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Information on EC 1.1.1.345 - D-2-hydroxyacid dehydrogenase (NAD+)
for references in articles please use BRENDA:EC1.1.1.345
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.345 D-2-hydroxyacid dehydrogenase (NAD+)
IUBMB Comments
The enzymes, characterized from bacteria (Peptoclostridium difficile, Enterococcus faecalis and from lactic acid bacteria) prefer substrates with a main chain of 5 carbons (such as 4-methyl-2-oxopentanoate) to those with a shorter chain. It also utilizes phenylpyruvate. The enzyme from the halophilic archaeon Haloferax mediterranei prefers substrates with a main chain of 3-4 carbons (pyruvate and 2-oxobutanoate). cf. EC 1.1.1.272, (D)-2-hydroxyacid dehydrogenase (NADP+).
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
showSynonyms
d-mandelate dehydrogenase, d-2-hydroxyisocaproate dehydrogenase, d-isomer-specific 2-hydroxyacid dehydrogenase, d-hicdh, mandh2, d-mdh, nad-dependent d-2-hydroxyacid dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-2-hydroxyacid dehydrogenase
D-2-hydroxyisocaproate dehydrogenase
D-HicDH
D-isomer specific 2-hydroxyacid dehydrogenase
D-isomer-specific 2-hydroxyacid dehydrogenase
D-lactate dehydrogenase
D-lactate:NAD+ oxidoreductase
D-malate dehydrogenases
D-mandelate dehydrogenase
D-ManDH1
-
the strain contains at least two distinct forms of D-ManDH, the two apparent D-mandelate dehydrogenases are named D-ManDH1 and D-ManDH2 according to the order of their elution
D-ManDH2
D-MDH
D2-HDH
HdhD
Ldb1010
ldh1837
LEUM_1837
NAD-dependent D-2-hydroxyacid dehydrogenase
PanE
D-isomer specific 2-hydroxyacid dehydrogenase
-
D-isomer specific 2-hydroxyacid dehydrogenase
-
-
D-ManDH2
-
the strain contains at least two distinct forms of D-ManDH, the two apparent D-mandelate dehydrogenases are named D-ManDH1 and D-ManDH2 according to the order of their elution
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an (R)-2-hydroxycarboxylate + NAD+ = a 2-oxocarboxylate + NADH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
L-leucine degradation IV (reductive Stickland reaction)
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SYSTEMATIC NAME
IUBMB Comments
(R)-2-hydroxycarboxylate:NAD+ oxidoreductase
The enzymes, characterized from bacteria (Peptoclostridium difficile, Enterococcus faecalis and from lactic acid bacteria) prefer substrates with a main chain of 5 carbons (such as 4-methyl-2-oxopentanoate) to those with a shorter chain. It also utilizes phenylpyruvate. The enzyme from the halophilic archaeon Haloferax mediterranei prefers substrates with a main chain of 3-4 carbons (pyruvate and 2-oxobutanoate). cf. EC 1.1.1.272, (D)-2-hydroxyacid dehydrogenase (NADP+).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-2-hydroxy-4-methylpentanoate + NAD+
4-methyl-2-oxopentanoate + NADH + H+
-
Substrates: i.e. (R)-2-hydroxyisocaproate
Products: i.e. 2-oxoisocaproate
Products: i.e. 2-oxoisocaproate
r
2-hydroxyhexanoate + NAD+
2-oxohexanoate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
2-hydroxyoctanoate + NAD+
2-oxooctanoate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
2-hydroxypentanoate + NAD+
2-oxopentanoate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
2-oxomethylthiobutyrate + NADH + H+
? + NAD+
-
Substrates: -
Products: -
Products: -
r
2-oxooctanoate + NADH + H+
2-hydroxyoctanoate + NAD+
-
Substrates: -
Products: -
Products: -
r
3-(4-hydroxyphenyl)-2-oxopropanoate + NADH + H+
2-hydroxy-3-(4-hydroxyphenyl)propanoate + NAD+
-
Substrates: -
Products: -
Products: -
?
