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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
-
-
?
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(E)-3-(4-((3R,5R,7R)-adamantan-1-yl)phenoxy)-N-(5-(piperidine-1-carbonyl)-1,4-dihydroindeno[1,2-c]pyrazol-3-yl) acrylamide
-
(NH4)2SO4
reduction of oxaloacetate to malate and oxidation of malate to oxaloacetate
1-(3,5-dichloro-2,6-dihydroxy-4-methoxyphenyl)hexan-1-one
-
i.e. differentiation-inducing factor DIF-1, a morphogen secreted from Dictyostelium discoideum, inhibits proliferation of several cancer cells via suppression of the Wnt/beta -catenin signaling pathway, specifically to mMDH and inhibits its activity, no binding of cytosolic MDH, overview
11-chloro-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
65.3% inhibition at 0.010 mM
2,3-dimethoxy-6-oxo-5,6,7,12-tetrahydroindolo[3,2-d][1]benzazepine-9-carbonitrile
-
89.2% inhibition at 0.010 mM
2,3-dimethoxy-9-(trifluoromethyl)-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
97.7% inhibition at 0.010 mM
2,4-dichlorophenoxybutyric acid
-
-
2-Hydroxy-5-nitrobenzyl bromide
-
-
2-methoxy-1-(3,5-dichloro-2,6-dihydroxy-4-methoxyphenyl)hexan-1-one
-
i.e. differentiation-inducing factor 2-MIDIF-1, a morphogen secreted from Dictyostelium discoideum, inhibits proliferation of several cancer cells via suppression of the Wnt/beta -catenin signaling pathway, binds specifically to mMDH and inhibits its activity, no binding of cytosolic MDH, overview
2-Thenoyltrifluoroacetone
-
3-Aminopyridine adenine dinucleotide
-
-
3-methoxy-9-trifluormethyl-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
83.9% inhibition at 0.010 mM
3-methylpyridine adenine dinucleotide
-
-
3-pyridylacetonitrile adenine dinucleotide
-
-
3-pyridylcarbinol adenine dinucleotide
-
-
4-coumaric acid
-
13.4% inhibition at 0.1 mM
4-methoxy-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
87.6% inhibition at 0.010 mM
5-(3,4-dichlorobenzyl)-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
-
5-(4-methylbenzyl)-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
-
5-benzyl-9-bromo-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
8.6% inhibition at 0.010 mM
5-benzyl-9-chloro-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
-
5-benzyl-9-methoxy-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
-
5-benzyl-9-methyl-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
-
5-benzyl-9-tert-butyl-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
-
5-benzyl-9-trifluoromethyl-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
-
6-oxo-5,6,7,12-tetrahydroindolo[3,2-d][1]benzazepine-9-carbonitrile
-
91.3% inhibition at 0.010 mM
6-oxo-5,6,7,12-tetrahydroindolo[3,2-d][1]benzazepine-9-carboxylic acid
-
98.7% inhibition at 0.010 mM
7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
78.7% inhibition at 0.010 mM
8,10-dichloro-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
28.7% inhibition at 0.010 mM
9-(methylsulfinyl)-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
96.2% inhibition at 0.010 mM
9-(methylthio)-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
76.6% inhibition at 0.010 mM
9-(trifluoromethyl)-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
88.3% inhibition at 0.010 mM
9-bromo-12-(prop-2-en-1-yl)-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
74.1% inhibition at 0.010 mM
9-bromo-12-methyl-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
98.0% inhibition at 0.010 mM
9-bromo-2,3-dimethoxy-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
56.3% inhibition at 0.010 mM
9-bromo-2-methoxy-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
58.7% inhibition at 0.010 mM
9-bromo-3-methoxy-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
15.0% inhibition at 0.010 mM
9-bromo-4-hydroxy-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
25.9% inhibition at 0.010 mM
9-bromo-4-methoxy-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
82.0% inhibition at 0.010 mM
9-bromo-5-(3,4-dichlorobenzyl)-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
-
9-bromo-5-(4-methoxybenzyl)-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
-
9-bromo-5-(4-methylbenzyl)-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
-
9-bromo-5-methyl-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
81.9% inhibition at 0.010 mM
9-bromo-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
74.5% inhibition at 0.010 mM
9-chloro-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
73.4% inhibition at 0.010 mM
9-fluoro-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
46.2% inhibition at 0.010 mM
9-methyl-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
87.8% inhibition at 0.010 mM
9-nitro-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
54.2% inhibition at 0.010 mM
9-tert-butyl-5-(3,4-dichlorobenzyl)-7,12-dihydroindolo[3,2-d][1]benzazepin-6(5H)-one
-
-
adenosine 5'-diphosphoribose
-
-
arsenate
-
uncompetitive inhibition
BaCl2
-
1 mM, 24.9% inhibition
butyl 6-oxo-5,6,7,12-tetrahydroindolo[3,2-d][1]benzazepine-9-carboxylate
-
-
CaCl2
-
1 mM, 29.1% inhibition
CoA
Coccochloris peniocystis
-
-
CoCl2
-
1 mM, 39% inhibition
CuCl2
-
1 mM, 89.8% inhibition
D-fructose 1,6-diphosphate
-
heart s-MDH, inhibits the binding of NADH
Diamide
-
isoforms cy MDH1 and cyMDH2 are reversibly inactivated by diamide treatment. Both NADH and GSH separately or together prevented inactivation of cyMDH1 and cyMDH2 by diamide
EDTA
-
1 mM, 52.2% inhibition
ethyl 6-oxo-5,6,7,12-tetrahydroindolo[3,2-d][1]benzazepine-9-carboxylate
-
-
Fe3+
complete inhibition at 5 mM
ferulic acid
-
24.5% inhibition at 0.1 mM
guanidine hydrochloride
in the presence of 4 M guanidine hydrochloride enzyme structure is unfolded with complete loss of enzyme activity
hexyl 6-oxo-5,6,7,12-tetrahydroindolo[3,2-d][1]benzazepine-9-carboxylate
-
-
HgCl2
-
1 mM, complete inhibition
hydroxylamine
-
1 mM, 57.1% inhibition
isocitrate
reduction of oxaloacetate to malate
methyl 6-oxo-5,6,7,12-tetrahydroindolo[3,2-d][1]benzazepine-9-carboxylate
-
60.9% inhibition at 0.010 mM
MgCl2
-
1 mM,34.9% inhibition
MnCl2
-
1 mM, 28.6% inhibition
NADP+
-
product inhibition; product inhibition, 26% inhibition at 10 mM
NEM
-
1 mM, complete inhibition
NiCl2
-
1 mM, 36.8% inhibition
octyl 6-oxo-5,6,7,12-tetrahydroindolo[3,2-d][1]benzazepine-9-carboxylate
-
-
oxalic acid
-
inhibits L-malate oxidation reaction
p-chloromercuribenzoate
-
-
p-chloromercuriphenylsulfonate
-
-
pentyl 6-oxo-5,6,7,12-tetrahydroindolo[3,2-d][1]benzazepine-9-carboxylate
-
-
Phenylmethanesulfonylfluoride
-
-
propyl 6-oxo-5,6,7,12-tetrahydroindolo[3,2-d][1]benzazepine-9-carboxylate
-
-
pyridine adenine dinucleotide
-
-
Semicarbazide
-
1 mM, 61.3% inhibition
sodium dodecylsulfate
0.1%, 70% loss of activity, 1%, complete loss of activity
succinate
slight inhibition of reduction of oxaloacetate
Urea
-
enzyme activity and electrophoretic pattern of MDH and lactate dehydrogenase, EC 1.1.1.27, compared in relation to heat and urea inactivation, LDH is more sensitive than MDH, overview
ZnCl2
-
1 mM, 72.6% inhibition
(S)-malate
product inhibitor
(S)-malate
substrate inhibition, 60% inhibition at 30 mM
(S)-malate
-
product inhibition, 66% inhibition at 5 mM
(S)-malate
-
24.2% substrate inhibition at 20 mM
2-oxoglutarate
reduction of oxaloacetate to malate and oxidation of malate to oxaloacetate
2-oxoglutarate
-
44% inhibition at 5 mM
acetyl-CoA
Coccochloris peniocystis
-
-
ADP
-
-
alpha-ketoglutarate
-
end-product inhibition
AMP
-
-
ATP
-
-
ATP
Coccochloris peniocystis
-
-
ATP
-
43.7% inhibition at 5 mM
Ca2+
-
-
Ca2+
-
decreases activity under normal and pathological conditions
Ca2+
-
inhibits isoform MDH1 at millimolar concentrations; inhibits isoform MDH2 at millimolar concentrations; inhibits isoform MDH3 at millimolar concentrations
