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(R)-lactate + NAD(P)+
pyruvate + NAD(P)H + H+
(R)-lactate + NAD+
pyruvate + NADH
(R)-lactate + NAD+
pyruvate + NADH + H+
2-ketocaproate + NADH
2-hydroxycaproate + NAD+
-
-
-
-
?
2-ketoisocaproate + NADH
2-hydroxyisocaproate + NAD+
-
-
-
-
?
2-ketoisovalerate + NADH
2-hydroxyisovalerate + NAD+
-
-
-
-
?
2-ketovalerate + NADH
2-hydroxyvalerate + NAD+
-
-
-
-
?
2-oxo-4-phenyl-butyric acid + NADH + H+
(R)-2-hydroxy-4-phenyl-butyric acid + NAD+
-
-
-
-
?
2-oxo-4-phenylbutyric acid + NADH + H+
(R)-2-hydroxy-4-phenylbutyric acid + NAD+
2-oxo-4-phenylbutyric acid + reduced acceptor
(R)-2-hydroxy-4-phenylbutyric acid + acceptor
-
-
-
-
?
2-oxobutanoate + NADH + H+
(R)-2-hydroxybutanoate + NAD+
2-oxobutanoate + NADH + H+
2-hydroxybutanoate + NAD+
2-oxobutyrate + NADH
2-hydroxybutyrate + NAD+
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
2-oxobutyric acid + NADH + H+
(R)-2-hydroxybutyric acid + NAD+
-
-
-
-
ir
2-oxocaproate + NADH + H+
2-hydroxycaproate + NAD+
2-oxoglutarate + NADH + H+
2-hydroxypentanedioate + NAD+
-
-
-
-
?
2-oxoglutarate + NADPH + H+
(R)-2-hydroxyglutarate + NADP+
2-oxoisocaproate + NADH + H+
2-hydroxyisocaproate + NAD+
2-oxoisovalerate + NADH + H+
2-hydroxyisovalerate + NAD+
-
-
-
r
2-oxovalerate + NADH + H+
2-hydroxyvalerate + NAD+
3,4-dihydroxyphenylpyruvate + NADH + H+
(R)-3,4-dihydroxyphenyllactate + NAD+
3,4-dihydroxyphenylpyruvic acid + NADH + H+
(R)-3,4-dihydroxyphenyllactic acid + NAD+
-
-
-
-
?
3,4-dihydroxyphenylpyruvic acid + NADH + H+
D-3,4-dihydroxyphenyllactic acid + NAD+
3-methyl-2-oxobutanoate + NADH + H+
(R)-2-hydroxy-3-methylbutanoate + NAD+
3-methyl-2-oxobutanoate + NADH + H+
2-hydroxy-3-methylbutanoate + NAD+
4-methyl-2-oxopentanoate + NADH + H+
(R)-2-hydroxy-4-methylpentanoate + NAD+
alpha-ketobutyrate + NADH
2-hydroxybutyrate + NAD+
benzoylformate + NADH + H+
phenylglyoxylate + NAD+
-
-
-
-
?
bromopyruvate + NADH
3-bromo-2-hydroxypropanoate + NAD+
-
-
-
-
?
D-3-phenylpyruvate + NADH + H+
D-3-phenyllactate + NAD+
D-lactate + cytochrome c2ox
pyruvate + cytochrome c2red
-
-
-
-
?
D-lactate + NAD+
pyruvate + NADH
D-lactate + NAD+
pyruvate + NADH + H+
D-lactate + NAD+ + H+
pyruvate + NADH
-
-
-
?
D-lactate + nicotinamide cytosine dinucleotide
pyruvate + reduced nicotinamide cytosine dinucleotide
-
-
-
?
DL-2-hydroxybutyrate + NAD+
2-oxobutyrate + NADH
DL-2-hydroxybutyrate + NAD+
? + NADH
-
about 44% of activity against D-lactate
-
-
?
glyoxylate + NADH
hydroxyacetic acid + NAD+
-
-
-
-
?
glyoxylate + NADH + H+
glycolate + NAD+
-
best substrate of isoform LDHL1
-
-
?
glyoxylate + NADH + H+
hydroxyacetate + NAD+
glyoxylate + NADH + H+
hydroxyacetic acid + NAD+
-
-
-
-
?
hydroxypyruvate + NADH
glycerate + NAD+
-
-
-
-
?
hydroxypyruvate + NADH + H+
glycerate + NAD+
L-lactate + NAD+
pyruvate + NADH + H+
methylpyruvate + NADH
? + NAD+
oxaloacetate + NADH
malate + NAD+
oxaloacetate + NADH + H+
D-malate + NAD+
oxaloacetate + NADH + H+
malate + NAD+
oxaloacetic acid + NADH + H+
(R)-malate + NAD+
-
-
-
-
ir
phenylpyruvate + NADH
phenyllactate + NAD+
-
-
-
-
?
phenylpyruvate + NADH + H+
(R)-3-phenyllactate + NAD+
phenylpyruvate + NADH + H+
2-hydroxy-3-phenylpropanoate + NAD+
-
-
-
-
?
phenylpyruvate + NADH + H+
D-phenyllactate + NAD+
pyruvate + NAD(P)H + H+
(R)-lactate + NAD(P)+
pyruvate + NADH
(R)-lactate + NAD+
pyruvate + NADH + H+
(R)-lactate + NAD+
pyruvate + NADH + H+
D-lactate + NAD+
-
-
-
-
?
pyruvate + NADPH + H+
(R)-lactate + NADP+
-
-
-
-
r
additional information
?
-
(R)-lactate + NAD(P)+
pyruvate + NAD(P)H + H+
the enzyme is confirmed to be a typical D-lactate dehydrogenase based on the activity detected with substrate pyruvate and coenzyme NAD(P)H
-
-
r
(R)-lactate + NAD(P)+
pyruvate + NAD(P)H + H+
the enzyme is confirmed to be a typical D-lactate dehydrogenase based on the activity detected with substrate pyruvate and coenzyme NAD(P)H
-
-
r
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
Allomyces sp.
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
Lactobacillus jugurt-helveticus
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
(R)-lactate + NAD+
pyruvate + NADH + H+
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH + H+
-
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH + H+
-
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH + H+
-
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH + H+
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH + H+
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH + H+
-
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH + H+
-
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH + H+
-
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH + H+
-
no activity with L-lactate
-
-
r
(R)-lactate + NAD+
pyruvate + NADH + H+
-
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH + H+
-
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH + H+
-
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH + H+
-
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH + H+
-
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH + H+
-
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH + H+
-
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH + H+
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH + H+
development of an assay system of D-lactate with good precision, accuracy, and sensitivity for the determination of D-lactate concentrations in rat serum. D-Lactate dehydrogenase (D-LDH) is utilized to catalyze D-lactate and NAD+ to pyruvate and NADH, analysis of D-lactate by HPLC, respectively. Structure of the enzymatic assay system with a UV-LED fluorescent spectrometer, and method optimization and validation, overview
-
-
r
(R)-lactate + NAD+
pyruvate + NADH + H+
-
-
-
r
(R)-lactate + NAD+
pyruvate + NADH + H+
development of an assay system of D-lactate with good precision, accuracy, and sensitivity for the determination of D-lactate concentrations in rat serum. D-Lactate dehydrogenase (D-LDH) is utilized to catalyze D-lactate and NAD+ to pyruvate and NADH, analysis of D-lactate by HPLC, respectively. Structure of the enzymatic assay system with a UV-LED fluorescent spectrometer, and method optimization and validation, overview
-
-
r
(R)-lactate + NAD+
pyruvate + NADH + H+
-
-
-
?
2-oxo-4-phenylbutyric acid + NADH + H+
(R)-2-hydroxy-4-phenylbutyric acid + NAD+
-
-
-
-
?
2-oxo-4-phenylbutyric acid + NADH + H+
(R)-2-hydroxy-4-phenylbutyric acid + NAD+
-
-
-
-
?
2-oxobutanoate + NADH + H+
(R)-2-hydroxybutanoate + NAD+
-
12.6% of the activity with pyruvate
-
-
?
2-oxobutanoate + NADH + H+
(R)-2-hydroxybutanoate + NAD+
-
12.6% of the activity with pyruvate
-
-
?
2-oxobutanoate + NADH + H+
2-hydroxybutanoate + NAD+
-
-
-
-
?
2-oxobutanoate + NADH + H+
2-hydroxybutanoate + NAD+
-
-
-
-
?
2-oxobutanoate + NADH + H+
2-hydroxybutanoate + NAD+
-
-
-
?
2-oxobutanoate + NADH + H+
2-hydroxybutanoate + NAD+
-
-
-
?
2-oxobutanoate + NADH + H+
2-hydroxybutanoate + NAD+
-
-
-
-
?
2-oxobutyrate + NADH
2-hydroxybutyrate + NAD+
-
11% of activity with pyruvate
-
-
r
2-oxobutyrate + NADH
2-hydroxybutyrate + NAD+
-
11% of activity with pyruvate
-
-
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+
-
-
-
-
?
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
-
?
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
-
?
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxocaproate + NADH + H+
2-hydroxycaproate + NAD+
-
-
-
r
2-oxocaproate + NADH + H+
2-hydroxycaproate + NAD+
-
-
-
r
2-oxocaproate + NADH + H+
2-hydroxycaproate + NAD+
-
-
-
r
2-oxoglutarate + NADPH + H+
(R)-2-hydroxyglutarate + NADP+
-
-
-
-
?
2-oxoglutarate + NADPH + H+
(R)-2-hydroxyglutarate + NADP+
-
-
-
-
?
2-oxoisocaproate + NADH + H+
2-hydroxyisocaproate + NAD+
-
-
-
r
2-oxoisocaproate + NADH + H+
2-hydroxyisocaproate + NAD+
-
-
-
r
2-oxovalerate + NADH + H+
2-hydroxyvalerate + NAD+
-
-
-
r
2-oxovalerate + NADH + H+
2-hydroxyvalerate + NAD+
-
-
-
-
?
2-oxovalerate + NADH + H+
2-hydroxyvalerate + NAD+
-
-
-
-
?
2-oxovalerate + NADH + H+
2-hydroxyvalerate + NAD+
-
-
-
r
2-oxovalerate + NADH + H+
2-hydroxyvalerate + NAD+
-
-
-
-
?
3,4-dihydroxyphenylpyruvate + NADH + H+
(R)-3,4-dihydroxyphenyllactate + NAD+
-
43.1% of the activity with pyruvate
-
-
?