4-methyl-2-oxopentanoate + NADH + H+
4-methyl-2-hydroxypentanoate + NAD+
-
Substrates: highest Vmax/Km value of all substrates tested
Products: -
Products: -
?
DL-2-hydroxyisocaproate + NADH + H+
? + NAD+
-
Substrates: -
Products: -
Products: -
r
L-2-hydroxycaproate + NAD+
2-oxocaproate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(R)-2-hydroxycarboxylate + NAD+
a 2-oxocarboxylate + NADH + H+
Substrates: -
Products: -
Products: -
r
(R)-2-hydroxycarboxylate + NAD+
a 2-oxocarboxylate + NADH + H+
Substrates: -
Products: -
Products: -
r
(R)-mandelate + NAD+
phenylglyoxylate + NADH + H+
-
Substrates: Vmax/Km is 0.4% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
(R)-mandelate + NAD+
phenylglyoxylate + NADH + H+
-
Substrates: Vmax/Km is 1% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
(R)-mandelate + NAD+
phenylglyoxylate + NADH + H+
-
Substrates: Vmax/KM is less than 1% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
2-formylbutanethioate + NADH + H+
?
-
Substrates: i.e. 2-ketomethylthiobutyrate
Products: -
Products: -
?
2-formylbutanethioate + NADH + H+
?
Lactococcus cremoris TIL46
-
Substrates: i.e. 2-ketomethylthiobutyrate
Products: -
Products: -
?
2-oxo-3-phenylpropanoate + NADH + H+
2-hydroxy-3-phenylpropanoate + NAD+
-
Substrates: Vmax/KM is 1.9% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
2-oxo-3-phenylpropanoate + NADH + H+
2-hydroxy-3-phenylpropanoate + NAD+
-
Substrates: Vmax/Km is 2.7% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
2-oxobutanoate + NADH + H+
2-hydroxybutanoate + NAD+
-
Substrates: Vmax/Km is 0.25% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
2-oxobutanoate + NADH + H+
2-hydroxybutanoate + NAD+
-
Substrates: Vmax/KM is less than 1% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
D-2-hydroxybutyrate + NAD+
-
Substrates: 55% activity compared to pyruvate
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
D-2-hydroxybutyrate + NAD+
-
Substrates: 55% activity compared to pyruvate
Products: -
Products: -
r
2-oxocarboxylate + NADH + H+
(R)-2-hydroxycarboxylate + NAD+
-
Substrates: -
Products: -
Products: -
r
2-oxocarboxylate + NADH + H+
(R)-2-hydroxycarboxylate + NAD+
-
Substrates: -
Products: -
Products: -
r
2-oxohexanoate + NADH + H+
2-hydroxyhexanoate + NAD+
-
Substrates: Vmax/KM is 3% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
2-oxohexanoate + NADH + H+
2-hydroxyhexanoate + NAD+
-
Substrates: Vmax/Km is 4.1% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
2-oxohexanoate + NADH + H+
2-hydroxyhexanoate + NAD+
-
Substrates: Vmax/Km is 5.1% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
2-oxohexanoate + NADH + H+
2-hydroxyhexanoate + NAD+
-
Substrates: i.e. 2-oxovalerate
Products: -
Products: -
r
2-oxohexanoate + NADH + H+
2-hydroxyhexanoate + NAD+
Substrates: i.e. 2-oxocaproate
Products: -
Products: -
r
2-oxohexanoate + NADH + H+
2-hydroxyhexanoate + NAD+
Substrates: i.e. 2-oxocaproate
Products: -
Products: -
?
2-oxoisocaproate + NADH + H+
?
Lactiplantibacillus plantarum ATCC 8041
-
Substrates: -
Products: -
Products: -
?
2-oxoisocaproate + NADH + H+
? + NAD+
-
Substrates: -
Products: -
Products: -
r
2-oxoisocaproate + NADH + H+
L-2-hydroxyisocaproate + NAD+
-
Substrates: 29% activity compared to pyruvate
Products: -
Products: -
r
2-oxoisocaproate + NADH + H+
L-2-hydroxyisocaproate + NAD+
-
Substrates: 29% activity compared to pyruvate
Products: -
Products: -
r
2-oxoisovalerate + NADH + H+
?
