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(2S,3S)-tartrate + NAD+
? + NADH
(S)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
-
oxidized at an extremely slow rate, less than 0.001% of the rate of L-malate oxidation
-
-
r
(S)-malate + 3-acetylnicotinamide-NAD+
oxaloacetate + 3-acetylnicotinamide-NADH + H+
-
-
-
-
r
(S)-malate + 3-acetylpyridine-adenine dinucleotide
oxaloacetate + reduced 3-acetylpyridine-adenine dinucleotide + H+
-
can also use 3-acetylpyridine-adenine as cofactor
-
-
r
(S)-malate + acetylpyridine adenine dinucleotide
oxaloacetate + reduced acetylpyridine adenine dinucleotide
-
-
-
?
(S)-malate + deamino-NAD+
oxaloacetate + deamino-NADH + H+
-
-
-
-
r
(S)-malate + NAD(P)+
oxaloacetate + NAD(P)H
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
(S)-malate + NADP+
oxaloacetate + NADPH + H+
(S)-malate + thionicotinamide-NAD+
oxaloacetate + thionicotinamide-NADH + H+
-
-
-
-
r
1,4,5,6-tetrahydronicotinamide + L-malate
?
-
-
-
-
?
2-oxobutyrate + NADH
2-hydroxybutyrate + NAD+
-
-
-
-
?
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
2-oxoglutarate + NADH + H+
2-hydroxyglutarate + NAD+
about 10% of the activity with oxaloacetate at pH 6.8 and at pH 8.2
-
-
?
3-acetylpyridine adenine dinucleotide + L-malate
?
-
-
-
-
?
3-bromopyruvate + NADH
3-bromo-2-hydroxypropanoate + NAD+
about 10% of the activity with oxaloacetate at pH 6.8
-
-
?
alpha-keto-malonate + NADH
? + NAD+
alpha-ketoisovalerate + NADH
2-hydroxyisovalerate + NAD+
about 10% of the activity with oxaloacetate at pH 8.2
-
-
?
alpha-ketomalonate + NADH
?
-
-
-
?
citrate + NAD+
? + NADH
-
-
-
-
?
hydroxymalonate + NAD+
? + NADH
L-lactate + NAD+
? + NADH
-
cMDH less catalytically efficient than against its natural substrate malate
-
-
?
L-malate + NAD+
oxaloacetate + NADH + H+
L-malate + NADP+
oxaloacetate + NADPH + H+
malate + NAD+
oxaloacetate + NADH + H+
meso-tartrate + NAD+
? + NADH
nicotinamide 1-N6-ethenoadenine dinucleotide + L-malate
?
-
-
-
-
?
nicotinamide hypoxanthine dinucleotide + L-malate
?
-
-
-
-
?
oxaloacetate + NADH
(S)-malate + NAD+
oxaloacetate + NADH
L-malate + NAD+
oxaloacetate + NADH + H+
(2S)-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
oxaloacetate + NADH + H+
L-malate + NAD+
oxaloacetate + NADPH + H+
(S)-malate + NADP+
oxaloglycolate + NAD+
? + NADH
-
-
-
-
r
p-hydroxyphenylpyruvate + NADH + H+
2-hydroxy-3-(4-hydroxyphenyl)propanoate
-
-
-
?
phenylpyruvate + NADH
2-hydroxy-3-phenylpropanoate + NAD+
about 30% of the activity with oxaloacetate at pH 8.2
-
-
?
phenylpyruvate + NADH + H+
2-hydroxy-3-phenylpropanoate + NAD+
-
-
-
?
pyridine 3-aldehyde adenine dinucleotide + L-malate
?
-
-
-
-
?
pyruvate + NAD+
? + NADH
-
cMDH less catalytically efficient than against its natural substrate malate
-
-
?
pyruvate + NADH
2-hydroxypropanoate + NAD+
about 25% of the activity with oxaloacetate at pH 8.2
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
pyruvate + NADH + H+
L-lactate + NAD+
thionicotinamide adenine dinucleotide + L-malate
?
-
-
-
-
?
additional information
?
