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(S)-lactate + 3-acetyl pyridine adenine dinucleotide
pyruvate + reduced 3-acetyl pyridine adenine dinucleotide
-
Substrates: assay is based on reduction of 3-acetyl pyridine adenine dinucleotide that is specific for PfLDH, which allows the distinction of PfLDH from that of the host erythrocyte
Products: -
?
(S)-lactate + 3-acetylpyridine adenine dinucleotide
pyruvate + reduced 3-acetylpyridine adenine dinucleotide
(S)-lactate + APAD+
pyruvate + APADH + H+
Substrates: -
Products: -
r
(S)-lactate + epsilon-NAD+
pyruvate + epsilon-NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD(P)+
pyruvate + NAD(P)H + H+
(S)-lactate + NAD+
pyruvate + NADH + H+
(S)-lactate + NADP+
pyruvate + NADPH + H+
Substrates: wild-type enzyme is specific for NAD+. Mutant enzyme F16Q/I37K/D38SC81S/N85R utilizes NADP+ better than wild-type enzyme, prefers NADP+ to NAD+. Mutant F16Q/C81S/N85R utilizes NAD+ better than wild-type enzyme, weakly active with NADP+
Products: -
?
(S)-lactate + nicotinamide hypoxanthine dinucleotide
pyruvate + reduced nicotinamide hypoxanthine dinucleotide
2-oxobutanoate + NADH + H+
2-hydroxybutanoate + NAD+
Substrates: -
Products: -
?
2-oxobutanoate + NADH + H+
2-hydroxybutyrate + NAD+
2-oxobutyrate + NADH
2-hydroxybutyrate + NAD+
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
2-oxoglutarate + NADH + H+
2-hydroxyglutarate + NAD+
2-oxopentanoate + NADH
2-hydroxypentanoate + NAD+
-
Substrates: 125% of the activity with pyruvate
Products: -
?
2-oxovalerate + NADH
2-hydroxyvalerate + NAD+
-
Substrates: -
Products: -
r
2-oxovalerate + NADH + H+
2-hydroxyvalerate + NAD+
3,4-dihydroxyphenylpyruvate + NADH + H+
L-3,4-dihydroxyphenyllactate + NAD+
Substrates: 8.5% of the activity with pyruvate
Products: -
?
3-fluoropyruvate + NADH
?
3-methyl-2-oxobutanoate + NADH
2-hydroxy-3-methylbutanoate + NAD+
-
Substrates: 28.5% of the activity with pyruvate
Products: -
?
3-methyl-2-oxopentanoate + NADH
2-hydroxy-3-methylpentanoate + NAD+
-
Substrates: 5.3% of the activity with pyruvate
Products: -
?
4-hydroxyphenylpyruvate + NADH + H+
L-4-hydroxyphenyllactate + NAD+
4-methyl-2-oxopentanoate + NADH
2-hydroxy-4-methylpentanoate + NAD+
4-methyl-2-oxopentanoate + NADH + H+
2-hydroxy-4-methylpentanoate + NAD+
Substrates: 25.9% of the activity with pyruvate
Products: -
?
benzoylformate + NADH + H+
L-hydroxy(phenyl)acetate + NAD+
Substrates: 20.5% of the activity with pyruvate
Products: -
?
benzoylformic acid + NADH + H+
? + NAD+
Substrates: -
Products: -
?
bromopyruvate + NADH
3-bromo-2-hydroxypropanoate + NAD+
-
Substrates: -
Products: -
?
ethyl pyruvate + NADH + H+
? + NAD+
glyoxylate + NADH
glycolate + NAD+
glyoxylate + NADH + H+
glycolate + NAD+
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
L-lactate + NAD+
pyruvate + NADH
L-lactate + NAD+
pyruvate + NADH + H+
methyl pyruvate + NADH + H+
? + NAD+
Substrates: -
Products: -
?
oxaloacetate + NADH + H+
? + NAD+
Substrates: -
Products: -
?
oxamate + NADH
?
