oxoisocaproate
i.e. (R)-2-hydroxyisocaproate
-
r
4-methyl-2-oxopentanoate + NADH + H+
(R)-2-hydroxy-4-methylpentanoate + NAD+
i.e. 2-oxoisocaproate
i.e. (R)-2-hydroxyisocaproate
-
r
4-methyl-2-oxopentanoate + NADH + H+
(R)-2-hydroxy-4-methylpentanoate + NAD+
i.e. 2-oxoisocaproate
i.e. (R)-2-hydroxyisocaproate
-
?
4-methyl-2-oxopentanoate + NADH + H+
(R)-2-hydroxy-4-methylpentanoate + NAD+
-
i.e. 2-oxoisocaproate. The apparent Vmax/Km ratio for the reverse reaction is about 0.5% of that for the forward reaction
i.e. (R)-2-hydroxyisocaproate
-
r
4-methyl-2-oxopentanoate + NADH + H+
(R)-2-hydroxy-4-methylpentanoate + NAD+
-
i.e. 2-oxoisocaproate. The apparent Vmax/Km ratio for the reverse reaction is about 0.5% of that for the forward reaction
i.e. (R)-2-hydroxyisocaproate
-
r
benzoylformate + NADH + H+

?
-
-
-
-
?
benzoylformate + NADH + H+
?
-
-
-
-
?
D-2-hydroxybutyrate + NAD+

2-oxobutyrate + NADH + H+
-
-
-
-
r
D-2-hydroxybutyrate + NAD+
2-oxobutyrate + NADH + H+
-
-
-
-
r
D-malate + NAD+

oxaloacetate + NADH + H+
-
-
-
r
D-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
D-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
D-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
D-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
D-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
D-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
D-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
D-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
D-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
D-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
D-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
oxaloacetate + NADH + H+

D-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
r
phenylglyoxylate + NADH + H+

hydroxy(phenyl)acetic acid + NAD+
-
Vmax/Km is 16.7% compared to 4-methyl-2-oxopentanoate
-
-
?
phenylglyoxylate + NADH + H+
hydroxy(phenyl)acetic acid + NAD+
-
Vmax/Km is 44% compared to 4-methyl-2-oxopentanoate
-
-
?
phenylglyoxylate + NADH + H+
hydroxy(phenyl)acetic acid + NAD+
-
Vmax/KM is 54% compared to 4-methyl-2-oxopentanoate
-
-
?
phenylpyruvate + NADH + H+

? + NAD+
-
-
-
-
r
phenylpyruvate + NADH + H+
? + NAD+
-
-
-
-
r
phenylpyruvate + NADH + H+

phenyl-D-lactate + NAD+
-
-
-
r
phenylpyruvate + NADH + H+
phenyl-D-lactate + NAD+
-
-
-
r
phenylpyruvate + NADH + H+

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

D-lactate + NAD+
-
100% activity
-
-
r
pyruvate + NADH + H+
D-lactate + NAD+
-
100% activity
-
-
r
pyruvate + NADH + H+

lactate + NAD+
-
-
-
-
?
pyruvate + NADH + H+
lactate + NAD+
-
-
-
-
?
additional information

?
-
-
both enzymes (D-mandelate dehydrogenase D-ManDH1 and D-mandelate dehydrogenase D-ManDH2) exhibit no or very little activity toward small 2-ketoacid substrates, such as pyruvate, hydroxypyruvate, and 2-ketobutyrate, and much higher activity toward substrates with larger aliphatic or aromatic side chains. The two enzymes exhibit higher activity (smaller Km and larger Vmax) for 2-ketoacid substrates branched at the C3 or C4 position than for unbranched substrates; i.e., 2-ketoisovalerate and 2-ketoisocaproate are more favorable than 2-ketovalerate and 2-ketocaproate, respectively. Among aromatic substrates, the two enzymes preferr benzoylformate to phenylpyruvate by 9- and 17-fold, respectively
-
-
?
additional information
?
-
-
both enzymes (D-mandelate dehydrogenase D-ManDH1 and D-mandelate dehydrogenase D-ManDH2) exhibit no or very little activity toward small 2-oxoacid substrates, such as pyruvate, hydroxypyruvate, and 2-oxobutyrate, and much higher activity toward substrates with larger aliphatic or aromatic side chains. The two enzymes exhibit higher activity (smaller Km and larger Vmax) for 2-ketoacid substrates branched at the C3 or C4 position than for unbranched substrates; i.e., 2-oxoisovalerate and 2-oxoisocaproate are more favorable than 2-oxovalerate and 2-oxocaproate, respectively. Among aromatic substrates, the two enzymes prefer benzoylformate to phenylpyruvate by 9- and 17-fold, respectively
-
-
?
additional information
?
-
-
the recombinant enzyme exhibits high catalytic activity toward various 2-oxoacid substrates with bulky hydrophobic side chains, particularly C3-branched substrates such as benzoylformate and 2-oxoisovalerate
-
-
?
additional information
?
-
-
no significant activity with L-lactate, L-2-hydroxybutyrate, L-hydroxyisocaproate, phenylpyruvate, 2-oxomethyl-n-valerate, and 2-oxoisovalerate
-
-
?
additional information
?
-
-
no significant activity with L-lactate, L-2-hydroxybutyrate, L-hydroxyisocaproate, phenylpyruvate, 2-oxomethyl-n-valerate, and 2-oxoisovalerate
-
-
?
additional information
?
-
very low specificity regarding size and chemical constitution of the accepted D-2-hydroxycarboxylates
-
-
?
additional information
?
-
-
the enzyme accepts D-2-hydroxyacids but not L-2-hydroxyacids and shows no NADP-dependent 2-ketopantoate reductase activity. No reactions are observed with 10 mM L-2-hydroxyisocaproate and 1 mM NAD+, 10 mM pyruvate and 0.3 mM NADH, 10 mM 2-oxooisocaproate and 0.3 mM NADPH, and 10 mM 2-oxopantoate and 0.3 mM NADH or NADPH
-
-
?
additional information
?
-
-
the enzyme accepts D-2-hydroxyacids but not L-2-hydroxyacids and shows no NADP-dependent 2-ketopantoate reductase activity. No reactions are observed with 10 mM L-2-hydroxyisocaproate and 1 mM NAD+, 10 mM pyruvate and 0.3 mM NADH, 10 mM 2-oxooisocaproate and 0.3 mM NADPH, and 10 mM 2-oxopantoate and 0.3 mM NADH or NADPH
-
-
?
additional information
?
-
the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
-
-
-
additional information
?
-
the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, pro