3,4-dihydroxyphenylpyruvate + NADH + H+
(R)-3,4-dihydroxyphenyllactate + NAD+
-
43.1% of the activity with pyruvate
-
-
?
3,4-dihydroxyphenylpyruvic acid + NADH + H+
D-3,4-dihydroxyphenyllactic acid + NAD+
-
-
-
-
?
3,4-dihydroxyphenylpyruvic acid + NADH + H+
D-3,4-dihydroxyphenyllactic acid + NAD+
-
-
-
-
?
3-methyl-2-oxobutanoate + NADH + H+
(R)-2-hydroxy-3-methylbutanoate + NAD+
-
19.4% of the activity with pyruvate
-
-
?
3-methyl-2-oxobutanoate + NADH + H+
(R)-2-hydroxy-3-methylbutanoate + NAD+
-
-
-
-
?
3-methyl-2-oxobutanoate + NADH + H+
(R)-2-hydroxy-3-methylbutanoate + NAD+
-
-
-
-
?
3-methyl-2-oxobutanoate + NADH + H+
2-hydroxy-3-methylbutanoate + NAD+
-
-
-
?
3-methyl-2-oxobutanoate + NADH + H+
2-hydroxy-3-methylbutanoate + NAD+
-
-
-
?
4-methyl-2-oxopentanoate + NADH + H+
(R)-2-hydroxy-4-methylpentanoate + NAD+
-
-
-
-
?
4-methyl-2-oxopentanoate + NADH + H+
(R)-2-hydroxy-4-methylpentanoate + NAD+
-
-
-
-
?
alpha-ketobutyrate + NADH
2-hydroxybutyrate + NAD+
-
-
-
-
?
alpha-ketobutyrate + NADH
2-hydroxybutyrate + NAD+
-
-
-
-
?
D-3-phenylpyruvate + NADH + H+
D-3-phenyllactate + NAD+
-
-
i.e. 2-hydroxy-3-phenylpropanoic acid
-
r
D-3-phenylpyruvate + NADH + H+
D-3-phenyllactate + NAD+
-
i.e. 2-hydroxy-3-phenylpropanoic acid
-
r
D-lactate + NAD+
pyruvate + NADH
-
-
-
r
D-lactate + NAD+
pyruvate + NADH
during oxidation of NADH to NAD+, NADH transfers a hydride ion to pyruvate, in the reverse reaction NAD+ receives a hydride ion from lactate, D-lactate binding structure, overview
pyruvate binding structure, overview
-
r
D-lactate + NAD+
pyruvate + NADH
-
-
-
-
?
D-lactate + NAD+
pyruvate + NADH + H+
-
-
-
?
D-lactate + NAD+
pyruvate + NADH + H+
-
-
-
?
DL-2-hydroxybutyrate + NAD+
2-oxobutyrate + NADH
-
3% of activity with (R)-lactate
-
-
r
DL-2-hydroxybutyrate + NAD+
2-oxobutyrate + NADH
-
3% of activity with (R)-lactate
-
-
r
glyoxylate + NADH + H+
hydroxyacetate + NAD+
-
-
-
r
glyoxylate + NADH + H+
hydroxyacetate + NAD+
-
-
-
r
glyoxylate + NADH + H+
hydroxyacetate + NAD+
-
-
-
r
glyoxylate + NADH + H+
hydroxyacetate + NAD+
-
-
-
r
hydroxypyruvate + NADH + H+
glycerate + NAD+
-
-
-
r
hydroxypyruvate + NADH + H+
glycerate + NAD+
-
-
-
r
hydroxypyruvate + NADH + H+
glycerate + NAD+
-
-
-
r
hydroxypyruvate + NADH + H+
glycerate + NAD+
-
-
-
-
?
hydroxypyruvate + NADH + H+
glycerate + NAD+
-
-
-
r
L-lactate + NAD+
pyruvate + NADH + H+
very poor substrate
-
-
?
L-lactate + NAD+
pyruvate + NADH + H+
very poor substrate
-
-
?
methylpyruvate + NADH
? + NAD+
-
84% of activity with pyruvate
-
-
r
methylpyruvate + NADH
? + NAD+
-
84% of activity with pyruvate
-
-
r
oxaloacetate + NADH
malate + NAD+
-
-
-
-
?
oxaloacetate + NADH
malate + NAD+
-
-
-
-
?
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
-
?
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
-
?
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
malate + NAD+
-
-
-
r
phenylpyruvate + NADH + H+
(R)-3-phenyllactate + NAD+
-
70.4% of the activity with pyruvate
-
-
?
phenylpyruvate + NADH + H+
(R)-3-phenyllactate + NAD+
-
70.4% of the activity with pyruvate
-
-
?
phenylpyruvate + NADH + H+
(R)-3-phenyllactate + NAD+
-
-
-
-
?
phenylpyruvate + NADH + H+
(R)-3-phenyllactate + NAD+
-
-
-
?
phenylpyruvate + NADH + H+
(R)-3-phenyllactate + NAD+
-
-
-
-
?
phenylpyruvate + NADH + H+
(R)-3-phenyllactate + NAD+
-
-
-
?
phenylpyruvate + NADH + H+
(R)-3-phenyllactate + NAD+
-
-
-
-
?
phenylpyruvate + NADH + H+
(R)-3-phenyllactate + NAD+
-
-
-
-
?
phenylpyruvate + NADH + H+
D-phenyllactate + NAD+
-
-
-
?
phenylpyruvate + NADH + H+
D-phenyllactate + NAD+
-
-
-
?
phenylpyruvate + NADH + H+
D-phenyllactate + NAD+
-
-
-
r
phenylpyruvate + NADH + H+
D-phenyllactate + NAD+
-
-
-
-
?
phenylpyruvate + NADH + H+
D-phenyllactate + NAD+
-
-
-
-
ir
phenylpyruvate + NADH + H+
D-phenyllactate + NAD+
-
-
-
r
phenylpyruvate + NADH + H+
D-phenyllactate + NAD+
-
-
-
r
phenylpyruvate + NADH + H+
D-phenyllactate + NAD+
-
-
-
r
phenylpyruvate + NADH + H+
D-phenyllactate + NAD+
-
-
-
r
pyruvate + NAD(P)H + H+
(R)-lactate + NAD(P)+
-
-
-
r
pyruvate + NAD(P)H + H+
(R)-lactate + NAD(P)+
-
-
-
r
pyruvate + NADH
(R)-lactate + NAD+
-
-
-
-
r
pyruvate + NADH
(R)-lactate + NAD+
-
-
-
-
r
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
-
r
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
r
pyruvate + NADH + H+
(R)-lactate + NAD+
-
a highly stereospecific reaction leading to 98-99%optical purity of the product
-
-
r
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
r
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
r
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
-
?
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
-
r
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
r
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
r
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
-
r
pyruvate + NADH + H+
(R)-lactate + NAD+
-
a highly stereospecific reaction leading to 98-99%optical purity of the product
-
-
r
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
-
r
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
r
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
-
r
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
r
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
-
r
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
-
r
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
-
?
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
-
?
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
r
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
r
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
-
?
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
-
?
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
-
r
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
-
r
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
-
?
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
-
r
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
-
?
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
-
r
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
?
pyruvate + NADH + H+
(R)-lactate + NAD+
preferred subtrate
-
-
?
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
r
pyruvate + NADH + H+
(R)-lactate + NAD+
-
-
-
r
additional information
?
-
each subunit of the homodimer in a closed conformation binds NADH to the coenzyme-binding domain and a lactate or pyruvate molecule at the interdomain active-site cleft, structure, overview
-
-
?
additional information
?
-
-
each subunit of the homodimer in a closed conformation binds NADH to the coenzyme-binding domain and a lactate or pyruvate molecule at the interdomain active-site cleft, structure, overview
-
-
?
additional information
?
-
-
effect of a single-gene knockout on the metabolic regulation in Escherichia coli for D-lactate production under microaerobic condition
-
-
?
additional information
?
-
the enzyme ECLDH exhibits high substrate specificity toward pyruvate. No or poor activity with 2-oxovalerate, 2-oxoisovalerate, 2-oxocaproate, 2-oxoisocaproate, phenylpyruvate, and hydroxyphenylpyruvate
-
-
?
additional information
?
-
-
the enzyme ECLDH exhibits high substrate specificity toward pyruvate. No or poor activity with 2-oxovalerate, 2-oxoisovalerate, 2-oxocaproate, 2-oxoisocaproate, phenylpyruvate, and hydroxyphenylpyruvate
-
-
?
additional information
?
-
the enzyme FNLDH exhibits a broad substrate specificity toward hydrophobic 2-oxoacids such as 2-oxobutyrate and 2-oxovalerate. Poor activity with hydroxyphenylpyruvate and 2-oxoisovalerate
-
-
?
additional information
?
-
the enzyme FNLDH exhibits a broad substrate specificity toward hydrophobic 2-oxoacids such as 2-oxobutyrate and 2-oxovalerate. Poor activity with hydroxyphenylpyruvate and 2-oxoisovalerate
-
-
?
additional information
?
-
-
D-LDH is an NADH-dependent reductase, substrate reduction is accompanied by the oxidation of NADH to NAD?
-
-
?
additional information
?
-
-
strain NCIMB 8826 produces optically pure D-lactic acid
-
-
?
additional information
?
-
-
strain NCIMB 8826 produces optically pure D-lactic acid
-
-
?
additional information
?
-
Lactiplantibacillus plantarum NCIMB 8826 delta ldhL1 -xpk1::tkt-delta xpk
-
strain NCIMB 8826 produces optically pure D-lactic acid
-
-
?
additional information
?
-
-
residues Tyr52 and Phe299 are mainly responsible for hindering larger substrates because of their short distance from the side chain of 2-oxocarboxylic acids and their steric orientation in the wild-type enzyme. Substrate specificity and enantioselectivity of D-nLDH and DnLDH mutants, overview
-
-
?
additional information
?
-
-
residues Tyr52 and Phe299 are mainly responsible for hindering larger substrates because of their short distance from the side chain of 2-oxocarboxylic acids and their steric orientation in the wild-type enzyme. Substrate specificity and enantioselectivity of D-nLDH and DnLDH mutants, overview
-
-
?
additional information
?
-
-
substrate specificities of the D-LDH isozymes, overview. (R)-2-Hydroxybutyric acid, D-(+)-malic acid, and D-(+)-3-phenyllactic acid are no substrates
-
-
?
additional information
?
-
-
no substrate: phenylpyruvate
-
-
-
additional information
?
-
-
no substrate: phenylpyruvate
-
-
-
additional information
?