citrate
Coccochloris peniocystis
-
-
citrate
reduction of oxaloacetate to malate
citrate
-
competitive with respect to oxaloacetate
Co2+
-
-
Co2+
36% inhibition at 2 mM
Cu2+
complete inhibition at 5 mM
Cu2+
-
0.01-0.4 mM, activity from ischemic tissue decreases more significantly compared to the control
Cu2+
-
in the presence of 1 mM Cu2+, the enzyme activity decreases to approximately 40% of normal activity
Cu2+
-
25% inhibition at 0.1 mM
Dicarbonate
-
-
Fe2+
-
-
Fe2+
complete inhibition at 2 mM
Hg2+
-
-
Hydroxymalonate
-
-
iodoacetate
-
1 mM, 93.6% inhibition
L-malate
-
inhibition constant: 3.65 mM
L-malate
-
MDH activity is strongly inhibited by excess of L-malate
L-malate
-
product inhibition
Mg2+
-
-
Mn2+
-
-
Mn2+
-
slight inhibition of all isoform MDH2; slight inhibition of isoform MDH1; slight inhibition of isoform MDH3
NAD+
-
-
NAD+
-
MDH activity is inhibited by 0.5 mM NADH
NAD+
-
product inhibition; product inhibition, 29% inhibition at 5 mM, 42% inhibition at 10 mM
NAD+
-
substrate inhibition
NADH
-
substrate inhibition
NADH
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
NADH
substrate inhibition
NADH
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH, over 2 mM
NADH
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
NADH
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH over 1 mM
NADH
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
NADH
-
product inhibition
NADH
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
NADH
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
NADH
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
NADH
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
NADH
-
MDH activity is inhibited by over 200 mM NADH
NADH
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
NADH
-
product inhibition
NADH
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
Ni2+
-
-
oxaloacetate
-
substrate inhibition
oxaloacetate
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
oxaloacetate
substrate inhibition
oxaloacetate
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH, overv 2 mM
oxaloacetate
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
oxaloacetate
substrate inhibition at above 0.3 mM, 37% inhibition at 1 mM
oxaloacetate
Coccochloris peniocystis
-
-
oxaloacetate
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH over 1 mM
oxaloacetate
above 0.025 mM
oxaloacetate
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
oxaloacetate
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
oxaloacetate
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
oxaloacetate
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
oxaloacetate
-
substrate inhibition
oxaloacetate
at high concentrations
oxaloacetate
substrate inhibition
oxaloacetate
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
oxaloacetate
-
substrate inhibition, pH-dependent
oxaloacetate
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH
oxaloacetate
-
MDH activity is inhibited at 0.33 mM
oxaloacetate
-
substrate inhibition
oxaloacetate
substrate inhibition, 50% inhibition at 6 mM
oxaloacetate
-
MDH activity is strongly inhibited by excess of oxaloacetate
oxaloacetate
-
substrate inhibition; substrate inhibition, 29% inhibition at 5 mM
oxaloacetate
-
substrate inhibition
oxaloacetate
-
MDH activity is inhibited by over 250 mM oxaloacetate
oxaloacetate
-
27.4% substrate inhibition at 1 mM
sulfite
-
-
Zn2+
42% inhibition at 5 mM
Zn2+
-
inhibition constant 1.7 mM
Zn2+
73% inhibition at 2 mM
Zn2+
-
25% inhibition at 1 mM
additional information
-
isoform cyMDH3 maintains its low basal activity upon oxidation with 0.5 mM diamide
-
additional information
-
strong decrease in MDH activity under aerobic conditions
-
additional information
-
no effect by NaCl
-
additional information
no substrate inhibition by L-malate up to 20 mM
-
additional information
-
no substrate inhibition by L-malate up to 20 mM
-
additional information
unaffected by excess of L-malate
-
additional information
-
unaffected by excess of L-malate
-
additional information
-
differentiation-inducing factors DIF-3, i.e. 1-(3-chloro-2,6-dihydroxy-4-methoxyphenyl)hexan-1-one, and 6-MIDIF-3, a 6-methoxy isomer of DIF-3, bind spefically to mMDH, but do not inhibit the enzyme activity, no binding of cytosolic MDH
-
additional information
cyMDH is sensitive to cold and salt stresses
-
additional information
-
cyMDH is sensitive to cold and salt stresses
-
additional information
-
the thermostable enzyme is not affected by metal ions (CuCl2, MgCl2, MnCl2, CoCl2, BaCl2, ZnCl2 or CaCl2 and NaCl or KCl) or various organic metabolites (pyruvate, phosphoenolpyruvate, ATP, ADP, AMP, glucose-1-phospate, fructose-1-phosphate, fructose-1,6-bisphosphate, fructose-6-phosphate, ribose-1-phosphate, ribose-5-phosphate (all 5 mM), glycerate, lactate, 2-oxoglutarate, citrate, serine, diphosphate (all 1 mM) or phosphate (10 mM))
-
additional information
the thermostable enzyme is not affected by metal ions (CuCl2, MgCl2, MnCl2, CoCl2, BaCl2, ZnCl2 or CaCl2 and NaCl or KCl) or various organic metabolites (Pyruvate, phosphoenolpyruvate, ATP, ADP, AMP, glucose-1-phospate, fructose-1-phosphate, fructose-1,6-bisphosphate, fructose-6-phosphate, ribose-1-phosphate, ribose-5-phosphate (all 5 mM), glycerate, lactate, 2-oxoglutarate, citrate, serine, pyrophosphate (all 1 mM) or ?H2PO4 (10 mM))
-
additional information
-
the thermostable enzyme is not affected by metal ions (CuCl2, MgCl2, MnCl2, CoCl2, BaCl2, ZnCl2 or CaCl2 and NaCl or KCl) or various organic metabolites (Pyruvate, phosphoenolpyruvate, ATP, ADP, AMP, glucose-1-phospate, fructose-1-phosphate, fructose-1,6-bisphosphate, fructose-6-phosphate, ribose-1-phosphate, ribose-5-phosphate (all 5 mM), glycerate, lactate, 2-oxoglutarate, citrate, serine, pyrophosphate (all 1 mM) or ?H2PO4 (10 mM))
-
additional information
MDH phosphorylation by PknD inhibits the MDH activity by 40%, phosphorylation by other kinases also inhibits the enzyme activity: 42-53% inhibition for PknF, 23-32% inhibition for PknH, and 27-38% inhibition for PknA
-
additional information
-
MDH phosphorylation by PknD inhibits the MDH activity by 40%, phosphorylation by other kinases also inhibits the enzyme activity: 42-53% inhibition for PknF, 23-32% inhibition for PknH, and 27-38% inhibition for PknA
-
additional information
urea cannot induce complete unfolding and inactivation of Pcal_1699 even at a final concentration of 8 M. Not inhibitory: EDTA Triton X-100, TWeen-20, dithiothreitol, glycerol
-
additional information
-
urea cannot induce complete unfolding and inactivation of Pcal_1699 even at a final concentration of 8 M. Not inhibitory: EDTA Triton X-100, TWeen-20, dithiothreitol, glycerol
-
additional information
-
strong decrease in MDH activity under aerobic conditions
-
additional information
MDH is not affected by DTT or EDTA
-
additional information
-
not inhibitory: AMP, ADP, ATP
-
additional information
-
development of 5-benzylpaullones and paullone-9-carboxylic acid alkyl esters as selective inhibitors of mMDH, overview
-
additional information
not inhibitory: praziquantel and albendazole
-
additional information
-
not inhibitory: praziquantel and albendazole
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.089
3-acetylnicotinamide-NAD+
-
-
0.0667
3-acetylpyridine adenine dinucleotide
-
-
0.04955 - 0.1114
3-acetylpyridine-adenine dinucleotide
0.022
acetylpyridine adenine dinucleotide
pH 7.5
5.44
alpha-ketomalonate
pH 7.5
0.178
NADP+
Coccochloris peniocystis
-
-
1.464
nicotinamide 1-N6-ethenoadenine dinucleotide
-
-
0.25
nicotinamide hypoxanthine dinucleotide
-
-
0.0001 - 29.5
oxaloacetate
2.7
p-hydroxyphenylpyruvate
-
0.19
pyridine 3-aldehyde adenine dinucleotide
-
-
0.37