-
Substrates: two distinct active site LDH/NADH-oxamate complex conformations, a major populated structure wherein all significant hydrogen-bonding patterns are formed at the active site between protein and bound ligand necessary for the catalytically productive Michaelis complex and, a minor structure in a configuration of the active site that is unfavorable to carry out catalyzed chemistry. This latter structure likely simulates a dead-end complex in the reaction mixture. The evolution of the encounter complex between LDH/NADH and oxamate collapses via a branched reaction pathway to form the major and minor bound species. Once the encounter complex is formed between LDH/NADH and substrate, the ternary protein-ligand complex appears to fold to form a compact productive complex in an all or nothing like fashion with all the important molecular interactions coming together at the same time
Products: -
?
phenylpyruvate + NADH
2-hydroxy-3-phenylpropanoate + NAD+
phenylpyruvate + NADH
phenyllactate + NAD+
phenylpyruvate + NADH + H+
2-hydroxy-3-phenylpropanoate + NAD+
phenylpyruvate + NADH + H+
L-phenyllactate + NAD+
pyruvate + APADH + H+
(S)-lactate + APAD+
Substrates: -
Products: -
r
pyruvate + NADH
?
-
Substrates: -
Products: -
?
pyruvate + NADH
L-lactate + NAD+
pyruvate + NADH + H+
(S)-lactate + NAD+
pyruvate + NADH + H+
L-lactate + NAD+
pyruvate + NADH + H+
lactate + NAD+
pyruvate + NADPH + H+
(S)-lactate + NADP+
pyruvate + NADPH + H+
L-lactate + NADP+
Substrates: -
Products: -
?
pyruvate ethyl ester + NADH
2-hydroxypropanoate ethyl ester
-
Substrates: -
Products: -
?
pyruvate methyl ester + NADH
2-hydroxypropanoate methyl ester
-
Substrates: -
Products: -
?
additional information
?
-
(S)-lactate + 3-acetylpyridine adenine dinucleotide
pyruvate + reduced 3-acetylpyridine adenine dinucleotide
-
Substrates: -
Products: -
r
(S)-lactate + 3-acetylpyridine adenine dinucleotide
pyruvate + reduced 3-acetylpyridine adenine dinucleotide
-
Substrates: -
Products: -
r
(S)-lactate + 3-acetylpyridine adenine dinucleotide
pyruvate + reduced 3-acetylpyridine adenine dinucleotide
Substrates: -
Products: -
?
(S)-lactate + 3-acetylpyridine adenine dinucleotide
pyruvate + reduced 3-acetylpyridine adenine dinucleotide
-
Substrates: -
Products: -
?
(S)-lactate + 3-acetylpyridine adenine dinucleotide
pyruvate + reduced 3-acetylpyridine adenine dinucleotide
-
Substrates: -
Products: -
?
(S)-lactate + 3-acetylpyridine adenine dinucleotide
pyruvate + reduced 3-acetylpyridine adenine dinucleotide
Substrates: -
Products: -
?
(S)-lactate + NAD(P)+
pyruvate + NAD(P)H + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD(P)+
pyruvate + NAD(P)H + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD(P)+
pyruvate + NAD(P)H + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD(P)+
pyruvate + NAD(P)H + H+
-
Substrates: L-lactate transport and metabolism, regulation and localization of enzyme participating in the pathway, overview
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
?
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
?
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: mutant I12V/R81Q/M85E/G210A/V214I, residues I12, R81, M85, G210, and V214 determine the enzyme's substrate specificity
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: wild-type enzyme is specific for NAD+. Mutant enzyme F16Q/I37K/D38SC81S/N85R utilizes NADP+ better than wild-type enzyme, prefers NADP+ to NAD+. Mutant F16Q/C81S/N85R utilizes NAD+ better than wild-type enzyme, weakly active with NADP+
Products: -
?