-
-
enzyme displays more than 99% enantioselectivity. No substrates: 3-methyl-2-oxopentanoate, 4-methyl-2-oxopentanoate, indole-3-pyruvate
-
-
-
additional information
?
-
-
enzyme displays more than 99% enantioselectivity. No substrates: 3-methyl-2-oxopentanoate, 4-methyl-2-oxopentanoate, indole-3-pyruvate
-
-
-
additional information
?
-
-
no or poor substrates: 2-oxobutanoate, phenylpyruvate, 4-hydroxyphenylpyruvate
-
-
-
additional information
?
-
-
no or poor substrates: 2-oxobutanoate, phenylpyruvate, 4-hydroxyphenylpyruvate
-
-
-
additional information
?
-
enzymatic production of D-3-phenyllactic acid by recombinant Pediococcus pentosaceus D-lactate dehydrogenase with NADH regeneration by recombinant Ogataea parapolymorpha formate dehydrogenase, EC 1.2.1.2
-
-
?
additional information
?
-
-
enzymatic production of D-3-phenyllactic acid by recombinant Pediococcus pentosaceus D-lactate dehydrogenase with NADH regeneration by recombinant Ogataea parapolymorpha formate dehydrogenase, EC 1.2.1.2
-
-
?
additional information
?
-
the enzyme PALDH exhibits high substrate specificity toward pyruvate. Poor activity with hydroxyphenylpyruvate and 2-oxoisovalerate
-
-
?
additional information
?
-
-
the enzyme PALDH exhibits high substrate specificity toward pyruvate. Poor activity with hydroxyphenylpyruvate and 2-oxoisovalerate
-
-
?
additional information
?
-
-
interactin of enzyme with F-actin in vivo, playing an important role in the yeast cell morphology
-
-
?
additional information
?
-
the bifunctional enzyme from Sporolactobacillus inulinus has both the D-LDH and NAD(P)+/NAD(P)H-utilizing glutamate dehydrogenase (GDH, EC 1.4.1.3) activities, the latter with reversible deamination. Identification of key residues from the crystal structure analysis and site-directed mutagenesis, enzyme reidues Arg234 and Gly79 residues play a significant role in both D-LDH and GDH activities. Residues His295 and Phe298 in DLDH744 are identified to be key residues for lactate dehydrogenase (LDH) activity only, whereas Tyr101 is a unique residue that is critical for GDH activity. DLDH744 is a strict D-2-hydroxyacid dehydrogenase, no formation of L-isomers
-
-
?
additional information
?
-
-
the bifunctional enzyme from Sporolactobacillus inulinus has both the D-LDH and NAD(P)+/NAD(P)H-utilizing glutamate dehydrogenase (GDH, EC 1.4.1.3) activities, the latter with reversible deamination. Identification of key residues from the crystal structure analysis and site-directed mutagenesis, enzyme reidues Arg234 and Gly79 residues play a significant role in both D-LDH and GDH activities. Residues His295 and Phe298 in DLDH744 are identified to be key residues for lactate dehydrogenase (LDH) activity only, whereas Tyr101 is a unique residue that is critical for GDH activity. DLDH744 is a strict D-2-hydroxyacid dehydrogenase, no formation of L-isomers
-
-
?
additional information
?
-
the bifunctional enzyme from Sporolactobacillus inulinus has both the D-LDH and NAD(P)+/NAD(P)H-utilizing glutamate dehydrogenase (GDH, EC 1.4.1.3) activities, the latter with reversible deamination. Identification of key residues from the crystal structure analysis and site-directed mutagenesis, enzyme reidues Arg234 and Gly79 residues play a significant role in both D-LDH and GDH activities. Residues His295 and Phe298 in DLDH744 are identified to be key residues for lactate dehydrogenase (LDH) activity only, whereas Tyr101 is a unique residue that is critical for GDH activity. DLDH744 is a strict D-2-hydroxyacid dehydrogenase, no formation of L-isomers
-
-
?
additional information
?
-
-
specific for NAD+/NADH
-
-
?
additional information
?
-
-
specific for NAD+/NADH
-
-
?
additional information
?
-
no activity towards L-lactate
-
-
?
additional information
?
-
the enzyme shows very low in vivo activity
-
-
?
additional information
?
-
-
the enzyme shows very low in vivo activity
-
-
?
additional information
?
-
the enzyme shows very low in vivo activity
-
-
?
additional information
?
-
-
the enzyme shows very low in vivo activity
-
-
?
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0.38 - 20.8
2-Ketobutyrate
1.18 - 189
2-ketocaproate
15.5
2-Ketoglutarate
-
30°C, pH 5.5, wild-type enzyme
0.124 - 31
2-ketoisocaproate
5.5 - 18.6
2-ketoisovalerate
3.8 - 12
2-oxoisocaproate
3.5
2-oxoisovalerate
pH 7.0, 30°C, recombinant enzyme
0.09 - 0.1
3,4-dihydroxyphenylpyruvic acid
7.7 - 38
3-methyl-2-oxobutanoate
4.4 - 10
alpha-Ketobutyrate
0.8
D-lactate
-
pH 8.0, 30°C
19
DL-2-hydroxybutyrate
-
pH 8.0, 25°C
0.28 - 53
Hydroxypyruvate
0.65 - 1.39
nicotinamide cytosine dinucleotide
additional information
additional information
-
0.59
(R)-lactate
-
-
8.5
(R)-lactate
-
pH 8.0, 25°C
9.54
(R)-lactate
pH 6.5, 30°C, recombinant enzyme
87.9
(R)-lactate
-
pH 8, , 30°C
260
(R)-lactate
-
pH 11.0, 20°C, recombinant enzyme
0.38
2-Ketobutyrate
-
30°C, pH 5.5, mutant enzyme Y52L
3.5
2-Ketobutyrate
-
30°C, pH 5.5, mutant enzyme Y52V
8.1
2-Ketobutyrate
-
30°C, pH 5.5, wild-type enzyme
20.8
2-Ketobutyrate
-
30°C, pH 5.5, mutant enzyme Y52A
1.18
2-ketocaproate
-
30°C, pH 5.5, mutant enzyme Y52R
13.3
2-ketocaproate
-
30°C, pH 5.5, wild-type enzyme
14.1
2-ketocaproate
-
30°C, pH 5.5, mutant enzyme Y52R/F299G
51
2-ketocaproate
-
30°C, pH 5.5, mutant enzyme Y52V
102
2-ketocaproate
-
30°C, pH 5.5, mutant enzyme Y52A
189
2-ketocaproate
-
30°C, pH 5.5, mutant enzyme Y52L
0.124
2-ketoisocaproate
-
30°C, pH 5.5, mutant enzyme Y52L
0.7
2-ketoisocaproate
-
30°C, pH 5.5, mutant enzyme Y52V
12.1
2-ketoisocaproate
-
30°C, pH 5.5, mutant enzyme Y52A
31
2-ketoisocaproate
-
30°C, pH 5.5, wild-type enzyme
5.5
2-ketoisovalerate
-
30°C, pH 5.5, wild-type enzyme
18.6
2-ketoisovalerate
-
30°C, pH 5.5, mutant enzyme Y52L
0.15
2-ketovalerate
-
30°C, pH 5.5, mutant enzyme Y52L
0.8
2-ketovalerate
-
30°C, pH 5.5, mutant enzyme Y52V
11.7
2-ketovalerate
-
30°C, pH 5.5, mutant enzyme Y52A
17
2-ketovalerate
-
30°C, pH 5.5, wild-type enzyme
2.7
2-oxobutanoate
mutant Y51F, pH 5.5, 30°C
7.5
2-oxobutanoate
mutant Y51M, pH 5.5, 30°C
11
2-oxobutanoate
wild-type, pH 5.5, 30°C
12
2-oxobutanoate
mutant Y51L, pH 5.5, 30°C
234
2-oxobutanoate
-
pH 8, 30°C
0.31
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
0.64
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
2.3
2-oxobutyrate
-
pH 8.0, 25°C
8.1
2-oxobutyrate
-
30°C, pH 5.5, wild-type enzyme
30
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
58
2-oxobutyrate
-
30°C, pH 5.5, mutant enzyme N97D
2.6
2-oxocaproate
pH 7.0, 30°C, recombinant enzyme
5.8
2-oxocaproate
pH 7.0, 30°C, recombinant enzyme
3.8
2-oxoisocaproate
pH 7.0, 30°C, recombinant enzyme
12
2-oxoisocaproate
pH 7.0, 30°C, recombinant enzyme
0.68
2-oxovalerate
pH 7.0, 30°C, recombinant enzyme
4
2-oxovalerate
pH 7.0, 30°C, recombinant enzyme
0.09
3,4-dihydroxyphenylpyruvic acid
-
cosubstrate NADH, pH 8.0, 25°C
0.1
3,4-dihydroxyphenylpyruvic acid
-
cosubstrate NADPH, pH 8.0, 25°C
7.7
3-methyl-2-oxobutanoate
mutant Y51F, pH 5.5, 30°C
8.6
3-methyl-2-oxobutanoate
mutant Y51M, pH 5.5, 30°C
12
3-methyl-2-oxobutanoate
mutant Y51L, pH 5.5, 30°C
38
3-methyl-2-oxobutanoate
wild-type, pH 5.5, 30°C
4.4
alpha-Ketobutyrate
-
-
10
alpha-Ketobutyrate
-
-
5.4
glyoxylate
-
30°C, pH 5.5, wild-type enzyme
6.8
glyoxylate
pH 7.0, 30°C, recombinant enzyme
18
glyoxylate
pH 7.0, 30°C, recombinant enzyme
20
glyoxylate
pH 7.0, 30°C, recombinant enzyme
72
glyoxylate
-
30°C, pH 5.5, mutant enzyme N97D
0.28
Hydroxypyruvate
-
30°C, pH 5.5, wild-type enzyme
2.1
Hydroxypyruvate
-
30°C, pH 5.5, mutant enzyme Y52R/F299G
3
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
3
Hydroxypyruvate
-
30°C, pH 5.5, mutant enzyme Y52L
8.7
Hydroxypyruvate
-
30°C, pH 5.5, mutant enzyme Y52V
12
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
17
Hydroxypyruvate
-
30°C, pH 5.5, mutant enzyme Y52A
18
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
18.6
Hydroxypyruvate
-
30°C, pH 5.5, mutant enzyme F299S
20.2
Hydroxypyruvate
-
30°C, pH 5.5, mutant enzyme Y52R
29
Hydroxypyruvate
-
30°C, pH 5.5, mutant enzyme N97D
53
Hydroxypyruvate
-
30°C, pH 5.5, mutant enzyme F299G
0.00044
NAD+
-
-
0.28
NAD+
wild-type, pH not specified in the publication, temperature not specified in the publication
0.41
NAD+
-
isozyme D-LDH3, pH 8.0, 25°C
0.87
NAD+
mutant V152R/I177K, pH not specified in the publication, temperature not specified in the publication
0.92
NAD+
mutant V152R, pH not specified in the publication, temperature not specified in the publication
1.05
NAD+
mutant V152R/I177K/N213I, pH not specified in the publication, temperature not specified in the publication
1.6
NAD+
mutant V152R/N213E, pH not specified in the publication, temperature not specified in the publication
1.96
NAD+
-
pH 11.0, 20°C, recombinant enzyme
2.58
NAD+
-
isozyme D-LDH2, pH 8.0, 25°C
2.75
NAD+
-
isozyme D-LDH1, pH 8.0, 25°C
0.00021
NADH
-
-
0.019
NADH
pH 7.0, 30°C, recombinant enzyme
0.022
NADH
pH 7.0, 30°C, recombinant enzyme
0.028
NADH
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