reduced acetylpyridine adenine dinucleotide
pH 10.2
0.132
Thionicotinamide adenine dinucleotide
-
-
0.23
thionicotinamide-NAD+
-
-
additional information
additional information
-
0.00012
(S)-malate
-
pH and temperature not specified in the publication
0.056
(S)-malate
-
pH 9.6, 25°C
0.063
(S)-malate
-
at 0.08-0.18 mM, pH and temperature not specified in the publication
0.1
(S)-malate
pH 8.0, temperature not specified in the publication
0.1
(S)-malate
pH 9.6, 22°C, recombinant enzyme
0.11
(S)-malate
recombinant enzyme, pH 10.0, 30°C
0.12
(S)-malate
-
pH and temperature not specified in the publication
0.177
(S)-malate
-
pH and temperature not specified in the publication
0.19
(S)-malate
pH 7.5, 30°C
0.19
(S)-malate
pH 7.9, 25°C
0.26
(S)-malate
-
pH and temperature not specified in the publication
0.269
(S)-malate
-
20°C, pH 10.0
0.288
(S)-malate
-
30°C, pH 10.0
0.3
(S)-malate
-
pH 8.1, 22°C
0.4
(S)-malate
-
pH and temperature not specified in the publication
0.447
(S)-malate
-
at pH 8.0 and 25°C
0.49
(S)-malate
-
pH and temperature not specified in the publication
0.494
(S)-malate
pH 8.5, 30°C
0.53
(S)-malate
-
pH 9.0, 25°C, dimeric enzyme form
0.543
(S)-malate
-
10°C, pH 10.0
0.55
(S)-malate
-
pH and temperature not specified in the publication
0.555
(S)-malate
-
pH 9.0, 25°C, tetrameric enzyme form
0.56
(S)-malate
pH 7.5, 37°C, mitochondrial enzyme
0.64
(S)-malate
-
recombinant wild type mitochondrial MDH, at 25°C
0.645
(S)-malate
-
pH 9.0, 25°C
0.67
(S)-malate
-
at 0.18-10.0 mM, pH and temperature not specified in the publication
0.74
(S)-malate
-
40°C, pH 10.0
0.94
(S)-malate
-
native wild type mitochondrial MDH, at 25°C
0.95
(S)-malate
-
isoform MDH1, at pH 8.5 and 25°C
1.007
(S)-malate
-
glycosomal isoenzyme
1.04
(S)-malate
recombinant enzyme, pH and temperature not specified in the publication
1.28
(S)-malate
-
recombinant enzyme, pH 9.5, 30°C
1.6
(S)-malate
-
enzyme from cancerous breast tissue, at pH 8.0, temperature not specified in the publication
1.67
(S)-malate
-
pH 9.0, 25°C
1.72
(S)-malate
-
recombinant wild type cytosolic MDH, at 25°C
1.75
(S)-malate
-
isoform MDH3, at pH 8.5 and 25°C
2.2
(S)-malate
-
isoform MDH2, at pH 8.5 and 25°C
2.6
(S)-malate
-
at pH 8.0 and 50°C
2.72
(S)-malate
pH 7.5, 37°C, glycosomal enzyme
3.13
(S)-malate
-
enzyme from normal breast tissue, at pH 8.0, temperature not specified in the publication
3.3
(S)-malate
-
cytosolic isoenzyme
4
(S)-malate
-
pH and temperature not specified in the publication
5
(S)-malate
-
pH and temperature not specified in the publication
9
(S)-malate
-
pH and temperature not specified in the publication
11.6
(S)-malate
-
at pH 8.0 and 25°C
15
(S)-malate
-
mitochondrial isoenzyme
0.04955
3-acetylpyridine-adenine dinucleotide
-
wild type enzyme
0.0962
3-acetylpyridine-adenine dinucleotide
-
mutant enzyme R214G
0.1114
3-acetylpyridine-adenine dinucleotide
-
mutant enzyme R183A
0.014
L-malate
-
fusion protein of MDH with mitochondrial citrate synthase
0.033
L-malate
pH 7.6, native enzyme
0.0341
L-malate
pH 8.2, 30°C
0.047
L-malate
pH 7.6, recombinant enzyme with a poly-His tail
0.054
L-malate
pH 7.6, native enzyme, recombinant protein fusions with glutathione S-transferase
0.069
L-malate
-
0.03-0.1 mM substrate
0.14
L-malate
-
fusion protein of MDH with mitochondrial citrate synthase
0.263
L-malate
-
0.2-10 mM substrate
0.5
L-malate
-
recombinant enzyme, pH 8.0, 80°C
0.8
L-malate
pH 10.5, 20-23°C
1
L-malate
pH 7.4, 30°C, recombinant enzyme
1.25
L-malate
pH 7.4, 30°C, native enzyme
1.33
L-malate
-
mitochondrial MDH
2.068
L-malate
-
pH 6.9, 30°C
2.28
L-malate
-
pH 7.5, 30°C
5.3
L-malate
mutant N122C-L305C(DTT)
5.6
L-malate
Coccochloris peniocystis
-
-
6.8
L-malate
mutant N122C-L305C(diamide)
8
L-malate
-
cytoplasmic isoenzyme
20
L-malate
-
mitochondrial isoenzyme
98.4
L-malate
pH 7.0, 25°C
0.55
malate
-
-
0.00087
NAD+
-
pH and temperature not specified in the publication
0.024
NAD+
Coccochloris peniocystis
-
-
0.024
NAD+
-
pH and temperature not specified in the publication
0.027
NAD+
pH 7.6, native enzyme
0.0279
NAD+
-
10°C, pH 10.0
0.028
NAD+
-
recombinant enzyme, pH 8.0, 80°C
0.0286
NAD+
-
20°C, pH 10.0
0.0299
NAD+
-
30°C, pH 10.0
0.033
NAD+
pH 7.6, recombinant enzyme with a poly-His tail
0.036
NAD+
pH 7.6, recombinant protein fusions with glutathione S-transferase
0.0382
NAD+
-
40°C, pH 10.0
0.042
NAD+
pH 8.0, temperature not specified in the publication
0.042
NAD+
pH 9.6, 22°C, recombinant enzyme
0.06
NAD+
-
isoform MDH1, at pH 8.5 and 25°C
0.069
NAD+
-
cytosolic isoenzyme
0.075
NAD+
-
isoform MDH3, at pH 8.5 and 25°C
0.085
NAD+
-
pH 9.0, 25°C, dimeric enzyme form
0.09
NAD+
-
pH and temperature not specified in the publication
0.094
NAD+
-
pH 9.6, 25°C
0.1
NAD+
-
mitochondrial MDH
0.1
NAD+
-
pH and temperature not specified in the publication
0.11
NAD+
-
fusion protein of MDH with mitochondrial citrate synthase
0.11
NAD+
-
isoform MDH2, at pH 8.5 and 25°C
0.117
NAD+
-
pH and temperature not specified in the publication
0.12
NAD+
pH 7.4, 30°C, native enzyme
0.12
NAD+
native enzyme, at pH 7.4 and 30°C
0.121
NAD+
-
mitochondrial isoenzyme
0.13
NAD+
pH 7.4, 30°C, recombinant enzyme
0.13
NAD+
recombinant enzyme, pH and temperature not specified in the publication
0.13
NAD+
recombinant enzyme, at pH 7.4 and 30°C
0.1338
NAD+
-
pH 7.5, 30°C
0.1397
NAD+
-
pH 6.9, 30°C
0.15
NAD+
-
pH and temperature not specified in the publication
0.161
NAD+
-
pH and temperature not specified in the publication
0.21
NAD+
-
native wild type mitochondrial MDH, at 25°C
0.21
NAD+
-
recombinant wild type cytosolic MDH, at 25°C
0.252
NAD+
-
glycosomal isoenzyme
0.263
NAD+
-
pH 9.0, 25°C
0.27
NAD+
-
pH 9.0, 25°C, tetrameric enzyme form
0.27
NAD+
-
pH and temperature not specified in the publication
0.309
NAD+
-
at pH 8.0 and 25°C
0.33
NAD+
-
recombinant enzyme, pH 9.5, 30°C
0.34
NAD+
-
pH and temperature not specified in the publication
0.37
NAD+
-
recombinant wild type mitochondrial MDH, at 25°C
0.38
NAD+
mutant N122C-L305C(DTT)
0.4
NAD+
pH 10.5, 20-23°C
0.43
NAD+
-
enzyme from normal breast tissue, at pH 8.0, temperature not specified in the publication
0.45
NAD+
recombinant enzyme, pH 10.0, 30°C
0.5
NAD+
mutant N122C-L305C(diamide)
0.58
NAD+
-
at pH 8.0 and 45°C
0.87
NAD+
-
pH and temperature not specified in the publication
0.93
NAD+
-
enzyme from cancerous breast tissue, at pH 8.0, temperature not specified in the publication
1.1
NAD+
-
pH and temperature not specified in the publication
129
NAD+
-
at pH 8.0 and 25°C
0.0014
NADH
-
-
0.0024
NADH
30°C, pH 7.0, wild-type enzyme
0.0041
NADH
-
40°C, pH 5.8
0.007
NADH
-
pH 8.5, 25°C
0.007
NADH
pH 8.0, native enzyme
0.0104
NADH
-
pH 6.9, 30°C
0.012
NADH
pH 8.0, 25°C, recombinant wild-type enzyme and mutant K205A
0.0127
NADH
pH 8.0, recombinant enzyme with a poly-His tai
0.0134
NADH
pH 7.5, 20°C, recombinant cytosolic isoenzyme cMDH-L
0.0134
NADH
isoform r-cMDH-L, at pH 7.5 and 20°C
0.0135
NADH
pH 7.0, 30°C, recombinant enzyme
0.0135
NADH
enzyme from strain 5710, at pH 7.5 and 30°C
0.0136
NADH
-
fusion protein of MDH with mitochondrial citrate synthase
0.014
NADH
-
pH and temperature not specified in the publication
0.0145
NADH
-
pH 7.5, 20°C, mitochondrial isoenzyme mMDH
0.0165
NADH
-
pH and temperature not specified in the publication
0.017
NADH
-
pH 7.5, 30°C
0.017
NADH
-
pH 8.0, 25°C, tetrameric enzyme form
0.0172
NADH
enzyme from strain 2D2, at pH 7.5 and 30°C
0.019
NADH
pH 8.0, recombinant protein fusions with glutathione S-transferase
0.0205
NADH
-
pH 7.5, 20°C, cytosolic isoenzyme cMDH
0.0207
NADH
pH 7.5, 20°C, recombinant cytosolic isoenzyme cMDH-S
0.0207
NADH
isoform r-cMDH-S, at pH 7.5 and 20°C
0.0214
NADH
pH 7.5, 20°C, cytosolic isoenzyme cMDH-S
0.0214
NADH
isoform cMDH-S, at pH 7.5 and 20°C
0.022
NADH
-