-
(2S,3S)-tartrate + NAD+
? + NADH
-
-
-
-
r
(2S,3S)-tartrate + NAD+
? + NADH
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
the peroxisomal malate dehydrogenase functions in beta-oxidation, serving to reoxidize NADH, but not in the glyoxylate cycle
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
reversible interconversion of malate and oxaloacetate
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
the reduction of oxaloacetate with NADH is preferred. Malate is oxidized by NAD+ at 10% of the maximal velocity for the reduction of oxaloacetate with NADH. No oxidation of malate with NADP+ as coenzyme
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
286629, 286630, 286633, 286635, 286640, 286641, 286645, 286648, 286653, 286655, 286659, 286661, 286662, 286669, 740926 -
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
Bryophyllum calycinum
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
Citrus sp.
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
the NAD-dependent mitochondrial malate dehydrogenase plays pivotal roles in tricarboxylic acid and is crucial for the survival and pathogenecity of parasites
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
Coccochloris peniocystis
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
Coccochloris peniocystis 1548
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
286629, 286630, 286633, 286635, 286639, 286640, 286641, 286645, 286648, 286655, 286660, 286661, 286662, 286666, 286669, 286672, 286673, 286674, 740926 -
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
residues I12, R81, M85, G210, and V214 determine the enzyme's substrate specificity
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
residues I12, R81, M85, G210, and V214 determine the enzyme's substrate specificity
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
NAD+ binds first to the enzyme and then oxaloacetate is consequently released randomly via an ordered via an ordered bi-bi mechanism
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
malate dehydrogenase is an oligomeric enzyme that catalyzes the reversible oxidation of malate to oxaloacetate in the presence of NAD+, MDH is an essential metabolic enzyme in the citric acid cycle
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
NAD+ binds first to the enzyme and then oxaloacetate is consequently released randomly via an ordered via an ordered bi-bi mechanism
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
malate dehydrogenase is an oligomeric enzyme that catalyzes the reversible oxidation of malate to oxaloacetate in the presence of NAD+, MDH is an essential metabolic enzyme in the citric acid cycle
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
highly specific for oxaloacetate and malate
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
enzyme activity and electrophoretic pattern of MDH and lactate dehydrogenase, EC 1.1.1.27, compared in relation to heat and urea inactivation, overview
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
mitochondrial isozyme Mdh1 preferably catalyzes the oxaloacetate formation, overview
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
the cytoplasmic isozyme Mdh2 catalyzes preferably the malate formation, overview
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
mitochondrial enzyme form mMDH functions in citric acid cycle and in the malate-aspartate shuttle
-
-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
the envelope- and plasma membrane-bound NAD-MDH exhibit the highest affinities for OAA, leaf plasma membrane-bound MDH exhibits a high capacity for both reaction directions (malate oxidation and oxaloacetate reduction), while the two chloroplast isoforms (stromal and envelope-bound) preferentially reduce oxaloacetate
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
1246fold preference for oxaloacetate reduction over L-malate oxidation
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
1246fold preference for oxaloacetate reduction over L-malate oxidation
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
the reverse reaction is highly preferred, with a 1050fold higher kcat/Km value
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
the reverse reaction is highly preferred, with a 1050fold higher kcat/Km value
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
low activity in this direction
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
286626, 286629, 286630, 286632, 286633, 286636, 286637, 286638, 286639, 286640, 286641, 286645, 286646, 286647, 286650, 286651, 286656, 286658, 286660, 286661, 286662, 286664, 286665, 286668, 286672, 286673, 286674, 286675, 711909, 712915, 740359 -
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
mitochondrial enzyme, Krebs cycle
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
Viola sp.
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
-
-
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
-
-
-
ir
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
-
-
-
ir
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
alpha-keto-malonate + NADH
? + NAD+
-
-
-
-
ir
alpha-keto-malonate + NADH
? + NAD+
-
-
-
-
?
alpha-keto-malonate + NADH
? + NAD+
-
-
-
-
?
alpha-keto-malonate + NADH
? + NAD+
-
reduced by m-MDH with half of the turnover number observed with oxaloacetate
-
-
?
hydroxymalonate + NAD+
? + NADH
-
tartronic acid
-
-
r
hydroxymalonate + NAD+
? + NADH
-
-
-
-
?