0.031
NADH
pH 8.0, 30°C, recombinant enzyme, with Mg2+
0.035
NADH
pH 8.0, 30°C, recombinant enzyme, with or without fructose 1,6-bisphosphate and Mg2+
0.036
NADH
pH 8.0, 30°C, recombinant enzyme
0.04
NADH
-
isozyme D-LDH3, pH 8.0, 25°C
0.055
NADH
pH 7.0, 30°C, recombinant enzyme
0.088
NADH
pH 8.0, 30°C, recombinant enzyme
0.09
NADH
pH 8.0, 30°C, recombinant enzyme, with Mg2+
0.092
NADH
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
0.5
NADH
-
pH 8.0, 30°C, recombinant enzyme
0.7
NADH
-
isozyme D-LDH1, pH 8.0, 25°C
2.83
NADH
-
isozyme D-LDH2, pH 8.0, 25°C
0.65
nicotinamide cytosine dinucleotide
mutant V152R, pH not specified in the publication, temperature not specified in the publication
0.66
nicotinamide cytosine dinucleotide
mutant V152R/I177K/N213I, pH not specified in the publication, temperature not specified in the publication
1.38
nicotinamide cytosine dinucleotide
mutant V152R/I177K, pH not specified in the publication, temperature not specified in the publication
1.38
nicotinamide cytosine dinucleotide
mutant V152R/N213E, pH not specified in the publication, temperature not specified in the publication
1.39
nicotinamide cytosine dinucleotide
wild-type, pH not specified in the publication, temperature not specified in the publication
1.7
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
2.2
oxaloacetate
-
30°C, pH 5.5, wild-type enzyme
2.5
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
3.8
oxaloacetate
-
30°C, pH 5.5, mutant enzyme Y52R
7.5 - 9
oxaloacetate
-
recombinant and wild-type enzyme
43.1
oxaloacetate
-
30°C, pH 5.5, mutant enzyme F299S
54
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
78.8
oxaloacetate
-
pH 8, 30°C
0.03
phenylpyruvate
-
30°C, pH 5.5, mutant enzyme Y52A
0.06
phenylpyruvate
-
30°C, pH 5.5, mutant enzyme Y52L
0.14
phenylpyruvate
-
30°C, pH 5.5, mutant enzyme Y52V
0.16
phenylpyruvate
mutant Y51A, pH 5.5, 30°C
0.17
phenylpyruvate
mutant Y51L, pH 5.5, 30°C
0.22
phenylpyruvate
mutant Y51F, pH 5.5, 30°C
0.22
phenylpyruvate
mutant Y51M, pH 5.5, 30°C
0.27
phenylpyruvate
-
pH 7.4, 37°C, recombinant His-taged mutant Y52L
0.32
phenylpyruvate
-
pH 7.4, 37°C, recombinant His-taged mutant F299Y
0.4
phenylpyruvate
mutant Y51S, pH 5.5, 30°C
0.49
phenylpyruvate
-
pH 5.5, 45°C
0.8
phenylpyruvate
-
30°C, pH 5.5, wild-type enzyme
1.4
phenylpyruvate
-
pH 7.4, 37°C, recombinant His-taged mutant Y52L/F299Y
1.68
phenylpyruvate
-
pH 8, 50°C
1.73
phenylpyruvate
-
pH 5.5, 45°C
2.1
phenylpyruvate
-
30°C, pH 5.5, mutant enzyme Y52R
2.6
phenylpyruvate
wild-type, pH 5.5, 30°C
2.83
phenylpyruvate
pH 7, 30°C
2.9
phenylpyruvate
-
recombinant enzyme, pH 5.5, 30°C
3.32
phenylpyruvate
recombinant enzyme, pH and temperature not specified in the publication
6.9
phenylpyruvate
-
30°C, pH 5.5, mutant enzyme Y52R/F299G
7.1
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
7.2
phenylpyruvate
-
30°C, pH 5.5, mutant enzyme F299S
8.7
phenylpyruvate
-
30°C, pH 5.5, mutant enzyme Y52T/D299S
11
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
11.4
phenylpyruvate
-
pH 7.4, 37°C, recombinant His-taged wild-type enzyme
22
phenylpyruvate
-
30°C, pH 5.5, mutant enzyme F299G
0.07
pyruvate
-
-
0.09
pyruvate
-
recombinant enzyme, pH 5.5, 30°C
0.1
pyruvate
pH 7.0, 30°C, recombinant enzyme
0.12
pyruvate
-
30°C, pH 5.5, wild-type enzyme
0.3
pyruvate
pH 6.5, 30°C, recombinant enzyme
0.34
pyruvate
pH 7.0, 30°C, recombinant enzyme
0.36
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
0.47
pyruvate
-
isoform LDHD1, pH 6, 35°C
0.58
pyruvate
-
pH 8.0, 30°C, recombinant enzyme
0.67
pyruvate
-
pH 8.0, 25°C
0.85
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
1.2
pyruvate
pH 8.0, 30°C, recombinant enzyme
1.2
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
1.4
pyruvate
-
isoform LDHD2, pH 7.5, 35°C
1.5 - 1.6
pyruvate
-
recombinant and wild-type enzyme
1.7
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
1.8
pyruvate
-
30°C, pH 5.5, mutant enzyme Y52L
2.5
pyruvate
pH 8.0, 30°C, recombinant enzyme
2.6
pyruvate
pH 7.0, 30°C, recombinant enzyme
2.66
pyruvate
-
pH 8, 30°C
2.7
pyruvate
pH 6.5, 30°C, recombinant enzyme
3.1
pyruvate
-
isoform LDHD3, pH 5.5, 35°C
3.4
pyruvate
recombinant enzyme, pH and temperature not specified in the publication
5.9
pyruvate
pH 6.5, 30°C, recombinant enzyme
6
pyruvate
-
mutant A234C, pH 7, 27°C
6.1
pyruvate
-
mutant G297A, pH 7, 27°C
6.5
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
7.2
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
7.6
pyruvate
pH 8.0, 30°C, recombinant enzyme
8.2
pyruvate
-
30°C, pH 5.5, mutant enzyme N97D
9.2
pyruvate
-
mutant A78V, pH 7, 27°C
9.5
pyruvate
-
mutant A234S, pH 7, 27°C
10.6
pyruvate
-
mutant T75L/A234S, pH 7, 27°C
11.5
pyruvate
-
mutant T75L/A234G, pH 7, 27°C
12.6
pyruvate
-
30°C, pH 5.5, mutant enzyme Y52A
13.1
pyruvate
-
30°C, pH 5.5, mutant enzyme Y52V
14.1
pyruvate
-
mutant T75L, pH 7, 27°C
14.8
pyruvate
-
wild-type, pH 7, 27°C
15.3
pyruvate
-
mutant A234T, pH 7, 27°C
18.5
pyruvate
-
mutant A234G, pH 7, 27°C
20.8
pyruvate
-
mutant F299Y, pH 7, 27°C
21.4
pyruvate
-
mutant T260V, pH 7, 27°C
31
pyruvate
-
30°C, pH 5.5, mutant enzyme F299G
67.3
pyruvate
-
mutant A100V, pH 7, 27°C
136
pyruvate
-
mutant N263G, pH 7, 27°C
additional information
additional information
kinetics and allosteric mechanism of D-LDHs, overview. The enzyme shows a hyperbolic shaped pyruvate saturation curve below pH 6.5, and shows negative cooperativity in the pyruvate saturation curve above pH 7.5
-
additional information
additional information
-
kinetics and allosteric mechanism of D-LDHs, overview. The enzyme shows a hyperbolic shaped pyruvate saturation curve below pH 6.5, and shows negative cooperativity in the pyruvate saturation curve above pH 7.5
-
additional information
additional information
kinetics and allosteric mechanism of D-LDHs, overview. The enzyme shows a hyperbolic shaped pyruvate saturation curve below pH 6.5, and shows positive cooperativity in the pyruvate saturation curve above pH 7.5
-
additional information
additional information
kinetics and allosteric mechanism of D-LDHs, overview. The enzyme shows a hyperbolic shaped pyruvate saturation curve below pH 6.5, and shows positive cooperativity in the pyruvate saturation curve above pH 7.5
-
additional information
additional information
-
kinetics and allosteric mechanism of D-LDHs, overview. The enzyme shows a hyperbolic shaped pyruvate saturation curve below pH 6.5, and shows positive cooperativity in the pyruvate saturation curve above pH 7.5
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.056 - 21
2-ketocaproate
0.51
2-Ketoglutarate
-
30°C, pH 5.5, wild-type enzyme
11.1 - 65.7
2-ketoisocaproate
11.7 - 27
2-ketoisovalerate
50.7 - 2220
2-oxobutanoate
39 - 200
2-oxoisocaproate
120
2-oxoisovalerate
pH 7.0, 30°C, recombinant enzyme
0.13 - 2.17
3,4-dihydroxyphenylpyruvic acid
33.9 - 179
3-methyl-2-oxobutanoate
8.1 - 420
Hydroxypyruvate
0.66 - 4.51
nicotinamide cytosine dinucleotide
0.31 - 2013
phenylpyruvate
0.07
(R)-lactate
pH 6.5, 30°C, recombinant enzyme
910
(R)-lactate
-
pH 8, , 30°C
2280
(R)-lactate
-
pH 11.0, 20°C, recombinant enzyme
41
2-Ketobutyrate
-
30°C, pH 5.5, mutant enzyme Y52V
41.5
2-Ketobutyrate
-
30°C, pH 5.5, mutant enzyme Y52A
118
2-Ketobutyrate
-
30°C, pH 5.5, wild-type enzyme
175
2-Ketobutyrate
-
30°C, pH 5.5, mutant enzyme Y52L
0.056
2-ketocaproate
-
30°C, pH 5.5, mutant enzyme Y52L
0.3
2-ketocaproate
-
30°C, pH 5.5, mutant enzyme Y52V
0.36
2-ketocaproate
-
30°C, pH 5.5, mutant enzyme Y52R/F299G
0.7
2-ketocaproate
-
30°C, pH 5.5, mutant enzyme Y52A
15.9
2-ketocaproate
-
30°C, pH 5.5, mutant enzyme Y52R
21
2-ketocaproate
-
30°C, pH 5.5, wild-type enzyme
11.1
2-ketoisocaproate
-
30°C, pH 5.5, wild-type enzyme
15.8
2-ketoisocaproate
-
30°C, pH 5.5, mutant enzyme Y52A
17
2-ketoisocaproate
-
30°C, pH 5.5, mutant enzyme Y52V
65.7
2-ketoisocaproate
-
30°C, pH 5.5, mutant enzyme Y52L
11.7
2-ketoisovalerate
-
30°C, pH 5.5, mutant enzyme Y52L
27
2-ketoisovalerate
-
30°C, pH 5.5, wild-type enzyme
5.7
2-ketovalerate
-
30°C, pH 5.5, wild-type enzyme
55.7
2-ketovalerate
-
30°C, pH 5.5, mutant enzyme Y52A
102
2-ketovalerate
-
30°C, pH 5.5, mutant enzyme Y52V
334
2-ketovalerate
-
30°C, pH 5.5, mutant enzyme Y52L
50.7
2-oxobutanoate
wild-type, pH 5.5, 30°C
99.4
2-oxobutanoate
mutant Y51F, pH 5.5, 30°C
152
2-oxobutanoate
mutant Y51M, pH 5.5, 30°C
199
2-oxobutanoate
mutant Y51L, pH 5.5, 30°C
2220
2-oxobutanoate
-
pH 8, 30°C
4.5
2-oxobutyrate
-
30°C, pH 5.5, mutant enzyme N97D
31
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
100
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
120
2-oxobutyrate
-
30°C, pH 5.5, wild-type enzyme
140
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
160
2-oxocaproate
pH 7.0, 30°C, recombinant enzyme
230
2-oxocaproate
pH 7.0, 30°C, recombinant enzyme
39
2-oxoisocaproate
pH 7.0, 30°C, recombinant enzyme
200
2-oxoisocaproate
pH 7.0, 30°C, recombinant enzyme
69
2-oxovalerate
pH 7.0, 30°C, recombinant enzyme