pH and temperature not specified in the publication
0.023
NADH
-
pH 8.0, 25°C, dimeric enzyme form
0.024
NADH
-
60°C, pH 8.0
0.024
NADH
-
pH and temperature not specified in the publication
0.024
NADH
pH 8.0, 65°C, at 0.4 mM oxaloacetate
0.0244
NADH
pH 7.5, 20°C, mitochondrial isoenzyme mMDH
0.0244
NADH
isoform r-mMDH, at pH 7.5 and 20°C
0.025
NADH
pH 7.4, 30°C, native enzyme
0.025
NADH
-
pH 7.5, temperature not specified in the publication, native enzyme
0.025
NADH
native enzyme, at pH 7.4 and 30°C
0.0252
NADH
recombinant enzyme, pH 10.0, 30°C
0.026
NADH
-
recombinant wild type cytosolic MDH, at 25°C
0.0266
NADH
-
pH 7.8, 25°C
0.028
NADH
-
60°C, pH 8.0
0.029
NADH
pH 7.4, 30°C, recombinant enzyme
0.029
NADH
-
pH 7.5, temperature not specified in the publication, recombinant enzyme
0.029
NADH
recombinant enzyme, at pH 7.4 and 30°C
0.03
NADH
-
whole cell MDH
0.03
NADH
-
pH and temperature not specified in the publication
0.03
NADH
-
at pH 6.5 and 45°C
0.036
NADH
glycosomal enzyme
0.036
NADH
-
pH and temperature not specified in the publication
0.0376
NADH
-
recombinant enzyme, pH 9.5, 30°C
0.0381
NADH
-
intact chloroplast enzyme fraction
0.04
NADH
-
mitochondrial MDH
0.041
NADH
-
mitochondrial isoenzyme
0.041
NADH
pH 8.0, 20-23°C
0.042
NADH
-
pH 7.8, 25°C
0.0434
NADH
-
chloroplast envelope enzyme fraction
0.05
NADH
oxidized isoform cytMDH1, at pH 7.5 and 25°C
0.052
NADH
mutant N122C-L305C(diamide)
0.054
NADH
pH 7.5, 37°C, glycosomal enzyme
0.056
NADH
mutant N122C-L305C(DTT)
0.057
NADH
cytosolic isoenzyme
0.061
NADH
-
glycosomal isoenzyme
0.065
NADH
-
pH and temperature not specified in the publication
0.065
NADH
-
isoform MDH2, at pH 8.5 and 25°C
0.066
NADH
-
cytosolic isoenzyme
0.07
NADH
pH 6.5, 20-23°C
0.072
NADH
reduced isoform cytMDH1, at pH 7.5 and 25°C
0.07238
NADH
-
wild type enzyme
0.0729
NADH
-
broken chloroplast enzyme fraction
0.0739
NADH
-
plasma membrane-bound enzyme fraction
0.075
NADH
-
ischemic rats
0.078
NADH
-
soluble enzyme fraction
0.08
NADH
recombinant enzyme, pH and temperature not specified in the publication
0.083
NADH
-
pH and temperature not specified in the publication
0.085
NADH
pH 7.5, 37°C, glycosomal enzyme
0.085
NADH
-
pH and temperature not specified in the publication
0.085
NADH
-
isoform MDH3, at pH 8.5 and 25°C
0.086
NADH
-
pH 8.0, 80°C
0.086
NADH
-
recombinant enzyme, pH 8.0, 80°C
0.086
NADH
-
recombinant wild type mitochondrial MDH, at 25°C
0.09
NADH
-
pH and temperature not specified in the publication
0.1172
NADH
-
chloroplast stroma enzyme fraction
0.1197
NADH
-
mutant enzyme R214G
0.123
NADH
at pH 7.0, temperature not specified in the publication
0.1231
NADH
-
mutant enzyme R183A
0.141
NADH
-
at pH 8.0 and 25°C
0.167
NADH
pH 8.0, temperature not specified in the publication
0.167
NADH
pH 8.0, 22°C, recombinant enzyme
0.192
NADH
-
cytosolic MDH
0.21
NADH
-
native wild type mitochondrial MDH, at 25°C
0.25
NADH
-
isoform MDH1, at pH 8.5 and 25°C
0.32
NADH
glacosomal enzyme
0.33
NADH
-
at pH 8.0 and 25°C
0.431
NADH
pH 7.5, 30°C, recombinant enzyme
0.0426
NADPH
30°C, pH 7.0, wild-type enzyme
0.165
NADPH
at pH 7.0, temperature not specified in the publication
0.25
NADPH
pH 6.5, 20-23°C
0.0001
oxaloacetate
-
pH and temperature not specified in the publication with NAD+
0.003
oxaloacetate
30°C, pH 7.0, wild-type enzyme, cofactor NADH
0.004
oxaloacetate
pH 8.0, native enzyme
0.006
oxaloacetate
-
30°C
0.0076
oxaloacetate
-
chloroplast envelope enzyme fraction
0.0081
oxaloacetate
-
plasma membrane-bound enzyme fraction
0.0083
oxaloacetate
-
pH 7.5, 20°C, cytosolic isoenzyme cMDH
0.0088
oxaloacetate
pH 6.8, 30°C
0.0094
oxaloacetate
-
fusion protein of MDH with mitochondrial citrate synthase
0.0096
oxaloacetate
-
pH 8.5, 25°C
0.0113
oxaloacetate
pH 7.5, 20°C, recombinant cytosolic isoenzyme cMDH-L
0.0113
oxaloacetate
isoform cMDH-S, at pH 7.5 and 20°C
0.012
oxaloacetate
-
at pH 6.5 and 50°C
0.0121
oxaloacetate
-
chloroplast stroma enzyme fraction
0.013
oxaloacetate
pH 8.0, recombinant protein fusions with glutathione S-transferase
0.0133
oxaloacetate
-
intact chloroplast enzyme fraction
0.0135
oxaloacetate
pH 7.5, 20°C, mitochondrial isoenzyme mMDH
0.0135
oxaloacetate
isoform r-cMDH-L, at pH 7.5 and 20°C
0.014
oxaloacetate
-
37°C
0.015
oxaloacetate
-
pH 8.0, 80°C
0.015
oxaloacetate
glycosomal enzyme
0.015
oxaloacetate
-
recombinant enzyme, pH 8.0, 80°C
0.0151
oxaloacetate
-
isoform B2, at 20°C
0.0162
oxaloacetate
-
Tv 10-02
0.018
oxaloacetate
pH 8.0, recombinant enzyme with a poly-His tail
0.0189
oxaloacetate
-
pH and temperature not specified in the publication
0.02
oxaloacetate
-
Tv-1961
0.02
oxaloacetate
pH 7.4, 30°C, native enzyme
0.02
oxaloacetate
-
pH and temperature not specified in the publication
0.02
oxaloacetate
-
pH 8.1, 22°C
0.02
oxaloacetate
native enzyme, at pH 7.4 and 30°C
0.022
oxaloacetate
pH 7.4, 30°C, recombinant enzyme
0.022
oxaloacetate
-
pH 8.0, 25°C, tetrameric enzyme form
0.022
oxaloacetate
-
recombinant wild type mitochondrial MDH, at 25°C
0.022
oxaloacetate
-
pH and temperature not specified in the publication
0.022
oxaloacetate
recombinant enzyme, at pH 7.4 and 30°C
0.023
oxaloacetate
-
m-MDH
0.024
oxaloacetate
-
20°C, isoenzyme B
0.024
oxaloacetate
-
isoform B1, at 20°C
0.025
oxaloacetate
pH 6.5, 20-23°C
0.026
oxaloacetate
-
10°C
0.027
oxaloacetate
-
cytosolic isoenzyme
0.03
oxaloacetate
-
cytoplasmic isoenzyme
0.03
oxaloacetate
-
pH 8.0, 25°C, dimeric enzyme form
0.03
oxaloacetate
-
pH and temperature not specified in the publication
0.0302
oxaloacetate
pH 7.5, 20°C, cytosolic isoenzyme cMDH-S
0.0302
oxaloacetate
isoform r-mMDH, at pH 7.5 and 20°C
0.031
oxaloacetate
cytosolic isoenzyme
0.032
oxaloacetate
-
pH and temperature not specified in the publication
0.034
oxaloacetate
-
s-MDH
0.0348
oxaloacetate
-
pH 7.5, 20°C, mitochondrial isoenzyme mMDH
0.035
oxaloacetate
-
native wild type mitochondrial MDH, at 25°C
0.035
oxaloacetate
-
isoform MDH2, at pH 8.5 and 25°C
0.036
oxaloacetate
-
in 50 mM Tris-HCl buffer (pH 7.6), 1 mM MgCl2
0.0368
oxaloacetate
at pH 8.1 and 30°C
0.039
oxaloacetate
pH 7.5, 20°C, recombinant cytosolic isoenzyme cMDH-S
0.039
oxaloacetate
isoform r-cMDH-S, at pH 7.5 and 20°C
0.0391
oxaloacetate
-
pH 6.9, 30°C
0.04
oxaloacetate
-
cytoplasmic enzyme
0.04
oxaloacetate
-
normal rats
0.04
oxaloacetate
pH 7.5, 30°C,recombinant wild-type enzyme
0.041
oxaloacetate
-
in 50 mM Tris-HCl buffer (pH 7.6), 1 mM MgCl2
0.043
oxaloacetate
-
Tv-1973
0.043
oxaloacetate
-
pH and temperature not specified in the publication
0.043
oxaloacetate
pH 8.0, 65°C, at 0.4 mM NADH
0.044
oxaloacetate
mutant L305C
0.044
oxaloacetate
pH 8.0, temperature not specified in the publication
0.044
oxaloacetate
pH 8.0, 22°C, recombinant enzyme
0.0449
oxaloacetate
pH 8.2, 30°C
0.0459
oxaloacetate
-
broken chloroplast enzyme fraction
0.047
oxaloacetate
-
mitochondrial enzyme
0.0476
oxaloacetate
-
pH 7.8, 25°C
0.049
oxaloacetate
wild-type
0.04954
oxaloacetate
-
wild type enzyme
0.05
oxaloacetate
-
ischemic rats
0.05
oxaloacetate
-
pH and temperature not specified in the publication
0.0502
oxaloacetate
-
soluble enzyme fraction
0.052
oxaloacetate
-
40°C, pH 5.8
0.052
oxaloacetate
-
isoform MDH3, at pH 8.5 and 25°C
0.053
oxaloacetate
-
pH 7.8, 25°C
0.056
oxaloacetate
-
37°C
0.056
oxaloacetate
-
mitochondrial isoenzyme
0.057
oxaloacetate
pH 8.0, 20-23°C
0.057
oxaloacetate
-
glycosomal isoenzyme
0.059
oxaloacetate
-
recombinant enzyme, pH 9.5, 30°C
0.06
oxaloacetate
-
s-MDH
0.06186
oxaloacetate
-
mutant enzyme R214G
0.0643
oxaloacetate
-
pH 6.8
0.069
oxaloacetate
glycosomal enzyme
0.072
oxaloacetate
-
pH and temperature not specified in the publication
0.074
oxaloacetate
-
m-MDH
0.08074
oxaloacetate
-
mutant enzyme R183A
0.081
oxaloacetate
-
in 50 mM Tris-HCl buffer (pH 7.6), 1 mM MgCl2
0.083
oxaloacetate
-