L-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
L-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
L-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
L-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
L-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
L-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
L-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
L-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
L-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
L-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
L-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
L-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
L-malate + NADP+
oxaloacetate + NADPH + H+
Coccochloris peniocystis
-
-
-
-
r
L-malate + NADP+
oxaloacetate + NADPH + H+
Coccochloris peniocystis 1548
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
286629, 286630, 286633, 286635, 286640, 286641, 286645, 286648, 286653, 286655, 286659, 286661, 286662, 286669 -
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
Bryophyllum calycinum
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
Citrus sp.
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
Coccochloris peniocystis
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
Coccochloris peniocystis 1548
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
286629, 286630, 286633, 286635, 286639, 286640, 286641, 286645, 286648, 286655, 286660, 286661, 286662, 286666, 286669, 286672, 286673, 286674 -
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
?
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
286626, 286629, 286630, 286632, 286633, 286636, 286637, 286638, 286639, 286640, 286641, 286645, 286646, 286647, 286650, 286651, 286656, 286658, 286660, 286661, 286662, 286664, 286665, 286668, 286672, 286673, 286674, 286675 -
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
?
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
Viola sp.
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
?
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
meso-tartrate + NAD+
? + NADH
-
-
-
-
r
meso-tartrate + NAD+
? + NADH
-
-
-
-
r
meso-tartrate + NAD+
? + NADH
-
slightly oxidized, 0.82 of the rate for L-malate oxidation
-
-
r
oxaloacetate + NADH
(S)-malate + NAD+
cytosolic enzyme and glycosomal enzyme
-
-
r
oxaloacetate + NADH
(S)-malate + NAD+
-
-
-
-
?
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
286629, 286630, 286633, 286635, 286640, 286641, 286645, 286648, 286653, 286655, 286659, 286661, 286662, 286669 -
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
Bryophyllum calycinum
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
?
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
Citrus sp.
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
Coccochloris peniocystis
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
Coccochloris peniocystis 1548
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
286629, 286630, 286633, 286635, 286639, 286640, 286641, 286645, 286648, 286655, 286660, 286661, 286662, 286666, 286669, 286672, 286673, 286674 -
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
?
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
?
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
?
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
the ratio of oxaloacetate reduction to malate oxidation is 28.4
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
?
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
ir
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
ir
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
?
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
?
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
?
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
?
oxaloacetate + NADH
L-malate + NAD+
-
-
286626, 286629, 286630, 286632, 286633, 286636, 286637, 286638, 286639, 286640, 286641, 286645, 286646, 286647, 286650, 286651, 286656, 286658, 286660, 286661, 286662, 286664, 286665, 286668, 286672, 286673, 286674, 286675, 656883 -
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
Viola sp.
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
reversible interconversion of malate and oxaloacetate
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
the reduction of oxaloacetate with NADH is preferred. Malate is oxidized by NAD+ at 10% of the maximal velocity for the reduction of oxaloacetate with NADH. Maximal activity with NADPH is 10% compared to the activity with NADH
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
?
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
?
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
?
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
?
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
?
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
?
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
?
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
?
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
?
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
?
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
?
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
?
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
the enzyme is more efficient in the reductive reaction in the tricarboxylic acid cycle
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
oxaloacetate + NADH + H+
L-malate + NAD+
-
-
-
ir
oxaloacetate + NADH + H+
L-malate + NAD+
-
-
-
ir
oxaloacetate + NADH + H+
L-malate + NAD+
-
-
-
ir
oxaloacetate + NADH + H+
L-malate + NAD+
-
-
-
ir
oxaloacetate + NADH + H+
L-malate + NAD+
-
-
-
ir
oxaloacetate + NADH + H+
L-malate + NAD+
-
-
-
ir
oxaloacetate + NADH + H+
L-malate + NAD+
-
-
-
ir
oxaloacetate + NADH + H+
L-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
L-malate + NAD+
best substrate
-
-
r
oxaloacetate + NADH + H+
L-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
L-malate + NAD+
best substrate
-
-
r
oxaloacetate + NADH + H+
L-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
L-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
L-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
L-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
L-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
L-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
L-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
L-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
L-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
L-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
L-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
L-malate + NAD+
-
-
-
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
wild-type enzyme shows no activity with pyruvate. Mutant enzyme R100Q has considerably higher specificity for pyruvate than for oxaloacetate
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
wild-type enzyme shows no activity with pyruvate. Mutant enzyme R100Q has considerably higher specificity for pyruvate than for oxaloacetate
-
-
?
pyruvate + NADH + H+
L-lactate + NAD+
-
-
-
r
pyruvate + NADH + H+
L-lactate + NAD+
-
-
-
r
additional information
?