140
2-oxovalerate
pH 7.0, 30°C, recombinant enzyme
0.13
3,4-dihydroxyphenylpyruvic acid
-
cosubstrate NADPH, pH 8.0, 25°C
2.17
3,4-dihydroxyphenylpyruvic acid
-
cosubstrate NADH, pH 8.0, 25°C
33.9
3-methyl-2-oxobutanoate
wild-type, pH 5.5, 30°C
76.2
3-methyl-2-oxobutanoate
mutant Y51M, pH 5.5, 30°C
90.2
3-methyl-2-oxobutanoate
mutant Y51L, pH 5.5, 30°C
179
3-methyl-2-oxobutanoate
mutant Y51F, pH 5.5, 30°C
11
glyoxylate
pH 7.0, 30°C, recombinant enzyme
50
glyoxylate
-
30°C, pH 5.5, mutant enzyme N97D
100
glyoxylate
pH 7.0, 30°C, recombinant enzyme
270
glyoxylate
-
30°C, pH 5.5, wild-type enzyme
880
glyoxylate
pH 7.0, 30°C, recombinant enzyme
8.1
Hydroxypyruvate
-
30°C, pH 5.5, mutant enzyme F299G
13.8
Hydroxypyruvate
-
30°C, pH 5.5, mutant enzyme Y52R
19
Hydroxypyruvate
-
30°C, pH 5.5, mutant enzyme Y52R/F299G
35.8
Hydroxypyruvate
-
30°C, pH 5.5, mutant enzyme F299S
38
Hydroxypyruvate
-
30°C, pH 5.5, mutant enzyme N97D
50
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
50
Hydroxypyruvate
-
30°C, pH 5.5, mutant enzyme Y52V
104
Hydroxypyruvate
-
30°C, pH 5.5, mutant enzyme Y52A
160
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
257
Hydroxypyruvate
-
30°C, pH 5.5, wild-type enzyme
260
Hydroxypyruvate
-
30°C, pH 5.5, wild-type enzyme
407
Hydroxypyruvate
-
30°C, pH 5.5, mutant enzyme Y52L
420
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
0.08
NAD+
mutant V152R/I177K/N213I, pH not specified in the publication, temperature not specified in the publication
0.08
NAD+
mutant V152R/N213E, pH not specified in the publication, temperature not specified in the publication
0.62
NAD+
mutant V152R/I177K, pH not specified in the publication, temperature not specified in the publication
0.64
NAD+
-
isozyme D-LDH3, pH 8.0, 25°C
2.14
NAD+
mutant V152R, pH not specified in the publication, temperature not specified in the publication
2.84
NAD+
wild-type, pH not specified in the publication, temperature not specified in the publication
3.65
NAD+
-
isozyme D-LDH2, pH 8.0, 25°C
4.42
NAD+
-
isozyme D-LDH1, pH 8.0, 25°C
8.28
NADH
-
isozyme D-LDH3, pH 8.0, 25°C
80
NADH
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
90
NADH
pH 8.0, 30°C, recombinant enzyme
98
NADH
pH 7.0, 30°C, recombinant enzyme
110
NADH
pH 8.0, 30°C, recombinant enzyme, with Mg2+
144.4
NADH
-
isozyme D-LDH1, pH 8.0, 25°C
270
NADH
pH 8.0, 30°C, recombinant enzyme, with or without fructose 1,6-bisphosphate and Mg2+
310
NADH
pH 7.0, 30°C, recombinant enzyme
516.4
NADH
-
isozyme D-LDH2, pH 8.0, 25°C
640
NADH
pH 7.0, 30°C, recombinant enzyme
690
NADH
pH 8.0, 30°C, recombinant enzyme, with Mg2+
710
NADH
pH 8.0, 30°C, recombinant enzyme
730
NADH
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
0.66
nicotinamide cytosine dinucleotide
wild-type, pH not specified in the publication, temperature not specified in the publication
2.02
nicotinamide cytosine dinucleotide
mutant V152R/I177K/N213I, pH not specified in the publication, temperature not specified in the publication
2.95
nicotinamide cytosine dinucleotide
mutant V152R/N213E, pH not specified in the publication, temperature not specified in the publication
3.61
nicotinamide cytosine dinucleotide
mutant V152R, pH not specified in the publication, temperature not specified in the publication
4.51
nicotinamide cytosine dinucleotide
mutant V152R/I177K, pH not specified in the publication, temperature not specified in the publication
0.48
oxaloacetate
-
30°C, pH 5.5, mutant enzyme Y52R
6.5
oxaloacetate
-
30°C, pH 5.5, mutant enzyme F299S
80
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
280
oxaloacetate
-
30°C, pH 5.5, wild-type enzyme
410
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
1100
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
1570
oxaloacetate
-
pH 8, 30°C
0.31
phenylpyruvate
-
30°C, pH 5.5, mutant enzyme Y52R
1.8
phenylpyruvate
-
pH 7.4, 37°C, recombinant His-taged mutant F299Y
2.1
phenylpyruvate
-
30°C, pH 5.5, mutant enzyme F299S
2.8
phenylpyruvate
-
30°C, pH 5.5, mutant enzyme Y52R/F299G
3.4
phenylpyruvate
-
30°C, pH 5.5, mutant enzyme F299G
5.2
phenylpyruvate
-
30°C, pH 5.5, mutant enzyme Y52T/D299S
11.3
phenylpyruvate
-
pH 7.4, 37°C, recombinant His-taged wild-type enzyme
12.29
phenylpyruvate
pH 7, 30°C
18
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
40
phenylpyruvate
-
30°C, pH 5.5, wild-type enzyme
41.3
phenylpyruvate
wild-type, pH 5.5, 30°C
120
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
122.7
phenylpyruvate
-
pH 8, 50°C
171
phenylpyruvate
-
30°C, pH 5.5, mutant enzyme Y52V
173
phenylpyruvate
-
pH 5.5, 45°C
232
phenylpyruvate
-
30°C, pH 5.5, mutant enzyme Y52A
239
phenylpyruvate
mutant Y51S, pH 5.5, 30°C
269
phenylpyruvate
mutant Y51A, pH 5.5, 30°C
305
phenylpyruvate
-
recombinant enzyme, pH 5.5, 30°C
376
phenylpyruvate
mutant Y51L, pH 5.5, 30°C
391
phenylpyruvate
mutant Y51F, pH 5.5, 30°C
462
phenylpyruvate
mutant Y51M, pH 5.5, 30°C
778
phenylpyruvate
-
30°C, pH 5.5, mutant enzyme Y52L
1447
phenylpyruvate
-
pH 7.4, 37°C, recombinant His-taged mutant Y52L/F299Y
2013
phenylpyruvate
-
pH 7.4, 37°C, recombinant His-taged mutant Y52L
0.00008
pyruvate
-
mutant A234C, pH 7, 27°C
0.00009
pyruvate
-
mutant A234T, pH 7, 27°C
0.00016
pyruvate
-
mutant A100V, pH 7, 27°C
0.00019
pyruvate
-
mutant G297A, pH 7, 27°C
0.00031
pyruvate
-
mutant A78V, pH 7, 27°C
0.00044
pyruvate
-
mutant F299Y, pH 7, 27°C
0.00046
pyruvate
-
wild-type, pH 7, 27°C
0.00057
pyruvate
-
mutant A234S, pH 7, 27°C
0.00057
pyruvate
-
mutant T260V, pH 7, 27°C
0.00069
pyruvate
-
mutant A234G, pH 7, 27°C
0.00072
pyruvate
-
mutant N263G, pH 7, 27°C
0.00078
pyruvate
-
mutant T75L, pH 7, 27°C
0.00181
pyruvate
-
mutant T75L/A234G, pH 7, 27°C
0.00225
pyruvate
-
mutant T75L/A234S, pH 7, 27°C
10.7
pyruvate
-
isoform LDHD3, pH 5.5, 35°C
11.3
pyruvate
pH 6.5, 30°C, recombinant enzyme
22
pyruvate
-
30°C, pH 5.5, mutant enzyme F299G
25.5
pyruvate
-
30°C, pH 5.5, mutant enzyme Y52A
37
pyruvate
-
30°C, pH 5.5, mutant enzyme Y52V
44.7
pyruvate
-
isoform LDHD2, pH 7.5, 35°C
75.8
pyruvate
-
isoform LDHD1, pH 6, 35°C
80
pyruvate
pH 7.0, 30°C, recombinant enzyme
80
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
87
pyruvate
pH 8.0, 30°C, recombinant enzyme
91.3
pyruvate
pH 6.5, 30°C, recombinant enzyme
100
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
213
pyruvate
-
30°C, pH 5.5, mutant enzyme Y52L
235.5
pyruvate
pH 6.5, 30°C, recombinant enzyme
240
pyruvate
pH 8.0, 30°C, recombinant enzyme
240
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
270
pyruvate
-
30°C, pH 5.5, mutant enzyme N97D
290
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
320
pyruvate
-
30°C, pH 5.5, wild-type enzyme
320
pyruvate
-
pH 5.5, 45°C
321
pyruvate
-
30°C, pH 5.5, wild-type enzyme
370
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
380
pyruvate
pH 8.0, 30°C, recombinant enzyme
400
pyruvate
pH 7.0, 30°C, recombinant enzyme
400
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
410
pyruvate
pH 7.0, 30°C, recombinant enzyme
512.2
pyruvate
recombinant enzyme, pH and temperature not specified in the publication
2750
pyruvate
-
pH 8, 30°C
29000
pyruvate
-
pH 8.0, 30°C, recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0073 - 10.32
(R)-lactate
4.4 - 37.2
2-oxobutanoate
3.2 - 53
2-oxoisocaproate
35
2-oxoisovalerate
pH 7.0, 30°C, recombinant enzyme
1.3 - 24.07
3,4-dihydroxyphenylpyruvic acid
0.89 - 23.2
3-methyl-2-oxobutanoate
4.2 - 140
Hydroxypyruvate
0.48 - 5.6
nicotinamide cytosine dinucleotide
0.0073
(R)-lactate
pH 6.5, 30°C, recombinant enzyme
10.32
(R)-lactate
-
pH 8, , 30°C
4.4
2-oxobutanoate
wild-type, pH 5.5, 30°C
9.48
2-oxobutanoate
-
pH 8, 30°C
16.8
2-oxobutanoate
mutant Y51L, pH 5.5, 30°C
20.7
2-oxobutanoate
mutant Y51M, pH 5.5, 30°C
37.2
2-oxobutanoate
mutant Y51F, pH 5.5, 30°C
1
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
150
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
440
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
27
2-oxocaproate
pH 7.0, 30°C, recombinant enzyme
87
2-oxocaproate
pH 7.0, 30°C, recombinant enzyme
3.2
2-oxoisocaproate
pH 7.0, 30°C, recombinant enzyme
53
2-oxoisocaproate
pH 7.0, 30°C, recombinant enzyme
18
2-oxovalerate
pH 7.0, 30°C, recombinant enzyme
200
2-oxovalerate
pH 7.0, 30°C, recombinant enzyme
1.3
3,4-dihydroxyphenylpyruvic acid
-
cosubstrate NADPH, pH 8.0, 25°C
24.07
3,4-dihydroxyphenylpyruvic acid
-
cosubstrate NADH, pH 8.0, 25°C
0.89
3-methyl-2-oxobutanoate
wild-type, pH 5.5, 30°C
7.4
3-methyl-2-oxobutanoate
mutant Y51L, pH 5.5, 30°C
8.9
3-methyl-2-oxobutanoate
mutant Y51M, pH 5.5, 30°C
23.2
3-methyl-2-oxobutanoate
mutant Y51F, pH 5.5, 30°C
0.7
glyoxylate
pH 7.0, 30°C, recombinant enzyme
5.3
glyoxylate
pH 7.0, 30°C, recombinant enzyme
130
glyoxylate
pH 7.0, 30°C, recombinant enzyme
4.2
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
8.7
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
140
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
0.05
NAD+
mutant V152R/N213E, pH not specified in the publication, temperature not specified in the publication