mitochondrial MDH
0.09
oxaloacetate
-
cyt MDH
0.111
oxaloacetate
-
pH 7.5, 30°C
0.126
oxaloacetate
-
pH 7.5, temperature not specified in the publication, native enzyme
0.128
oxaloacetate
-
pH and temperature not specified in the publication
0.13
oxaloacetate
pH 8.0, 25°C, recombinant wild-type enzyme and mutant K205A
0.14
oxaloacetate
recombinant enzyme, pH and temperature not specified in the publication
0.143
oxaloacetate
oxidized isoform cytMDH1, at pH 7.5 and 25°C
0.176
oxaloacetate
-
recombinant wild type cytosolic MDH, at 25°C
0.189
oxaloacetate
pH 8.5, 30°C
0.2
oxaloacetate
pH 9.5, 20-23°C
0.2
oxaloacetate
-
isoform MDH1, at pH 8.5 and 25°C
0.23
oxaloacetate
pH 10, 55°C
0.238
oxaloacetate
reduced isoform cytMDH1, at pH 7.5 and 25°C
0.26
oxaloacetate
-
at pH 8.0 and 25°C
0.27
oxaloacetate
-
mitochondrial MDH
0.276
oxaloacetate
-
at pH 8.0 and 25°C
0.287
oxaloacetate
-
pH 7.5
0.289
oxaloacetate
-
pH 7.5, temperature not specified in the publication, recombinant enzyme
0.324
oxaloacetate
pH 7.5, 30°C, recombinant enzyme
0.34
oxaloacetate
mutant N122C-L305C(DTT)
0.34
oxaloacetate
recombinant enzyme, pH 10.0, 30°C
0.38
oxaloacetate
pH 7.0, 70°C
0.405
oxaloacetate
pH 7.8, 30°C
0.55
oxaloacetate
pH 6.5, 20.23°C
0.58
oxaloacetate
mutant N122C-L305C(diamide)
0.7
oxaloacetate
pH 7.0, temperature not specified in the publication, 4 M NaCl, wild-type enzyme
0.74
oxaloacetate
30°C, pH 7.0, wild-type enzyme, cofactor NADPH
0.9
oxaloacetate
pH 7.0, temperature not specified in the publication, 2 M NaCl, wild-type enzyme
3
oxaloacetate
pH 7.5, 30°C, recombinant mutant R81Q
21.8
oxaloacetate
pH 7.0, temperature not specified in the publication, 4 M NaCl, mutant enzyme R100Q
29.4
oxaloacetate
pH 7.0, temperature not specified in the publication, 2 M NaCl, mutant enzyme R100Q
29.5
oxaloacetate
pH 6.0, 25°C
2.2
pyruvate
pH 7.0, temperature not specified in the publication, 0.15 M NaCl, mutant enzyme R100Q
2.2
pyruvate
pH 7.0, temperature not specified in the publication, 2 M NaCl, mutant enzyme R100Q
2.9
pyruvate
pH 7.0, temperature not specified in the publication, 4 M NaCl, mutant enzyme R100Q
additional information
additional information
-
-
additional information
additional information
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-
-
additional information
additional information
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-
additional information
additional information
-
-
-
additional information
additional information
-
-
additional information
additional information
-
-
-
additional information
additional information
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
the enzyme displays a strong KCl-concentration dependent variation in KM-value for oxaloacetate, but not for NADH
-
additional information
additional information
-
the enzyme displays a strong KCl-concentration dependent variation in KM-value for oxaloacetate, but not for NADH
-
additional information
additional information
-
activity kinetics of the native and recombinant proteins are identical
-
additional information
additional information
pH-dependent kinetic mechanism for cMDH, and kinetic modelling for cMDH-catalyzed oxidation of L-malate, detailed overview
-
additional information
additional information
pH-dependent kinetic mechanism for mMDH, and kinetic modelling for mMDH-catalyzed oxidation of L-malate, detailed overview
-
additional information
additional information
Michaelis-Menten and allosteric sigmoidal kinetics
-
additional information
additional information
-
Michaelis-Menten and allosteric sigmoidal kinetics
-
additional information
additional information
recombinant L-MDH displays a typical Michaelis-Menten kinetic profile for both substrates
-
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evolution
-
the plasma membrane-associated isozyme belongs belongs to the lactate dehydrogenase/MDH superfamily, MDH type 2 family
evolution
the three different enzyme forms in cytosol, peroxisome and mitochondrion are encoded by three different genes in Saccharomyces cerevisiae, but by only two genes in Yarrowia lipolytica, where the second gene is differentiated into cytosolic and peroxisomal isozymes by alternative splicing, overview
evolution
Arabidopsis thaliana contains 10 MDHs with only one single copy of MDH gene in the chloroplast, which is a plastidlocalized NAD-dependent MDH
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus. The other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
the enzyme belongs to the MalDH/LDH superfamily, which is divided into several phylogenetically related groups, lactate dehydrogenases (LDHs) and malate dehydrogenases (MalDHs) belong to a wide group of 2-oxoacid:NAD(P)-dependent dehydrogenases that catalyze the reversible conversion of 2-hydroxyacids to the corresponding 2-oxoacids, evolutionary history of the LDHs and MalDHs, overview. The enzyme structure belongs to the NAD(P)-binding Rossmann-like domain CATH superfamily
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
-
evolution
-
the plasma membrane-associated isozyme belongs belongs to the lactate dehydrogenase/MDH superfamily, MDH type 2 family
-
evolution
-
the enzyme belongs to the MalDH/LDH superfamily, which is divided into several phylogenetically related groups, lactate dehydrogenases (LDHs) and malate dehydrogenases (MalDHs) belong to a wide group of 2-oxoacid:NAD(P)-dependent dehydrogenases that catalyze the reversible conversion of 2-hydroxyacids to the corresponding 2-oxoacids, evolutionary history of the LDHs and MalDHs, overview. The enzyme structure belongs to the NAD(P)-binding Rossmann-like domain CATH superfamily
-
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
-
malfunction
absence of either the peroxisomal or the cytosolic form of the MDH does not affect growth rate, irrespective of the carbon source
malfunction
-
exposure of maize plants to excess concentrations of Zn2+ and Cu2+ in the hydroponic solution inhibited lateral root growth, decreased malate dehydrogenase activity and changed isoform profiles
malfunction
-
knockdown of MDH1 in young human dermal fibroblasts and the IMR90 human fibroblast cell line results in the appearance of significant cellular senescence features, including senescence-associated beta-galactosidase staining, flattened and enlarged morphology, increased population doubling time, and elevated p16INK4A and p21CIP1 protein levels. The NAD/NADH ratio is decreased by 90% in MDH1 knockdown dermal fibroblasts but only by about 30% in MDH2 knockdown dermal fibroblasts
malfunction
a pdnad-mdh null mutation is embryo lethal. Plants with reduced pdNAD-MDH levels by means of artificial microRNA (miR-mdh-1) are viable, but dark metabolism is altered as reflected by increased nighttime malate, starch, and glutathione levels and a reduced respiration rate. pdNAD-MDH Silencing Results in small and pale green plants, phenotype, overvew. In addition, miR-mdh-1 plants exhibit strong pleiotropic effects, including dwarfism, reductions in chlorophyll levels, photosynthetic rate, and daytime carbohydrate levels, and disordered chloroplast ultrastructure, particularly in developing leaves, compared with the wild type. pdNAD-MDH deficiency in miR-mdh-1 can be functionally complemented by expression of a microRNA-insensitive pdNAD-MDH but not NADP-MDH, confirming distinct roles for NAD- and NADP-linked redox homeostasis
malfunction
-
Arabidopsis enzyme knockout mutants are embryo-lethal, and a line with lowered enzyme from gene silencing has poor growth, pale leaves, disorganized chloroplasts, and low nighttime respiration
malfunction
-
Arabidopsis mutants lacking the enzyme are embryo-lethal, and constitutive silencing causes a pale, dwarfed phenotype
malfunction
-