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: residues I12, R81, M85, G210, and V214 determine the enzyme's substrate specificity
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: the astrocytic cell line CCF-STTG1 is able to consume lactate to generate ATP via oxidative phosphorylation, overview
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: since the mitochondrial metabolism of (S)-lactate results in synthesis and export of oxaloacetate, malate and citrate into the extramitochondrial phase, an anaplerotic role for the mitochondrial (S)-lactate metabolism is proposed
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: the maximal velocity of lactate oxidation is about 10% of pyruvate reduction
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: lactate oxidation does not occur unless pyruvate and especially NADH drop to low levels
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: lactate oxidation does not occur unless pyruvate and especially NADH drop to low levels
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: inactive towards D-lactate
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: LDH is a key enzyme in homolactic fermentation catalyzing the reduction of pyruvate to lactate with the concomitant oxidation of NADH, LDH and LDHB are involved in glycolysis
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: LDH posseses a catalytic His171 residue
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: LDH is a key enzyme in homolactic fermentation catalyzing the reduction of pyruvate to lactate with the concomitant oxidation of NADH, LDH and LDHB are involved in glycolysis
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: LDH posseses a catalytic His171 residue
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: the maximal velocity of lactate oxidation is about 10% of pyruvate reduction
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Molinema dessetae
-
Substrates: pyruvate reduction is the favored reaction
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: involved in glycolysis
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: enzyme activity and electrophoretic pattern of LDH-A4 and malate dehydrogenase, EC 1.1.1.37, compared in relation to heat and urea inactivation, overview
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
?
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: mitochondrial metabolism of L-lactate plays a role in the response of potato to hypoxic stress
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: poor reaction
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
r
(S)-lactate + nicotinamide hypoxanthine dinucleotide
pyruvate + reduced nicotinamide hypoxanthine dinucleotide
-
Substrates: -
Products: -
r
(S)-lactate + nicotinamide hypoxanthine dinucleotide
pyruvate + reduced nicotinamide hypoxanthine dinucleotide
-
Substrates: -
Products: -
r
2-oxobutanoate + NADH + H+
2-hydroxybutyrate + NAD+
-
Substrates: -
Products: -
?
2-oxobutanoate + NADH + H+
2-hydroxybutyrate + NAD+
-
Substrates: -
Products: -
?
2-oxobutyrate + NADH
2-hydroxybutyrate + NAD+
-
Substrates: 107% of the activity with pyruvate
Products: -
?
2-oxobutyrate + NADH
2-hydroxybutyrate + NAD+
-
Substrates: 3% of the activity with pyruvate
Products: -
?
2-oxobutyrate + NADH
2-hydroxybutyrate + NAD+
-
Substrates: -
Products: -
r
2-oxobutyrate + NADH
2-hydroxybutyrate + NAD+
-
Substrates: -
Products: -
?
2-oxobutyrate + NADH
2-hydroxybutyrate + NAD+
-
Substrates: -
Products: -
?
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: 11.5% of the activity with pyruvate
Products: -
?
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: low activity
Products: -
?
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: low activity
Products: -
?
2-oxoglutarate + NADH + H+
2-hydroxyglutarate + NAD+
-
Substrates: 79.6% of the activity with pyruvate
Products: -
?
2-oxoglutarate + NADH + H+
2-hydroxyglutarate + NAD+
Substrates: 14.6% of the activity with pyruvate
Products: -
?
2-oxoglutarate + NADH + H+
2-hydroxyglutarate + NAD+
-
Substrates: -
Products: -
?
2-oxovalerate + NADH + H+
2-hydroxyvalerate + NAD+
-
Substrates: -
Products: -
?
2-oxovalerate + NADH + H+
2-hydroxyvalerate + NAD+
-
Substrates: -
Products: -
?
3-fluoropyruvate + NADH
?
-
Substrates: -
Products: -
?
3-fluoropyruvate + NADH
?
-
Substrates: 33.6% of the activity with pyruvate
Products: -
?
3-fluoropyruvate + NADH
?