0.074
NAD+
mutant V152R/I177K/N213I, pH not specified in the publication, temperature not specified in the publication
0.71
NAD+
mutant V152R/I177K, pH not specified in the publication, temperature not specified in the publication
1.41
NAD+
-
isozyme D-LDH2, pH 8.0, 25°C
1.56
NAD+
-
isozyme D-LDH3, pH 8.0, 25°C
1.61
NAD+
-
isozyme D-LDH1, pH 8.0, 25°C
2.3
NAD+
mutant V152R, pH not specified in the publication, temperature not specified in the publication
10.1
NAD+
wild-type, pH not specified in the publication, temperature not specified in the publication
56.16
NADH
-
pH 8, 50°C
182.6
NADH
-
isozyme D-LDH2, pH 8.0, 25°C
206.3
NADH
-
isozyme D-LDH1, pH 8.0, 25°C
232.6
NADH
-
isozyme D-LDH3, pH 8.0, 25°C
2500
NADH
pH 8.0, 30°C, recombinant enzyme
2800
NADH
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
3700
NADH
pH 8.0, 30°C, recombinant enzyme, with Mg2+
4400
NADH
pH 7.0, 30°C, recombinant enzyme
7700
NADH
pH 8.0, 30°C, recombinant enzyme
7700
NADH
pH 8.0, 30°C, recombinant enzyme, with Mg2+
7700
NADH
pH 8.0, 30°C, recombinant enzyme, with Mg2+
7800
NADH
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
8000
NADH
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
8100
NADH
pH 8.0, 30°C, recombinant enzyme
12000
NADH
pH 7.0, 30°C, recombinant enzyme
17000
NADH
pH 7.0, 30°C, recombinant enzyme
0.48
nicotinamide cytosine dinucleotide
wild-type, pH not specified in the publication, temperature not specified in the publication
2.1
nicotinamide cytosine dinucleotide
mutant V152R/N213E, pH not specified in the publication, temperature not specified in the publication
3.1
nicotinamide cytosine dinucleotide
mutant V152R/I177K/N213I, pH not specified in the publication, temperature not specified in the publication
3.3
nicotinamide cytosine dinucleotide
mutant V152R/I177K, pH not specified in the publication, temperature not specified in the publication
5.6
nicotinamide cytosine dinucleotide
mutant V152R, pH not specified in the publication, temperature not specified in the publication
19.87
oxaloacetate
-
pH 8, 30°C
21
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
31
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
230
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
1
phenylpyruvate
-
pH 7.4, 37°C, recombinant His-taged wild-type enzyme
2.6
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
4.34
phenylpyruvate
pH 7, 30°C
5.7
phenylpyruvate
-
pH 7.4, 37°C, recombinant His-taged mutant F299Y
6 - 12
phenylpyruvate
mutant Y51S, pH 5.5, 30°C
11
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
15.9
phenylpyruvate
wild-type, pH 5.5, 30°C
73.01
phenylpyruvate
-
pH 8, 50°C
100
phenylpyruvate
-
pH 5.5, 45°C
105
phenylpyruvate
-
recombinant enzyme, pH 5.5, 30°C
1000
phenylpyruvate
-
pH 7.4, 37°C, recombinant His-taged mutant Y52L/F299Y
1720
phenylpyruvate
mutant Y51A, pH 5.5, 30°C
1880
phenylpyruvate
mutant Y51F, pH 5.5, 30°C
2130
phenylpyruvate
mutant Y51M, pH 5.5, 30°C
2200
phenylpyruvate
mutant Y51L, pH 5.5, 30°C
7500
phenylpyruvate
-
pH 7.4, 37°C, recombinant His-taged mutant Y52L
0.000002
pyruvate
-
mutant A100V, pH 7, 27°C
0.000005
pyruvate
-
mutant N263G, pH 7, 27°C
0.000006
pyruvate
-
mutant A234T, pH 7, 27°C
0.000013
pyruvate
-
mutant A234C, pH 7, 27°C
0.000021
pyruvate
-
mutant F299Y, pH 7, 27°C
0.000027
pyruvate
-
mutant T260V, pH 7, 27°C
0.000031
pyruvate
-
mutant G297A, pH 7, 27°C
0.000031
pyruvate
-
wild-type, pH 7, 27°C
0.000034
pyruvate
-
mutant A78V, pH 7, 27°C
0.000037
pyruvate
-
mutant A234G, pH 7, 27°C
0.000055
pyruvate
-
mutant T75L, pH 7, 27°C
0.00006
pyruvate
-
mutant A234S, pH 7, 27°C
0.000157
pyruvate
-
mutant T75L/A234G, pH 7, 27°C
0.000211
pyruvate
-
mutant T75L/A234S, pH 7, 27°C
1.9
pyruvate
pH 6.5, 30°C, recombinant enzyme
3.5
pyruvate
-
isoform LDHD3, pH 5.5, 35°C
32
pyruvate
-
isoform LDHD2, pH 7.5, 35°C
34
pyruvate
pH 6.5, 30°C, recombinant enzyme
35
pyruvate
pH 8.0, 30°C, recombinant enzyme
50
pyruvate
pH 8.0, 30°C, recombinant enzyme
51
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
60
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
61
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
65
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
160
pyruvate
pH 7.0, 30°C, recombinant enzyme
161
pyruvate
-
isoform LDHD1, pH 6, 35°C
200
pyruvate
pH 8.0, 30°C, recombinant enzyme
230
pyruvate
pH 7.0, 30°C, recombinant enzyme
280
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
658
pyruvate
-
pH 5.5, 45°C
820
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
1030
pyruvate
-
pH 8, 30°C
3157
pyruvate
-
recombinant enzyme, pH 5.5, 30°C
4000
pyruvate
pH 7.0, 30°C, recombinant enzyme
7900
pyruvate
pH 6.5, 30°C, recombinant enzyme
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F299G
-
mutation reduces enzyme activity with less marked change in substrate preference
F299S
-
mutation reduces enzyme activity with less marked change in substrate preference
Y52D
-
mutation severely reduces enzyme activity
Y52L
-
site-directed mutagenesis, enhancement of phenyllactic acid biosynthesis by recognition site replacement of D-lactate dehydrogenase from Lactobacillus pentosus
Y52R
-
mutation severely reduces enzyme activity, preference for large aliphatic 2-ketoacids and phenylpyruvate
Y52R/F299G
-
mutation abolishes activity with pyruvate, 2-ketobutyrate, 2-ketovalerate, 2-ketoisovalerate, 2-ketoisocaproate and oxaloacetate, weak activity with 2-ketocaproate, 2-ketoglutarate and phenylpyruvate
Y52T
-
mutation severely reduces enzyme activity
Y52T/F299S
-
mutation abolishes activity with pyruvate, 2-ketobutyrate, 2-ketovalerate, 2-ketoisovalerate, 2-ketoisocaproate, 2-ketoglutarate and oxaloacetate, weak activity with hydroxypyruvate and phenylpyruvate
Y52L
-
mutant used for synthesis of (R)-2-hydroxy-4-phenylbutyric acid in Pichia pastoris
D259N
-
56fold reduction in kcat, 5fold lowering of Km, shifting of the enzymatic activity profile towards the acidic range by two units
E264G
-
shift of 2 units in optimal pH toward the acidic range
F299Y
-
site-directed mutagenesis
H205K
-
125-fold reduction in Kcat
H303K
-
Km for pyruvate increased fourfold
Y52L
-
site-directed mutagenesis
F299Y
-
site-directed mutagenesis
-
Y52L
-
site-directed mutagenesis
-
Y52L/F299Y
-
site-directed mutagenesis
-
V152R
catalytic efficiency with NAD analogue nicotinamide cytosine dinucleotide is 2.4fold higher than that with NAD
V152R/I177K
mutant shows good activity with NAD analogue nicotinamide cytosine dinucleotide and reduced activity with NAD
V152R/I177K/N213I
triple mutant shows high preference or activity with NAD analogue nicotinamide cytosine dinucleotide
V152R/N213E
mutant shows good activity with NAD analogue nicotinamide cytosine dinucleotide and reduced activity with NAD
V152R/V210N/N213E
triple mutant shows high preference or activity with NAD analogue nicotinamide cytosine dinucleotide
F298L
negligible activity
F298V
negligible activity
N76A
reduced activity compared to wild-type
N76L
reduced activity compared to wild-type
N76V
reduced activity compared to wild-type
V77I
reduced activity compared to wild-type
Y100F
reduced activity compared to wild-type
Y100I
negligible activity
Y100L
negligible activity
Y51A
mutant with improved catalytic efficiency on phenylpyruvate
Y51F
mutant with improved catalytic efficiency on 2-oxobutanoate and 3-methyl-2-oxobutanoate of 37.2 and 23.2 per s and mM, respectively
Y51L
mutant with improved catalytic efficiency on phenylpyruvate of 2200 per s and mM
Y51M
mutant with improved catalytic efficiency on phenylpyruvate
Y51S
mutant with improved catalytic efficiency on phenylpyruvate
N76A
-
reduced activity compared to wild-type
-
V77I
-
reduced activity compared to wild-type
-
Y100L
-
negligible activity
-
Y51A
-
mutant with improved catalytic efficiency on phenylpyruvate
-
Y51F
-
mutant with improved catalytic efficiency on 2-oxobutanoate and 3-methyl-2-oxobutanoate of 37.2 and 23.2 per s and mM, respectively
-
E263A
site-directed mutagenesis, the mutant shows highly reduced D-lactate dehydrogenase activity compared to the wild-type enzyme
F298A
site-directed mutagenesis, almost inactive D-lactate dehydrogenase mutant
G79A
site-directed mutagenesis, almost inactive D-lactate dehydrogenase mutant
H295A
site-directed mutagenesis, inactive D-lactate dehydrogenase mutant
M307A
site-directed mutagenesisthe mutant shows highly reduced D-lactate dehydrogenase activity compared to the wild-type enzyme
R234A
site-directed mutagenesis, inactive D-lactate dehydrogenase mutant
Y101A
site-directed mutagenesis, the mutant shows 50% reduced D-lactate dehydrogenase activity compared to the wild-type enzyme
G79A
-
site-directed mutagenesis, almost inactive D-lactate dehydrogenase mutant
-
H295A
-
site-directed mutagenesis, inactive D-lactate dehydrogenase mutant
-
R234A
-
site-directed mutagenesis, inactive D-lactate dehydrogenase mutant
-
Y101A
-