in a flo16 knockout mutant, the transition from sucrose to starch is partially disrupted during mutant grain filling
malfunction
in glucose minimal medium, the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR. Ndh, Mdh and LdhA together cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
malfunction
-
in glucose minimal medium, the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR. Ndh, Mdh and LdhA together cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
-
malfunction
-
in glucose minimal medium, the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR. Ndh, Mdh and LdhA together cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
-
malfunction
-
in glucose minimal medium, the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR. Ndh, Mdh and LdhA together cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
-
malfunction
-
in glucose minimal medium, the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR. Ndh, Mdh and LdhA together cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
-
malfunction
-
in glucose minimal medium, the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR. Ndh, Mdh and LdhA together cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
-
malfunction
-
exposure of maize plants to excess concentrations of Zn2+ and Cu2+ in the hydroponic solution inhibited lateral root growth, decreased malate dehydrogenase activity and changed isoform profiles
-
malfunction
-
in glucose minimal medium, the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR. Ndh, Mdh and LdhA together cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
-
metabolism
malate dehydrogenase utilizes NAD/NADH as coenzyme to reversibly catalyze the oxidation/reduction of the malate/oxaloacetate. The mitochondrial isoenzyme (mMDH) catalyzes the oxidation of malate, and is the last step of the citric acid cycle, while the cytoplasmic isoenzyme (cMDH) primarily reduces oxaloacetate in the cytoplasm
metabolism
malate dehydrogenase utilizes NAD/NADH as coenzyme to reversibly catalyze the oxidation/reduction of the malate/oxaloacetate. The mitochondrial isoenzyme (mMDH) catalyzes the oxidation of malate, and is the last step of the citric acid cycle, while the cytoplasmic isoenzyme (cMDH) primarily reduces oxaloacetate in the cytoplasm
metabolism
-
the enzyme is involved in the Krebs cycle (catabolism), glyoxylate and Hatch-Slack cycles, and malate metabolism, as well as other anabolic processes
metabolism
-
the enzyme plays crucial roles in many metabolic pathways, including the tricarboxylic acid (TCA) cycle, energy generation and the formation of metabolites for biosynthesis
metabolism
the enzyme plays crucial roles in many metabolic pathways, including the tricarboxylic acid (TCA) cycle, energy generation and the formation of metabolites for biosynthesis
metabolism
-
isoform MDH1 generates malate with carbons derived from glutamine, thus enabling utilization of glucose carbons for glycolysis and for biomass
metabolism
-
isoform MDH3 is an essential component of the gluconeogenesis pathway that generates glucose from noncarbohydrate carbon substrates and is involved in the reoxidation of NADH produced by fatty-acid beta-oxidation in glyoxysomes
metabolism
-
the enzyme gene FLO16 plays a critical role in redox homeostasis that is important for compound starch grain formation and subsequent starch biosynthesis in rice endosperm
metabolism
the enzyme is more efficient in the reductive reaction in the tricarboxylic acid cycle
metabolism
the enzyme is more efficient in the reductive reaction in the tricarboxylic acid cycle
metabolism
the enzyme is more efficient in the reductive reaction in the tricarboxylic acid cycle
metabolism
the enzyme is more efficient in the reductive reaction in the tricarboxylic acid cycle
metabolism
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
metabolism
the oxidation of NADH with the concomitant reduction of a quinone is a crucial step in the metabolism of respiring cells. Relevance of three different NADH oxidation systems in the actinobacterial model organism Corynebacterium glutamicum: non-proton-pumping NADH dehydrogenase (Ndh), and NADH-oxidizing enzymes, L-lactate dehydrogenase (LdhA) and malate dehydrogenase (Mdh)
metabolism
when the competent catalytic state is reached, LDH catalyzes the direct transfer of a hydride ion from the pro-R face of NADH to the C2 carbon of pyruvate to produce lactate, whereas MalDH transforms oxaloacetate into malate
metabolism
-
the oxidation of NADH with the concomitant reduction of a quinone is a crucial step in the metabolism of respiring cells. Relevance of three different NADH oxidation systems in the actinobacterial model organism Corynebacterium glutamicum: non-proton-pumping NADH dehydrogenase (Ndh), and NADH-oxidizing enzymes, L-lactate dehydrogenase (LdhA) and malate dehydrogenase (Mdh)
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
the oxidation of NADH with the concomitant reduction of a quinone is a crucial step in the metabolism of respiring cells. Relevance of three different NADH oxidation systems in the actinobacterial model organism Corynebacterium glutamicum: non-proton-pumping NADH dehydrogenase (Ndh), and NADH-oxidizing enzymes, L-lactate dehydrogenase (LdhA) and malate dehydrogenase (Mdh)
-
metabolism
-
the oxidation of NADH with the concomitant reduction of a quinone is a crucial step in the metabolism of respiring cells. Relevance of three different NADH oxidation systems in the actinobacterial model organism Corynebacterium glutamicum: non-proton-pumping NADH dehydrogenase (Ndh), and NADH-oxidizing enzymes, L-lactate dehydrogenase (LdhA) and malate dehydrogenase (Mdh)
-
metabolism
-
when the competent catalytic state is reached, LDH catalyzes the direct transfer of a hydride ion from the pro-R face of NADH to the C2 carbon of pyruvate to produce lactate, whereas MalDH transforms oxaloacetate into malate
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
the oxidation of NADH with the concomitant reduction of a quinone is a crucial step in the metabolism of respiring cells. Relevance of three different NADH oxidation systems in the actinobacterial model organism Corynebacterium glutamicum: non-proton-pumping NADH dehydrogenase (Ndh), and NADH-oxidizing enzymes, L-lactate dehydrogenase (LdhA) and malate dehydrogenase (Mdh)
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
the enzyme plays crucial roles in many metabolic pathways, including the tricarboxylic acid (TCA) cycle, energy generation and the formation of metabolites for biosynthesis
-
metabolism
-
the oxidation of NADH with the concomitant reduction of a quinone is a crucial step in the metabolism of respiring cells. Relevance of three different NADH oxidation systems in the actinobacterial model organism Corynebacterium glutamicum: non-proton-pumping NADH dehydrogenase (Ndh), and NADH-oxidizing enzymes, L-lactate dehydrogenase (LdhA) and malate dehydrogenase (Mdh)
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
the oxidation of NADH with the concomitant reduction of a quinone is a crucial step in the metabolism of respiring cells. Relevance of three different NADH oxidation systems in the actinobacterial model organism Corynebacterium glutamicum: non-proton-pumping NADH dehydrogenase (Ndh), and NADH-oxidizing enzymes, L-lactate dehydrogenase (LdhA) and malate dehydrogenase (Mdh)
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physiological function
cyMDH is an enzyme crucial for malate synthesis in the cytosol. Involvement of MdcyMDH directly in malate synthesis and indirectly in malate accumulation through the regulation of genes/enzymes associated with malate degradation and transportation, gluconeogenesis and the tricarboxylic acid cycle.