-
Substrates: -
Products: -
?
4-hydroxyphenylpyruvate + NADH + H+
L-4-hydroxyphenyllactate + NAD+
Substrates: -
Products: -
?
4-hydroxyphenylpyruvate + NADH + H+
L-4-hydroxyphenyllactate + NAD+
Substrates: 11.1% of the activity with pyruvate
Products: -
?
4-methyl-2-oxopentanoate + NADH
2-hydroxy-4-methylpentanoate + NAD+
-
Substrates: 39% of the activity with pyruvate
Products: -
?
4-methyl-2-oxopentanoate + NADH
2-hydroxy-4-methylpentanoate + NAD+
-
Substrates: -
Products: -
?
ethyl pyruvate + NADH + H+
? + NAD+
Substrates: -
Products: -
?
ethyl pyruvate + NADH + H+
? + NAD+
Substrates: -
Products: -
?
glyoxylate + NADH
glycolate + NAD+
-
Substrates: -
Products: -
?
glyoxylate + NADH
glycolate + NAD+
-
Substrates: -
Products: -
?
glyoxylate + NADH + H+
glycolate + NAD+
-
Substrates: best substrate of isoform LDHL1
Products: -
?
glyoxylate + NADH + H+
glycolate + NAD+
-
Substrates: best substrate of isoform LDHL1
Products: -
?
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
-
Substrates: -
Products: -
?
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
-
Substrates: -
Products: -
?
L-lactate + NAD+
pyruvate + NADH
-
Substrates: -
Products: -
r
L-lactate + NAD+
pyruvate + NADH
-
Substrates: the enzyme plays two important roles in heart metabolism, it catalyzes pyruvate reduction, mainly at the beginning of effort, or during hypoxia, and also catalyzes the oxidation of lactate released into the blood by other tissues, such as skeletal muscle, which would be used as substrate fuel by the heart mainly during steady-state exercise or during recuperation
Products: -
r
L-lactate + NAD+
pyruvate + NADH
-
Substrates: -
Products: -
r
L-lactate + NAD+
pyruvate + NADH
-
Substrates: LDH binds its substrate via the formation of a LDH/NADH-substrate encounter complex through a select-fit mechanism, whereby only a minority population of LDH/NADH is binding-competent, molecular dynamics calculations to explore the variations in structure accessible to the binary complex and binding-competent structures, active site interactions in the ternary complex, overview
Products: -
r
L-lactate + NAD+
pyruvate + NADH
-
Substrates: the enzyme plays two important roles in heart metabolism, it catalyzes pyruvate reduction, mainly at the beginning of effort, or during hypoxia, and also catalyzes the oxidation of lactate released into the blood by other tissues, such as skeletal muscle, which would be used as substrate fuel by the heart mainly during steady-state exercise or during recuperation
Products: -
r
L-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: no activity with D-lactate
Products: -
r
L-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: no activity with D-lactate, activity of recombinant His6-tagged LctD is determined in the presence of the electron carriers 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl-2H-tetrazolium bromide and phenazine methosulfate
Products: -
r
L-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: no activity with D-lactate
Products: -
r
L-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: no activity with D-lactate, activity of recombinant His6-tagged LctD is determined in the presence of the electron carriers 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl-2H-tetrazolium bromide and phenazine methosulfate
Products: -
r
L-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
L-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
L-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: the wild-type V583 strain converts glucose almost exclusively to L-lactate under anaerobic conditions
Products: -
r
L-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
r
L-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
L-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
L-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: amino acid residues involved in substrate and cofactor binding are Arg109, Asp168, Arg171, and His195
Products: -
r
L-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
r
L-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
?
L-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: an encounter complex is formed between LDH-NAD+ and lactate, collapses to form a chemically active species and loop closure/opening steps
Products: -
?