site-directed mutagenesis, the mutant shows 50% reduced D-lactate dehydrogenase activity compared to the wild-type enzyme
-
A100V
-
less than 10% of wild-type catalytic efficiency
A234C
-
about 30% of wild-type catalytic efficiency
A234G
-
mutation enhances catalytic activity toward pyruvate
A234S
-
mutation enhances catalytic activity toward pyruvate
A234T
-
about 15% of wild-type catalytic efficiency
A78V
-
specific activity similar to wild-type
F299Y
-
specific activity similar to wild-type
G297A
-
about 20% increase in activity
N263G
-
about 30% of wild-type activity
T260V
-
specific activity similar to wild-type
T75L
-
increase in specific acitivity
T75L/A234g
-
mutation improves kcat/Km by 5fold
T75L/A234S
-
mutation improves kcat/Km by 6.8fold
V296G
-
strong decrease in activity
A234G
-
mutation enhances catalytic activity toward pyruvate
-
A234S
-
mutation enhances catalytic activity toward pyruvate
-
F299Y
-
specific activity similar to wild-type
-
T75L
-
increase in specific acitivity
-
Y101A
strong decrease in activity
H296A
-
loss of activity
-
R235A
-
loss of activity
-
Y101A
-
strong decrease in activity
-
Y52A
-
mutation induces high activity and preference for large aliphatic 2-ketoacids and phenylpyruvate
Y52A
-
site-directed mutagenesis, enhancement of phenyllactic acid biosynthesis by recognition site replacement of D-lactate dehydrogenase from Lactobacillus pentosus
Y52V
-
mutation induces high activity and preference for large aliphatic 2-ketoacids and phenylpyruvate
Y52V
-
site-directed mutagenesis, enhancement of phenyllactic acid biosynthesis by recognition site replacement of D-lactate dehydrogenase from Lactobacillus pentosus. Escherichia coli pET-28a-d-ldh produces 12.2 g phenyllactate/l in 3 h with a molar conversion rate of 61%, while Escherichia coli pET-28a-d-ldhY52V produces 15.6 g phenyllactate/l with a molar conversion rate of 77%. Site-directed mutagenesis of d-ldh markedly improves D-phenyllactate yield and substrate conversion rate. Phenyllactate yield does not show a significant increase when higher glucose amounts are added. Method optimization, overview
H296K
-
no significant change
H296K
no significant changes in kcat or Km value, shift of optimum pH value from 7.0-7.5 to 6
Y52L/F299Y
-
site-directed mutagenesis
Y52L/F299Y
-
the mutant shows a specific activity that is 233.2-312.3fold higher than that of the wild type recombinant enzyme
Y52L/F299Y
-
the mutant shows a specific activity that is 233.2-312.3fold higher than that of the wild type recombinant enzyme
-
additional information
-
at media D-lactate concentrations greater than 5-10 mM the development of wild-type plants is arrested shortly after germination whereas plants overexpressing the endogenous D-lactate dehydrogenase detoxify D-lactate to pyruvate and survive, phenotypes, overview
additional information
-
at media D-lactate concentrations greater than 5-10 mM the development of wild-type plants is arrested shortly after germination whereas plants overexpressing the endogenous D-lactate dehydrogenase detoxify D-lactate to pyruvate and survive, phenotypes, overview
-
additional information
-
due to the presence of the pentose phosphate pathway, wild-type strain IO-1 produces only L-lactic acid, disruption of the phosphoketolase pathway by deletion of the phosphoketolase 1 gene xpk1 in the L-lactate dehydrogenase gene ldhL1-deficient DELTAxpk1,DELTAldhL1 NCIMB 8826 strain results in strain DELTAldhL1 NCIMB 8826, which produces optically pure D-lactic acid, introduction of the pentose phosphate pathway by introduction of the transketolase gene from Lactococcus lactis IL 1403 into this strain. Xylose fermentation by the mutant strains, overview
additional information
-
due to the presence of the pentose phosphate pathway, wild-type strain IO-1 produces only L-lactic acid, disruption of the phosphoketolase pathway by deletion of the phosphoketolase 1 gene xpk1 in the L-lactate dehydrogenase gene ldhL1-deficient DELTAxpk1,DELTAldhL1 NCIMB 8826 strain results in strain DELTAldhL1 NCIMB 8826, which produces optically pure D-lactic acid, introduction of the pentose phosphate pathway by introduction of the transketolase gene from Lactococcus lactis IL 1403 into this strain. Xylose fermentation by the mutant strains, overview
-
additional information
Lactiplantibacillus plantarum NCIMB 8826 delta ldhL1 -xpk1::tkt-delta xpk
-
due to the presence of the pentose phosphate pathway, wild-type strain IO-1 produces only L-lactic acid, disruption of the phosphoketolase pathway by deletion of the phosphoketolase 1 gene xpk1 in the L-lactate dehydrogenase gene ldhL1-deficient DELTAxpk1,DELTAldhL1 NCIMB 8826 strain results in strain DELTAldhL1 NCIMB 8826, which produces optically pure D-lactic acid, introduction of the pentose phosphate pathway by introduction of the transketolase gene from Lactococcus lactis IL 1403 into this strain. Xylose fermentation by the mutant strains, overview
-
additional information
-
highly stereoselective biosynthesis of (R)-alpha-hydroxy carboxylic acids through rationally re-designed mutation of D-lactate dehydrogenase, asymmetric reduction of a homologous series of alpha-keto carboxylic acids such as phenylpyruvic acid, 2-oxobutyric acid, 2-oxovaleric acid, beta-hydroxypyruvate, overview. Compared with wild-type D-nLDH, the Y52L mutant D-nLDH shows elevated activities toward unnatural substrates especially with large substitutes at C-3. By the biocatalysis combined with a formate dehydrogenase for in situ generation of NADH, the corresponding (R)-alpha-hydroxy carboxylic acids can be produced at high yields and highly optical purity. Production of chiral (R)-phenyllactic acid. 50 mM PPA is completely reduced to (R)-phenyllactate in 90 min with a high yield of 99.0% and a highly optical purity (99.9% e.e.) by the engineered coupled production system. Activties of the F299Y mutant are similar to the wild-type enzyme
additional information
-
highly stereoselective biosynthesis of (R)-alpha-hydroxy carboxylic acids through rationally re-designed mutation of D-lactate dehydrogenase, asymmetric reduction of a homologous series of alpha-keto carboxylic acids such as phenylpyruvic acid, 2-oxobutyric acid, 2-oxovaleric acid, beta-hydroxypyruvate, overview. Compared with wild-type D-nLDH, the Y52L mutant D-nLDH shows elevated activities toward unnatural substrates especially with large substitutes at C-3. By the biocatalysis combined with a formate dehydrogenase for in situ generation of NADH, the corresponding (R)-alpha-hydroxy carboxylic acids can be produced at high yields and highly optical purity. Production of chiral (R)-phenyllactic acid. 50 mM PPA is completely reduced to (R)-phenyllactate in 90 min with a high yield of 99.0% and a highly optical purity (99.9% e.e.) by the engineered coupled production system. Activties of the F299Y mutant are similar to the wild-type enzyme
-
additional information
enzymatic production of D-3-phenyllactic acid by recombinant Pediococcus pentosaceus D-lactate dehydrogenase with NADH regeneration by recombinant Ogataea parapolymorpha formate dehydrogenase, EC 1.2.1.2, at pH 6.0, 50°C
additional information
-
enzymatic production of D-3-phenyllactic acid by recombinant Pediococcus pentosaceus D-lactate dehydrogenase with NADH regeneration by recombinant Ogataea parapolymorpha formate dehydrogenase, EC 1.2.1.2, at pH 6.0, 50°C
additional information
-
enzyme deletion mutant, sensitive to osmotic conditions indicating an aktin disfunction
additional information
glutamate dehydrogenase activities of enzyme mutants, overview
additional information
-
glutamate dehydrogenase activities of enzyme mutants, overview
additional information
-
glutamate dehydrogenase activities of enzyme mutants, overview
-
additional information
-
random mutagensis, and screening for gain-of-function mutants, mutant Y2-8 shows improved D(-)-lactate synthesis, which is 2fold increased compared to the wild-type strain DX12
additional information
-
random mutagensis, and screening for gain-of-function mutants, mutant Y2-8 shows improved D(-)-lactate synthesis, which is 2fold increased compared to the wild-type strain DX12
-
additional information
-
construction of peroxidase-based biosensors for the selective determination of D,L-lactic acid and L-malic acid in wines, enzyme immobilization, method optimization, overview
additional information
fermentation conditions are critical for microbial growth and lactic acid secretion, optimization of enzyme and D-lactic acid production by the enzyme from Thermodesulfatator indicus in Bacillus licheniformis strains B11 and BA11, overview. Disruption of the lactate permease LctP in host strains BN11 and BA11 results in reductions in D-lactic acid (28.6 and 35.2%, respectively). Replacement of LctP inhost strain BN11 with the mesophilic permease LldP of Escherichia coli also leads to a 12.1% decrease in D-lactic acid accumulation
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Garvie, E.I.