physiological function
cyMDH is an enzyme crucial for malic acid synthesis in the cytosol. Role of the apple cyMDH gene in growth and tolerance to cold and salt stresses. cyMDH was sensitive to cold and salt stresses. cyMDH overexpression favourably contributes to cell and plant growth and confers stress tolerance in the apple
physiological function
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MDH is an essential enzyme in the tricarboxylic acid cycle. Inhibition of mMDH activity affects cell energy production, probably leading to the inhibition of proliferation. Inhibition of mMDH activity by DIF-1 and 2-MIDIF-1 can be one of the mechanisms to induce anti-proliferative effects, independent of the inhibition of the Wnt/beta-catenin signaling pathway
physiological function
mitochondrial and cytosolic MDH isozymes are required for maintaining the balance of NAD+ and NADH in mitochondria and cytosol
physiological function
mMDH has a role in maximizing photorespiratory rate. The slow-growing mmdh1mmdh2 mutant has elevated leaf respiration rate in the dark and light, without loss of photosynthetic capacity, suggesting that mMDH normally uses NADH to reduce oxaloacetate to malate, which is then exported to the cytosol, rather than to drive mitochondrial respiration. Increased respiratory rate in leaves can account in part for the low net CO2 assimilation and slow growth rate of mmdh1mmdh2. Loss of mMDH also affects photorespiration with alterations in CO2 assimilation/intercellular CO2 at low CO2, and the light-dependent elevated concentration of photorespiratory metabolites
physiological function
mMDH has a role in maximizing the photorespiratory rate. The slow-growing mmdh1mmdh2 mutant has elevated leaf respiration rate in the dark and light, without loss of photosynthetic capacity, suggesting that mMDH normally uses NADH to reduce oxaloacetate to malate, which is then exported to the cytosol, rather than to drive mitochondrial respiration. Increased respiratory rate in leaves can account in part for the low net CO2 assimilation and slow growth rate of mmdh1mmdh2. Loss of mMDH also affects photorespiration with alterations in CO2 assimilation/intercellular CO2 at low CO2, and the light-dependent elevated concentration of photorespiratory metabolites
physiological function
-
besides its function in malate synthesis, MDH is responsible for the exchange of reducing equivalents between metabolic pathways in distinct cell compartments
physiological function
-
besides its function in malate synthesis, MDH is responsible for the exchange of reducing equivalents between metabolic pathways in distinct cell compartments
physiological function
-
besides its function in malate synthesis, MDH is responsible for the exchange of reducing equivalents between metabolic pathways in distinct cell compartments
physiological function
cytosolic NAD-dependent malate dehydrogenase is an enzyme crucial for malate synthesis in the cytosol
physiological function
-
MDH1 plays a critical role in the cellular senescence of human fibroblasts. MDH1 is the major regulator of the cofactor NAD, the loss of which induces cellular senescence
physiological function
in illuminated chloroplasts, one mechanism involved in reduction-oxidation (redox) homeostasis is the malate-oxaloacetate shuttle. Excess electrons from photosynthetic electron transport in the form of nicotinamide adenine dinucleotide phosphate, reduced are used by NADP-dependent malate dehydrogenase (MDH), EC 1.1.1.82, to reduce oxaloacetate to malate, thus regenerating the electron acceptor NADP. NADP-MDH is a strictly redox-regulated, light-activated enzyme that is inactive in the dark. In the dark or in nonphotosynthetic tissues, the malate-oxaloacetate shuttle was proposed to be mediated by the constitutively active plastidial NAD-specific MDH isoform (pdNAD-MDH), but evidence is scarce. Critical role of pdNAD-MDH in Arabidopsis thaliana plants. Distinct roles for NAD- and NADP-linked redox homeostasis. pdNAD-MDH influences chloroplast ultrastructure and photosynthetic metabolism
physiological function
MDH is an energy-supplying enzyme, that catalyzes the interconversion of malate and oxaloacetate and plays crucial roles in several metabolic pathways including the citric acid cycle. The phosphorylation of enzyme MDH by serine/threonine protein kinases negatively regulates its activity
physiological function
-
regulation of MDH activity, overview
physiological function
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regulation of MDH activity, overview
physiological function
-
regulation of MDH activity, overview
physiological function
-
regulation of MDH activity, overview
physiological function
-
regulation of MDH activity, overview
physiological function
-
regulation of MDH activity, overview
physiological function
-
regulation of MDH activity, overview
physiological function
-
regulation of MDH activity, overview
physiological function
-
regulation of MDH activity, overview
physiological function
-
regulation of MDH activity, overview
physiological function
-
regulation of MDH activity, overview
physiological function
-
regulation of MDH activity, overview
physiological function
-
regulation of MDH activity, overview
physiological function
-
regulation of MDH activity, overview
physiological function
the mitochondrial isozyme is allosterically regulated by citrate
physiological function
the plastid-localized NAD-dependent MDH is important for plant survival in a dark or shady environment under which plNAD-MDH replaces the inactive chloroplast NADP-MDH in the regeneration of NAD+ to produce ATP
physiological function
-
plastidial NAD-dependent malate dehydrogenase 1 negatively regulates salt stress response by reducing the vitamin B6 content. The enzyme negatively regulates salt stress-induced pyridoxine accumulation. Enzyme-overexpressing plants exhibit salt stress-sensitive phenotypes
physiological function
-
the enzyme has strong effects on starch biosynthesis during seed development
physiological function
-
the enzyme is essential during embryogenesis and seed development. The protein, but not its NAD+-dependent malate dehydrogenase enzyme activity, is required for plastid development. The enzyme is required to stabilize filamentous temperature sensitive protease FtsH12
physiological function
-
the enzyme is essential for early etioplast and chloroplast development due to its moonlighting role in stabilizing FtsH12, distinct from its enzymatic function
physiological function
-
the enzyme isoform MDH1 plays a critical role in replenishing cytosolic NAD+ to support increased glycolysis during proliferation
physiological function
the enzyme is required for oxidation of NADH. The net reaction of the Mdh-Mqo couple equals that of an Ndh and it can serve as an alternative NADH dehydrogenase, as Mdh reduces oxaloacetate with NADH to L-malate, and the membrane-associated malate:quinone oxidoreductase (Mqo) subsequently re-oxidizes L-malate back to oxaloacetate and reduces menaquinone (MK)
physiological function
-
the enzyme is required for oxidation of NADH. The net reaction of the Mdh-Mqo couple equals that of an Ndh and it can serve as an alternative NADH dehydrogenase, as Mdh reduces oxaloacetate with NADH to L-malate, and the membrane-associated malate:quinone oxidoreductase (Mqo) subsequently re-oxidizes L-malate back to oxaloacetate and reduces menaquinone (MK)
-
physiological function
-
the enzyme is required for oxidation of NADH. The net reaction of the Mdh-Mqo couple equals that of an Ndh and it can serve as an alternative NADH dehydrogenase, as Mdh reduces oxaloacetate with NADH to L-malate, and the membrane-associated malate:quinone oxidoreductase (Mqo) subsequently re-oxidizes L-malate back to oxaloacetate and reduces menaquinone (MK)
-
physiological function
-
regulation of MDH activity, overview
-
physiological function
-
mitochondrial and cytosolic MDH isozymes are required for maintaining the balance of NAD+ and NADH in mitochondria and cytosol
-
physiological function
-
besides its function in malate synthesis, MDH is responsible for the exchange of reducing equivalents between metabolic pathways in distinct cell compartments
-
physiological function
-
the enzyme is required for oxidation of NADH. The net reaction of the Mdh-Mqo couple equals that of an Ndh and it can serve as an alternative NADH dehydrogenase, as Mdh reduces oxaloacetate with NADH to L-malate, and the membrane-associated malate:quinone oxidoreductase (Mqo) subsequently re-oxidizes L-malate back to oxaloacetate and reduces menaquinone (MK)
-
physiological function
-
MDH is an energy-supplying enzyme, that catalyzes the interconversion of malate and oxaloacetate and plays crucial roles in several metabolic pathways including the citric acid cycle. The phosphorylation of enzyme MDH by serine/threonine protein kinases negatively regulates its activity
-
physiological function
-
the enzyme is required for oxidation of NADH. The net reaction of the Mdh-Mqo couple equals that of an Ndh and it can serve as an alternative NADH dehydrogenase, as Mdh reduces oxaloacetate with NADH to L-malate, and the membrane-associated malate:quinone oxidoreductase (Mqo) subsequently re-oxidizes L-malate back to oxaloacetate and reduces menaquinone (MK)
-
physiological function
-
regulation of MDH activity, overview
-
physiological function
-
the enzyme is required for oxidation of NADH. The net reaction of the Mdh-Mqo couple equals that of an Ndh and it can serve as an alternative NADH dehydrogenase, as Mdh reduces oxaloacetate with NADH to L-malate, and the membrane-associated malate:quinone oxidoreductase (Mqo) subsequently re-oxidizes L-malate back to oxaloacetate and reduces menaquinone (MK)
-
physiological function
-