Lactiplantibacillus plantarum ATCC 8041
-
Substrates: -
Products: -
Products: -
?
2-oxopentanoate + NADH + H+
2-hydroxypentanoate + NAD+
-
Substrates: Vmax/KM is 10.6% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
2-oxopentanoate + NADH + H+
2-hydroxypentanoate + NAD+
-
Substrates: Vmax/Km is 5.8% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
2-oxopentanoate + NADH + H+
2-hydroxypentanoate + NAD+
-
Substrates: Vmax/Km is 7.6% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
2-oxopentanoate + NADH + H+
2-hydroxypentanoate + NAD+
-
Substrates: i.e. 2-oxocaproate
Products: -
Products: -
r
2-oxopentanoate + NADH + H+
2-hydroxypentanoate + NAD+
Substrates: i.e. 2-oxovalerate
Products: -
Products: -
r
2-oxopentanoate + NADH + H+
2-hydroxypentanoate + NAD+
Substrates: i.e. 2-oxovalerate
Products: -
Products: -
?
3-methyl-2-oxobutanoate + NADH + H+
2-hydroxy-3-methylbutanoate + NAD+
-
Substrates: i.e.2-oxoisovalerate
Products: -
Products: -
?
3-methyl-2-oxobutanoate + NADH + H+
2-hydroxy-3-methylbutanoate + NAD+
Lactococcus cremoris TIL46
-
Substrates: i.e.2-oxoisovalerate
Products: -
Products: -
?
3-methyl-2-oxobutanoate + NADH + H+
3-methyl-2-hydroxybutanoate + NAD+
-
Substrates: Vmax/Km is 51% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
3-methyl-2-oxobutanoate + NADH + H+
3-methyl-2-hydroxybutanoate + NAD+
-
Substrates: Vmax/KM is 56% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
3-methyl-2-oxobutanoate + NADH + H+
3-methyl-2-hydroxybutanoate + NAD+
-
Substrates: Vmax/Km is 85.7% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
3-methyl-2-oxopentanoate + NADH + H+
2-hydroxy-3-methylpentanoate + NAD+
-
Substrates: i.e. 2-oxomethylvalerate
Products: -
Products: -
?
3-methyl-2-oxopentanoate + NADH + H+
2-hydroxy-3-methylpentanoate + NAD+
Lactococcus cremoris TIL46
-
Substrates: i.e. 2-oxomethylvalerate
Products: -
Products: -
?
4-methyl-2-oxopentanoate + NADH + H+
(R)-2-hydroxy-4-methylpentanoate + NAD+
-
Substrates: i.e. 2-oxoisocaproate
Products: i.e. (R)-2-hydroxyisocaproate
Products: i.e. (R)-2-hydroxyisocaproate
r
4-methyl-2-oxopentanoate + NADH + H+
(R)-2-hydroxy-4-methylpentanoate + NAD+
Substrates: i.e. 2-oxoisocaproate
Products: i.e. (R)-2-hydroxyisocaproate
Products: i.e. (R)-2-hydroxyisocaproate
r
4-methyl-2-oxopentanoate + NADH + H+
(R)-2-hydroxy-4-methylpentanoate + NAD+
Substrates: i.e. 2-oxoisocaproate
Products: i.e. (R)-2-hydroxyisocaproate
Products: i.e. (R)-2-hydroxyisocaproate
?