Bacterial lactate dehydrogenases
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Escherichia coli, Eubacterium limosum, Klebsiella aerogenes, Lacticaseibacillus casei, Lactiplantibacillus plantarum, Lactobacillus acidophilus, Lactobacillus delbrueckii, Lactobacillus delbrueckii subsp. bulgaricus, Lactobacillus delbrueckii subsp. lactis, Lactobacillus jensenii, Lactobacillus jugurt-helveticus, Lactobacillus leichmannii, Lactobacillus vermiforme, Lactococcus lactis, Lentilactobacillus buchneri, Leuconostoc lactis, Leuconostoc mesenteroides, Leuconostoc mesenteroides subsp. cremoris, Leuconostoc mesenteroides subsp. dextranicum, Levilactobacillus brevis, Limosilactobacillus fermentum, Mammalia, Mycoplasma sp., Oenococcus oeni, Pediococcus acidilactici, Pediococcus damnosus, Pediococcus inopinatus, Pediococcus pentosaceus, Selenomonas ruminantium, Staphylococcus aureus, Staphylococcus haemolyticus, Staphylococcus hominis, Staphylococcus sp., Staphylococcus warneri, Weissella confusa, Weissella paramesenteroides, Weissella viridescens
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-
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D(-)-lactate dehydrogenase from fungi
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Globisporangium debaryanum, Elongisporangium undulatum, Sapromyces elongatus
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Salt-induced alteration of D(-) lactate dehydrogenase from Polyspondylium pallidum
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-
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Cornu aspersum
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207
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Haliotis cracherodii, Cornu aspersum
-
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D(-)-Lactate dehydrogenase from butyribacterium rettgeri
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Limulus polyphemus
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Allomyces sp.
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Lactobacillus delbrueckii subsp. bulgaricus
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Saccharomyces cerevisiae
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Okino, S.; Suda, M.; Fujikura, K.; Inui, M.; Yukawa, H.
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Escherichia coli, Lactobacillus delbrueckii
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Okano, K.; Yoshida, S.; Yamada, R.; Tanaka, T.; Ogino, C.; Fukuda, H.; Kondo, A.
Improved production of homo-D-lactic acid via xylose fermentation by introduction of xylose assimilation genes and redirection of the phosphoketolase pathway to the pentose phosphate pathway in L-Lactate dehydrogenase gene-deficient Lactobacillus plantarum
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Antonyuk, S.V.; Strange, R.W.; Ellis, M.J.; Bessho, Y.; Kuramitsu, S.; Inoue, Y.; Yokoyama, S.; Hasnain, S.S.
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Crystallization and preliminary X-ray analysis of a dye-linked D-lactate dehydrogenase from the aerobic hyperthermophilic archaeon Aeropyrum pernix
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Cloning, expression, purification, crystallization and X-ray crystallographic analysis of D-lactate dehydrogenase from Lactobacillus jensenii
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The D-lactate dehydrogenase from Sporolactobacillus inulinus also possessing reversible deamination activity
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Enzymological characterization of a novel D-lactate dehydrogenase from Lactobacillus rossiae and its application in D-phenyllactic acid synthesis
3 Biotech
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Furfurilactobacillus rossiae (A0A0R1RJ30), Furfurilactobacillus rossiae, Furfurilactobacillus rossiae DSM 15814 (A0A0R1RJ30)
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Luo, X.; Zhang, Y.; Yin, L.; Zheng, W.; Fu, Y.
Efficient synthesis of d-phenyllactic acid by a whole-cell biocatalyst co-expressing glucose dehydrogenase and a novel D-lactate dehydrogenase from Lactobacillus rossiae
3 Biotech
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Cloning of D-lactate dehydrogenase genes of Lactobacillus delbrueckii subsp. bulgaricus and their roles in D-lactic acid production
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Regulator LdhR and D-lactate dehydrogenase LdhA of Burkholderia multivorans play roles in carbon overflow and in planktonic cellular aggregate formation
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Burkholderia multivorans
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Shewanella oneidensis (Q8EI78)
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Nakano, K.; Sawada, S.; Yamada, R.; Mimitsuka, T.; Ogino, H.
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Sporolactobacillus laevolacticus, Sporolactobacillus laevolacticus JCM 2513
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Lawton, J.A.; Prescott, N.A.; Lawton, P.X.
From gene to structure Lactobacillus bulgaricus D-lactate dehydrogenase from yogurt as an integrated curriculum model for undergraduate molecular biology and biochemistry laboratory courses
Biochem. Mol. Biol. Educ.
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Lactobacillus delbrueckii subsp. bulgaricus
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Furukawa, N.; Miyanaga, A.; Nakajima, M.; Taguchi, H.
Structural basis of sequential allosteric transitions in tetrameric D-lactate dehydrogenases from three Gram-negative bacteria
Biochemistry
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Escherichia coli (A0A140N893), Escherichia coli, Fusobacterium nucleatum subsp. nucleatum (Q8RG11), Pseudomonas aeruginosa (Q9I530), Pseudomonas aeruginosa, Pseudomonas aeruginosa DSM 22644 (Q9I530), Fusobacterium nucleatum subsp. nucleatum DSM 15643 (Q8RG11), Escherichia coli BL21-DE3 (A0A140N893)
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Wang, X.; Yu, Z.; Tang, J.; Yi, D.; Chen, S.
Efficient production of (R)-(-)-2-hydroxy-4-phenylbutyric acid by recombinant Pichia pastoris expressing engineered D-lactate dehydrogenase from Lactobacillus plantarum with a single-site mutation
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Lactiplantibacillus plantarum
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Liu, Y.; Li, Q.; Wang, L.; Guo, X.; Wang, J.; Wang, Q.; Zhao, Z.K.
Engineering D-lactate dehydrogenase to favor an non-natural cofactor nicotinamide cytosine dinucleotide
ChemBioChem
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Lactobacillus helveticus (P30901), Lactobacillus helveticus
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Zhou, T.; Qin, L.; Zhu, X.; Shen, W.; Zou, J.; Wang, Z.; Wei, Y.
The D-lactate dehydrogenase MoDLD1 is essential for growth and infection-related development in Magnaporthe oryzae
Environ. Microbiol.
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Pyricularia oryzae (G4MWZ3), Pyricularia oryzae, Pyricularia oryzae ATCC MYA-4617 (G4MWZ3)
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Catalytic, computational, and evolutionary analysis of the (R)-lactate dehydrogenases responsible for D-lactic acid production in lactic acid bacteria
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Leuconostoc mesenteroides subsp. mesenteroides, Leuconostoc mesenteroides subsp. mesenteroides J18
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Wang, Y.; Bai, Y.; Fan, T.; Zheng, X.; Cai, Y.
Reducing 3,4-dihydroxyphenylpyruvic acid to D-3,4-dihydroxyphenyllactic acid via a coenzyme nonspecific D-lactate dehydrogenase from Lactobacillus reuteri
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Limosilactobacillus reuteri, Limosilactobacillus reuteri JN516
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Chen, L.; Bai, Y.; Fan, T.P.; Zheng, X.; Cai, Y.
Characterization of a D-lactate dehydrogenase from Lactobacillus fermentum JN248 with high phenylpyruvate reductive activity
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Limosilactobacillus fermentum, Limosilactobacillus fermentum JN248
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Deka, R.; Liu, W.; Norgard, M.; Brautigam, C.
Biophysical and biochemical characterization of tp0037, a D-lactate dehydrogenase, supports an acetogenic energy conservation pathway in Treponema pallidum
mBio
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Treponema pallidum (O83080), Treponema pallidum, Treponema pallidum Nichols (O83080)
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Wu, B.; Yu, Q.; Zheng, S.; Pedroso, M.; Guddat, L.; He, B.; Schenk, G.
Relative catalytic efficiencies and transcript levels of three d- and two l-lactate dehydrogenases for optically pure d-lactate production in Sporolactobacillus inulinus
MicrobiologyOpen
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Sporolactobacillus inulinus, Sporolactobacillus inulinus YBS1-5
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