L-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
r
L-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
r
phenylpyruvate + NADH
2-hydroxy-3-phenylpropanoate + NAD+
-
Substrates: 28% of the activity with pyruvate
Products: -
?
phenylpyruvate + NADH
2-hydroxy-3-phenylpropanoate + NAD+
-
Substrates: -
Products: -
?
phenylpyruvate + NADH
phenyllactate + NAD+
-
Substrates: -
Products: -
r
phenylpyruvate + NADH
phenyllactate + NAD+
-
Substrates: -
Products: -
r
phenylpyruvate + NADH + H+
2-hydroxy-3-phenylpropanoate + NAD+
-
Substrates: -
Products: -
?
phenylpyruvate + NADH + H+
2-hydroxy-3-phenylpropanoate + NAD+
-
Substrates: -
Products: -
?
phenylpyruvate + NADH + H+
L-phenyllactate + NAD+
Substrates: -
Products: -
?
phenylpyruvate + NADH + H+
L-phenyllactate + NAD+
Substrates: 47.4% of the activity with pyruvate
Products: -
?
phenylpyruvate + NADH + H+
L-phenyllactate + NAD+
Substrates: low activity
Products: -
?
pyruvate + NADH
L-lactate + NAD+
-
Substrates: lactate yield is increased in the pyruvate decarboxylase 1/alcohol dehydrogenase 1 double mutant compared with that in the single pyruvate decarboxylase 1 mutant
Products: -
?
pyruvate + NADH
L-lactate + NAD+
Substrates: in the cell lysate of the host strain, L-LDH activity is hardly detectable during cultivation. As a consequence of transformation, the ratio between D- and L-isomers is changed due to the increment of L-lactate and the decrement of D-lactate, but there are no significant differences in total lactate concentration between the host and transformant cells. In the transformant harboring pLC18lld, L-LDH activity is detected during the entire cultivation period. L-LDH activity increases rapidly to the maximum level (0.18 U/mg protein) between the early- and mid-exponential growth phases (0-8 h), and decreases thereafter during the stationary phase
Products: -
?
pyruvate + NADH
L-lactate + NAD+
Substrates: LDH1 has an important physiological function, in addition to being a glycolytic enzyme and differentiation marker. The enzymatic activity, growth, and virulence of tachyzoites are unaffected by the presence of the recombinant protein. Overexpression of LDH1 enhances the parasite's ability to differentiate
Products: -
?
pyruvate + NADH
L-lactate + NAD+
Substrates: LDH2 has an important physiological function, in addition to being a glycolytic enzyme and differentiation marker. The enzymatic activity, growth, and virulence of tachyzoites are unaffected by the presence of the recombinant protein. Overexpression of LDH2 enhances the parasite's ability to differentiate
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: LDH catalyzes the conversion of pyruvate to lactate with concomitant oxidation of NADH during the last step in anaerobic glycolysis
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: active site structure and substrate binding, overview
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: LDH catalyzes the conversion of pyruvate to lactate with concomitant oxidation of NADH during the last step in anaerobic glycolysis
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: active site structure and substrate binding, overview
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: study of the dependence of the chemical reaction mechanism of lactate dehydrogenase on the protonation state of titratable residues and on the level of the quantum mechanical description by means of hybrid quantum-mechanical methods
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: the maximal velocity of lactate oxidation is only 10% of pyruvate reduction
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: inactivation of the lshL does not abolish the production of L-lactate, but the lactate final concentration decreases about 25% compared to the wild-type, suggesting the presence of at least a second L-Ldh
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Lactobacillus mesenteroides
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: the maximal velocity of lactate oxidation is only 10% of pyruvate reduction
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Molinema dessetae
-
Substrates: pyruvate reduction is the favored reaction
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: LdhB enzymes from type-I isolate NRRL 395 and type-II isolate 99-880 show reductive LDH activity, but no oxidative LDH activity, overview
Products: -
ir
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: LdhB
Products: -
ir
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: the nitric oxide-inducible lactate dehydrogenase enables Staphylococcus aureus to resist innate immunity, L-lactate production allows Staphylococcus aureus to maintain redox homeostasis during nitrosative stress and is essential for virulence, regulation, overview
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
ir
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Streptococcus mitior
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: D-glyceraldehyde-3-phosphate dehydrogenase and L-lactate dehydrogenase have a functional interaction that can affect NAD+/NADH metabolism and glycolysis in living cells
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: LDH catalyzes the conversion of pyruvate to lactate with concomitant oxidation of NADH during the last step in anaerobic glycolysis
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: active site structure and substrate binding, overview
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: terminal enzyme in aerobic glycolysis necessary for NAD+ regeneration
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
L-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
L-lactate + NAD+
-
Substrates: enzyme activity increases in response to infection by black-rot fungus but decreases in response to cutting
Products: -
?