-
-
PMDH activity is not essential for photosynthesis in air in Arabidopsis
-
-
?
additional information
?
-
-
the enzyme is involved in the tricarboxylic acid cycle supplying organic acids as the main source of carbon but not energy
-
-
?
additional information
?
-
-
the enzyme is involved in the tricarboxylic acid cycle supplying organic acids as the main source of carbon but not energy
-
-
?
additional information
?
-
-
the dimeric 74-kDa isozyme is involved in tricarboxylic acid cycle, while the tetrameric 148-kDa isozyme takes part in the citramalate pathway
-
-
?
additional information
?
-
-
the dimeric 74-kDa isozyme is involved in tricarboxylic acid cycle, while the tetrameric 148-kDa isozyme takes part in the citramalate pathway
-
-
?
additional information
?
-
-
D-malate, (+)-tartrate, succinate and L-aspartate are not oxidized
-
-
?
additional information
?
-
-
determination of intracellular NAD+/NADH ratios
-
-
-
additional information
?
-
determination of intracellular NAD+/NADH ratios
-
-
-
additional information
?
-
-
determination of intracellular NAD+/NADH ratios
-
-
-
additional information
?
-
determination of intracellular NAD+/NADH ratios
-
-
-
additional information
?
-
determination of intracellular NAD+/NADH ratios
-
-
-
additional information
?
-
determination of intracellular NAD+/NADH ratios
-
-
-
additional information
?
-
determination of intracellular NAD+/NADH ratios
-
-
-
additional information
?
-
determination of intracellular NAD+/NADH ratios
-
-
-
additional information
?
-
determination of intracellular NAD+/NADH ratios
-
-
-
additional information
?
-
-
MDH1 stabilizes and transactivates p53 protein by binding to p53-responsive elements in the promotor of downstream genes, MDH1 directly regulates p53-dependent apoptosis upon glucose deprivation
-
-
?
additional information
?
-
Ignicoccus islandicus MalDH recognizes oxaloacetate as main substrate, but it is also able to use pyruvate
-
-
-
additional information
?
-
-
Ignicoccus islandicus MalDH recognizes oxaloacetate as main substrate, but it is also able to use pyruvate
-
-
-
additional information
?
-
Ignicoccus islandicus MalDH recognizes oxaloacetate as main substrate, but it is also able to use pyruvate
-
-
-
additional information
?
-
the recombinant proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
-
-
-
additional information
?
-
the recombinant proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
-
-
-
additional information
?
-
the recombinant proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
-
-
-
additional information
?
-
the recombinant proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
-
-
-
additional information
?
-
the recombinant proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
-
-
-
additional information
?
-
the recombinant proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
-
-
-
additional information
?
-
the recombinant proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
-
-
-
additional information
?
-
the recombinant proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
-
-
-
additional information
?
-
the recombinant proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
-
-
-
additional information
?
-
the recombinant proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
-
-
-
additional information
?
-
the recombinant proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
-
-
-
additional information
?
-
the recombinant proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
-
-
-
additional information
?
-
the enzyme plays a central role in Crassulacean acid metabolism
-
-
?
additional information
?
-
less than 10% of the activity with oxaloacetate with the substrates: alpha-ketobutyrate, alpha-ketoisocaproate, alpha-ketovalerate and alpha-ketomethylvalerate
-
-
?
additional information
?
-
-
the dual specificity for the cofactor results from alanine at position 53 in Methanobacterium jannaschii
-
-
?
additional information
?
-
-
the enzyme is 2fold more active in the reaction of oxaloacetate reduction compared to malate oxidation and exhibiting higher affinity to oxaloacetate than to malate
-
-
?
additional information
?
-
the enzyme displays nearly equal reductive (malate formation) and oxidative (oxaloacetate formation) activities and higher affinity to malate than to oxaloacetate
-
-
?
additional information
?