4-methyl-2-oxopentanoate + NADH + H+
(R)-2-hydroxy-4-methylpentanoate + NAD+
-
Substrates: i.e. 2-oxoisocaproate. The apparent Vmax/Km ratio for the reverse reaction is about 0.5% of that for the forward reaction
Products: i.e. (R)-2-hydroxyisocaproate
Products: i.e. (R)-2-hydroxyisocaproate
r
4-methyl-2-oxopentanoate + NADH + H+
(R)-2-hydroxy-4-methylpentanoate + NAD+
Lactococcus cremoris TIL46
-
Substrates: i.e. 2-oxoisocaproate. The apparent Vmax/Km ratio for the reverse reaction is about 0.5% of that for the forward reaction
Products: i.e. (R)-2-hydroxyisocaproate
Products: i.e. (R)-2-hydroxyisocaproate
r
D-2-hydroxybutyrate + NAD+
2-oxobutyrate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-2-hydroxybutyrate + NAD+
2-oxobutyrate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADH + H+
D-malate + NAD+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADH + H+
D-malate + NAD+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADH + H+
D-malate + NAD+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADH + H+
D-malate + NAD+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADH + H+
D-malate + NAD+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADH + H+
D-malate + NAD+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADH + H+
D-malate + NAD+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADH + H+
D-malate + NAD+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADH + H+
D-malate + NAD+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADH + H+
D-malate + NAD+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADH + H+
D-malate + NAD+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADH + H+
D-malate + NAD+
Substrates: -
Products: -
Products: -
r
phenylglyoxylate + NADH + H+
hydroxy(phenyl)acetic acid + NAD+
-
Substrates: Vmax/Km is 16.7% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
phenylglyoxylate + NADH + H+
hydroxy(phenyl)acetic acid + NAD+
-
Substrates: Vmax/Km is 44% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
phenylglyoxylate + NADH + H+
hydroxy(phenyl)acetic acid + NAD+
-
Substrates: Vmax/KM is 54% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
phenylpyruvate + NADH + H+
phenyl-D-lactate + NAD+
Substrates: -
Products: -
Products: -
r
phenylpyruvate + NADH + H+
phenyl-D-lactate + NAD+
Substrates: -
Products: -
Products: -
r
phenylpyruvate + NADH + H+
phenyllactate + NAD+
-
Substrates: -
Products: -
Products: -
?
phenylpyruvate + NADH + H+
phenyllactate + NAD+
Substrates: -
Products: -
Products: -
r
phenylpyruvate + NADH + H+
phenyllactate + NAD+
Substrates: -
Products: -
Products: -
?
phenylpyruvate + NADH + H+
phenyllactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
D-lactate + NAD+
-
Substrates: 100% activity
Products: -
Products: -
r
pyruvate + NADH + H+
D-lactate + NAD+
-
Substrates: 100% activity
Products: -
Products: -
r
pyruvate + NADH + H+
lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
lactate + NAD+
Lactiplantibacillus plantarum ATCC 8041
-
Substrates: -
Products: -
Products: -
?
additional information
?
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Substrates: 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
Products: -
Products: -
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additional information
?
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Substrates: 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
Products: -
Products: -
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additional information
?
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-
Substrates: 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
Products: -
Products: -
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additional information
?
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Substrates: no significant activity with L-lactate, L-2-hydroxybutyrate, L-hydroxyisocaproate, phenylpyruvate, 2-oxomethyl-n-valerate, and 2-oxoisovalerate
Products: -
Products: -
?
additional information
?
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Substrates: no significant activity with L-lactate, L-2-hydroxybutyrate, L-hydroxyisocaproate, phenylpyruvate, 2-oxomethyl-n-valerate, and 2-oxoisovalerate
Products: -
Products: -
?
additional information
?
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Substrates: very low specificity regarding size and chemical constitution of the accepted D-2-hydroxycarboxylates
Products: -
Products: -
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additional information
?
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Substrates: 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
Products: -
Products: -
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additional information
?
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Substrates: 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
Products: -
Products: -
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additional information
?
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Substrates: 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
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Products: -
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additional information
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Substrates: 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
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Products: -
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additional information
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Substrates: 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
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Products: -
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additional information
?
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Substrates: 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
Products: -
Products: -
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additional information
?
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Substrates: 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
Products: -
Products: -
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additional information
?
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Substrates: 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
Products: -
Products: -
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additional information
?
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Substrates: 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
Products: -
Products: -
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additional information
?
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Substrates: 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
Products: -
Products: -
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additional information
?
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Substrates: 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
Products: -
Products: -
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additional information
?
-
Substrates: 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
Products: -
Products: -
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additional information
?
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Substrates: 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
Products: -
Products: -
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additional information
?
-
Substrates: 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
Products: -
Products: -
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