pyruvate + NADH + H+
L-lactate + NAD+
Substrates: -
Products: -
?
pyruvate + NADH + H+
L-lactate + NAD+
-
Substrates: key enzyme in anaerobic metabolism which converts pyruvate to lactate
Products: -
?
pyruvate + NADH + H+
L-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
L-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
L-lactate + NAD+
-
Substrates: -
Products: -
r
pyruvate + NADH + H+
L-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
L-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
L-lactate + NAD+
-
Substrates: an encounter complex is formed between LDH-NADH and pyruvate, collapses to form a chemically active species and loop closure/opening steps
Products: -
?
pyruvate + NADH + H+
L-lactate + NAD+
-
Substrates: last step in anaerobic glycolysis
Products: -
?
pyruvate + NADH + H+
L-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
L-lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADH + H+
lactate + NAD+
-
Substrates: -
Products: -
?
pyruvate + NADPH + H+
(S)-lactate + NADP+
-
Substrates: 15% of the activity with NADH
Products: -
?
pyruvate + NADPH + H+
(S)-lactate + NADP+
-
Substrates: 20% of the activity with NADH
Products: -
?
pyruvate + NADPH + H+
(S)-lactate + NADP+
-
Substrates: -
Products: -
?
pyruvate + NADPH + H+
(S)-lactate + NADP+
-
Substrates: 34% of the activity with NADH
Products: -
?
additional information
?
-
-
Substrates: -
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
?
additional information
?
-
Substrates: amino acid sequence, structure and kinetic comparison of L-LDH with citrate synthase, EC 2.3.3.1, overview
Products: -
?
additional information
?
-
-
Substrates: amino acid sequence, structure and kinetic comparison of L-LDH with citrate synthase, EC 2.3.3.1, overview
Products: -
?
additional information
?
-
-
Substrates: in addition of lactate dehydrogenase activity, the epsilon-crystallin also possesses the enzymatic activity of malate dehydrogenase
Products: -
?
additional information
?
-
-
Substrates: -
Products: -
?
additional information
?
-
-
Substrates: Bacillus subtilis fermentation pathways, overview
Products: -
?
additional information
?
-
-
Substrates: the enzyme also utilizes NADP(H)
Products: -
?
additional information
?
-
-
Substrates: Bacillus subtilis fermentation pathways, overview
Products: -
?
additional information
?
-
-
Substrates: the enzyme also utilizes NADP(H)
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
?
additional information
?