-
-
the enzyme displays nearly equal reductive (malate formation) and oxidative (oxaloacetate formation) activities and higher affinity to malate than to oxaloacetate
-
-
?
additional information
?
-
the enzyme displays nearly equal reductive (malate formation) and oxidative (oxaloacetate formation) activities and higher affinity to malate than to oxaloacetate
-
-
?
additional information
?
-
-
the enzyme displays nearly equal reductive (malate formation) and oxidative (oxaloacetate formation) activities and higher affinity to malate than to oxaloacetate
-
-
?
additional information
?
-
the PknD phosphorylated MDH can bind to Rv1827 and Rv0020c, i.e. glycogen accumulation regulator GarA and protein Fha, two proteins containing a FHA domain. The FHA domain recognizes phosphothreonine on proteins
-
-
?
additional information
?
-
-
the PknD phosphorylated MDH can bind to Rv1827 and Rv0020c, i.e. glycogen accumulation regulator GarA and protein Fha, two proteins containing a FHA domain. The FHA domain recognizes phosphothreonine on proteins
-
-
?
additional information
?
-
the in vitro conditions to assay the activity of recombinant MDH favors the reduction of oxaloacetate coupled to the oxidation of NADH
-
-
?
additional information
?
-
-
the in vitro conditions to assay the activity of recombinant MDH favors the reduction of oxaloacetate coupled to the oxidation of NADH
-
-
?
additional information
?
-
the PknD phosphorylated MDH can bind to Rv1827 and Rv0020c, i.e. glycogen accumulation regulator GarA and protein Fha, two proteins containing a FHA domain. The FHA domain recognizes phosphothreonine on proteins
-
-
?
additional information
?
-
the in vitro conditions to assay the activity of recombinant MDH favors the reduction of oxaloacetate coupled to the oxidation of NADH
-
-
?
additional information
?
-
-
D-malate, L-tartarate, D-tartarate, hydroxymalonate, dihydroxyfumarate, L-lactate, D-lactate Dl-alpha-hydroxybutyrate, pyruvate, alpha-hydroxypyruvate, alpha-ketoisovalerate and alpha-ketoglutarate are no substrates
-
-
?
additional information
?
-
-
the dimeric isoform of the enzyme is responsible for Krebs cycle function and the tetrameric isoform is involved in functioning of the glyoxylate cycle
-
-
?
additional information
?
-
-
the dimeric isoform of the enzyme is responsible for Krebs cycle function and the tetrameric isoform is involved in functioning of the glyoxylate cycle
-
-
?
additional information
?
-
-
the malate-aspartate NADH shuttle components are metabolic longevity regulators required for calorie restriction-mediated life span extension in yeast, the shuttle plays a major role in the activation of the downstream targets of calorie restriction such as Sir2, mechanism and regulation, detailed overview
-
-
?
additional information
?
-
the malate-aspartate NADH shuttle components are metabolic longevity regulators required for calorie restriction-mediated life span extension in yeast, the shuttle plays a major role in the activation of the downstream targets of calorie restriction such as Sir2, mechanism and regulation, detailed overview
-
-
?
additional information
?
-
-
the recombinant SaMDH may also use NADPH as a cofactor although it is a highly NAD(H)-specific enzyme. No activity with malate and NADP+ as substrates
-
-
?
additional information
?
-
-
the recombinant SaMDH may also use NADPH as a cofactor although it is a highly NAD(H)-specific enzyme. No activity with malate and NADP+ as substrates
-
-
?
additional information
?
-
-
the enzyme has no activity toward NADP+ and NADPH both in vitro and in vivo
-
-
-
additional information
?
-
no substrate: lactate
-
-
?
additional information
?
-
-
no substrate: lactate
-
-
?
additional information
?
-
crystal structures and molecular dynamics simulations of thermophilic malate dehydrogenase reveal critical loop motion for co-substrate binding
-
-
?
additional information
?
-
-
crystal structures and molecular dynamics simulations of thermophilic malate dehydrogenase reveal critical loop motion for co-substrate binding
-
-
?
additional information
?
-
-
the tetrameric MDH enzyme form has a higher affinity for NADH and oxaloacetate, and the dimeric has a higher affinity for NAD+ and malate
-
-
?