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Substrates: substrate binding structure, overview. The side chain of the Arg171 residue of LDH-2 seems to be important for the binding of pyruvate, pointing toward the pyruvate-binding site
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Substrates: substrate binding structure, overview. The side chain of the Arg171 residue of LDH-2 seems to be important for the binding of pyruvate, pointing toward the pyruvate-binding site
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Substrates: substrate binding structure, overview. The side chain of the Arg171 residue of LDH-2 seems to be important for the binding of pyruvate, pointing toward the pyruvate-binding site
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Substrates: substrate binding structure, overview. The side chain of the Arg171 residue of LDH-2 seems to be important for the binding of pyruvate, pointing toward the pyruvate-binding site
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Substrates: substrate analogue oxamate is isoelectric and isosteric to pyruvate and has binding kinetics very similar to that of pyruvate. As the substrate approaches the catalytic site, a catalytically key surface loop (residues 98-110) closes over the ligand, bringing residue Arg109 into hydrogen bonding contact with ligand, water leaves the pocket, and the pocket geometry rearranges to allow for favorable interactions between the cofactor and the ligand, which facilitates on-enzyme catalysis
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Substrates: substrate analogue oxamate is isoelectric and isosteric to pyruvate and has binding kinetics very similar to that of pyruvate. As the substrate approaches the catalytic site, a catalytically key surface loop (residues 98-110) closes over the ligand, bringing residue Arg109 into hydrogen bonding contact with ligand, water leaves the pocket, and the pocket geometry rearranges to allow for favorable interactions between the cofactor and the ligand, which facilitates on-enzyme catalysis
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Substrates: LDH is essential for continuous glycolysis necessary for accelerated tumor growth and increased LDH activity occurs already in grade 1 EC carcinomas
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Substrates: amino acid sequence, structure and kinetic comparison of L-LDH with citrate synthase, EC 2.3.3.1, overview
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Substrates: amino acid sequence, structure and kinetic comparison of L-LDH with citrate synthase, EC 2.3.3.1, overview
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Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
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Substrates: -
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Substrates: -
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Substrates: -
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Lactobacillus mesenteroides
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Substrates: -
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Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
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Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
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Substrates: the enzyme is unlikely to catalyze lactate oxidation at an appreciable rate under physiological conditions
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Substrates: intracellular isozyme regulation in relation to pH, overview
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Substrates: intracellular isozyme regulation in relation to pH, overview
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Substrates: intracellular isozyme regulation in relation to pH, overview
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Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
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Substrates: the enzyme is a component of the system regulating the cellular pH and/or controlling the concentration of reducing equivalents in the cytoplasm of leaf cells
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Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
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Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
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Substrates: -
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Substrates: -
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Substrates: -
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Substrates: -
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Substrates: LDH is critically implicated in tumor growth
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Substrates: LDH is critically implicated in tumor growth
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Substrates: -
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Substrates: the formation of lactate in satellite gliocytes is induced by nicotinic cholinergic synapses directly involved in neuron-glial interactions and in controlling the activity of the LDH enzyme system in sympathetic neurons
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Substrates: L-lactate dehydrogenase catalyzes the conversion of pyruvate to L-lactate using NADH as a cofactor
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Substrates: -
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Substrates: Plasmodium falciparum lactate dehydrogenase has L-malate dehydrogenase activity, which plays a role in the tricarboxylic acid cycle
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Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
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Substrates: -
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Substrates: exogenous L-lactate enters mitochondria by a proton-compensated process, is converted to pyruvate, which is exported to the cytoplasm via a non-energy-competent L-lactate-pyruvate shuttle, overview
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Substrates: -
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Substrates: -
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Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
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Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
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Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
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Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
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Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
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Streptococcus mitior
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Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
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Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
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Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
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Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
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Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
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Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
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Substrates: the heart-type isozyme interacts with liposomes made of acidic phospholipids, such as phosphatidylserine or cardiolipin, most effectively at low pH close to the isoelectric point of the isozyme of pH 5.5 strongly involving the enzyme's NADH-cofactor binding site, no interaction with liposomes of the muscle-type isozyme, overview
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Substrates: -
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Substrates: -
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Substrates: L-nLDH shows higher specificity towards pyruvate esters, such as methyl pyruvate and ethyl pyruvate. Very poor activity with 4-methyl-2-oxovalerate
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Substrates: L-nLDH shows higher specificity towards pyruvate esters, such as methyl pyruvate and ethyl pyruvate. Very poor activity with 4-methyl-2-oxovalerate
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Substrates: L-nLDH shows higher specificity towards pyruvate esters, such as methyl pyruvate and ethyl pyruvate. Very poor activity with 4-methyl-2-oxovalerate
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Substrates: -
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