the enzyme is required for oxidation of NADH. The net reaction of the Mdh-Mqo couple equals that of an Ndh and it can serve as an alternative NADH dehydrogenase, as Mdh reduces oxaloacetate with NADH to L-malate, and the membrane-associated malate:quinone oxidoreductase (Mqo) subsequently re-oxidizes L-malate back to oxaloacetate and reduces menaquinone (MK)
-
additional information
inverse correlation between mMDH and ascorbate content
additional information
inverse correlation between mMDH and ascorbate content
additional information
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mMDH inhibition is of minor relevance for the growth inhibition caused by paullones
additional information
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a significant decrease of both mass and elongation of maize roots and shoots, as well as loss of root turgor and completely repressed lateral root growth were demonstrated in 0.1 mM Cu2+ and 5 mM Zn2+ treatments, overview
additional information
possible role for alternative splicing in the regulation of MDH compartmentalization in this yeast, gene YlMDH2 encodes the cytosolic and peroxisomal forms of MDH
additional information
possible role for alternative splicing in the regulation of MDH compartmentalization in this yeast, gene YlMDH2 encodes the cytosolic and peroxisomal forms of MDH
additional information
molecular dynamics simulation at higher temperatures were used to reconstruct structures from the crystal structure of TtMDH. At the simulated structure of 80°C, a large change occurs around the active site such that with increasing temperature, a mobile loop is closed to co-substrate binding region. The thermal-induced conformational change of the co-substrate binding loop of TtMDH may contribute to the essential movement of the enzyme for admitting NAD and may benefit the enzyme's activity
additional information
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molecular dynamics simulation at higher temperatures were used to reconstruct structures from the crystal structure of TtMDH. At the simulated structure of 80°C, a large change occurs around the active site such that with increasing temperature, a mobile loop is closed to co-substrate binding region. The thermal-induced conformational change of the co-substrate binding loop of TtMDH may contribute to the essential movement of the enzyme for admitting NAD and may benefit the enzyme's activity
additional information
the active loop on cMDH closing after sequential binding of NADH binding to the enzyme followed by the substrate
additional information
MalDH is an enzyme with intermediate properties between allosteric LDHs and non-allosteric tetrameric MalDHs. The catalytic residue is histidine H195. The structure of Ignicoccus islandicus MalDH resembles that of canonical LDHs. The amino acid at position 102 is considered as the most important substrate-discriminating residue between LDHs and MalDHs. Structure-function analysis and comparisons, overview
additional information
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MalDH is an enzyme with intermediate properties between allosteric LDHs and non-allosteric tetrameric MalDHs. The catalytic residue is histidine H195. The structure of Ignicoccus islandicus MalDH resembles that of canonical LDHs. The amino acid at position 102 is considered as the most important substrate-discriminating residue between LDHs and MalDHs. Structure-function analysis and comparisons, overview
additional information
sequence-similarity networks analysis
additional information
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sequence-similarity networks analysis
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additional information
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sequence-similarity networks analysis
-
additional information
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sequence-similarity networks analysis
-
additional information
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sequence-similarity networks analysis
-
additional information
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MalDH is an enzyme with intermediate properties between allosteric LDHs and non-allosteric tetrameric MalDHs. The catalytic residue is histidine H195. The structure of Ignicoccus islandicus MalDH resembles that of canonical LDHs. The amino acid at position 102 is considered as the most important substrate-discriminating residue between LDHs and MalDHs. Structure-function analysis and comparisons, overview
-
additional information
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sequence-similarity networks analysis
-
additional information
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sequence-similarity networks analysis
-
additional information
-
sequence-similarity networks analysis
-
additional information
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sequence-similarity networks analysis
-
additional information
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sequence-similarity networks analysis
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additional information
-
sequence-similarity networks analysis
-
additional information
-
sequence-similarity networks analysis
-
additional information
-
a significant decrease of both mass and elongation of maize roots and shoots, as well as loss of root turgor and completely repressed lateral root growth were demonstrated in 0.1 mM Cu2+ and 5 mM Zn2+ treatments, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
110000
-
cross-linking experiment
117000 - 148000
-
sedimentation equilibrium centrifugation
126600
-
enzyme form 1, gel fitration
133600
-
sedimentation equilibrium method
134900
-
sedimentation equlibrium method
137100
-
N.C.A. 1518 Ra2, N.C.A. 1503, sedimentation equilibrium method
140900
-
sedimentation equilibrium method
144000
-
cross-linking data
146000
-
cross-linking experiment
170000
-
fusion protein of MDH with mitochondrial citrate synthase, gel filtration
21550
-
4 * 21550, SDS-PAGE
27500
-
2 * 27500, SDS-PAGE
280000
-
isoform MDH1, gel filtration
31350
-
2 * 31350, SDS-PAGE
32200
2 * 32200, calculated from amino acid sequence
32638
x * 32638, calculated from sequence
33292
4 * 33292, calculated, 4 * 35086, MALDI-TOF
34500
-
2 * 34500, SDS-PAGE
34600
-
2 * 34600, SDS-PAGE
34689
-
x * 35000, SDS-PAGE, x * 34689, sequence calculation
35086
4 * 33292, calculated, 4 * 35086, MALDI-TOF
35300
-
4 * 35300, SDS-PAGE
35400
-
subunit of mitochondrial MDH, calculated from amino acid sequence
35560
-
x * 35000, recombinant enzyme, SDS-PAGE, x * 35560, plasma membrane-associated enzyme, sequence calculation
35600
-
2 * 35600, cytoplasmic form, SDS-PAGE
36100
-
4 * 36100, calculated from amino acid sequence
36400
-
subunit of cytosolic MDH, calculated from amino acid sequence
36600
-
4 * 36600, SDS-PAGE
37340
x * 36517, cMDH, sequence calculation, x * 37340, C-terminally His-tagged cMDH, sequence calculation, x * 36000, His-tagged cMDH, SDS-PAGE
39400
-
2 * 39400, SDS-PAGE
41000
-
subunit of mitochondrial MDH, SDS-PAGE
42000
-
subunit of cytosolic MDH, SDS-PAGE
43000
-
sedimentation equilibrium centrifugation
55000
-
x * 55000, SDS-PAGE
58000
-
2 * 58000, SDS-PAGE
60000 - 67000
-
sedimentation equilibrium centrifugation
60300
-
ultracentrifugation
63300
-
enzyme form 2, gel fitration
64200
-
ultracentrifugation equlibrium
64400
calculated from amino acid sequence
69500
-
both isoenzymes, sedimentation equilibrium
73350
dimeric enzyme, MALDI-TOF mass spectrometry
74200
-
sedimentation equilibrium centrifugation
79120
-
sedimentation equilibrium method
85040
-
sedimentation equilibrium method
124000
-
gel filtration
128000
-
-
128500
-
ultracentrifugation
128500
-
ultracentrifugation, sedimentation equilibrium studies
130000
-
-
130000
-
sedimentation equilibrium experiment
130000 - 140000
-
gel filtration
130000 - 140000
-
gel filtration
130000 - 140000
-
gel filtration
133000
gel filtration
133000
about, sequence calculation
134000
-
-
134000
-
sucrose density gradient centrifugation
134000
-
cross-linking data
134000
-
SDS-PAGE of enzyme after cross-linking
137000
-
-
138000
-
-
138000
-
sucrose density gradient centrifugation
138000
-
N.C.A. 1518 Ra2, gel filtration
138600
-
-
138600
-
sedimentation equilibrium method
140000
-
-
140000
-
recombinant enzyme, gel filtration
140000
-
various isoenzymes
140000
-
isoform MDH2, gel filtration
142000
-
-
142000
-
sucrose density gradient centrifugation
142000
-
sucrose density gradient centrifugation
148000
-
-
148000
-
enzyme cross-linking
148000
-
tetrameric isoform, gel filtration
150000
-
gel filtration
150000
-
native enzyme, gel filtration
160000
-
native PAGE
160000
-
enzymatically active preparation of recombinant wild type MDH, calculated from amino acid sequence
180000
-
tetrameric enzyme form, gel filtration
180000
-
K+ and/or dithioerythritol treated
31600
-
-
31600
-
2 * 31600, SDS-PAGE
32000
-
-
32000
-
4 * 32000, SDS-PAGE
32000
-
4 * 32000, SDS-PAGE
32000
4 * 32000, SDS-PAGE
32000
-
2 * 32000, native enzyme, gel filtration
33000
-
mass spectrometry
33000
-
mass spectrometry
33000
-
4 * 33000, SDS-PAGE
33000
4 * 33000, SDS-PAGE
33500
-
4 * 33500, SDS-PAGE
34000
-
2 * 34000, SDS-PAGE
34000
-
2 * 34000, SDS-PAGE
34000
-
4 * 34000, SDS-PAGE
34000
-
4 * 34000, SDS-PAGE
34000
-
2 * 34000, m-MDH, SDS-PAGE
35000
-
-
35000
-
K+ and/or dithioerythritol treated
35000
-
2 * 35000, SDS-PAGE
35000
-
2 * 35000, SDS-PAGE
35000
-
2 * 35000, SDS-PAGE
35000
-
2 * 35000, SDS-PAGE
35000
-
2 * 35000, SDS-PAGE
35000
2 * 35000, SDS-PAGE
35000
2 * 35000, SDS-PAGE
35000
-
4 * 35000, SDS-PAGE
35000
-
4 * 35000, SDS-PAGE
35000
-
4 * 35000, native enzyme, SDS-PAGE
35000
-
x * 35000, recombinant enzyme, SDS-PAGE, x * 35560, plasma membrane-associated enzyme, sequence calculation
35000
-
x * 35000, SDS-PAGE, x * 34689, sequence calculation
36000
-
2 * 36000, SDS-PAGE
36000
-
2 * 36000, SDS-PAGE
36000
-
4 * 36000, SDS-PAGE
36000
-
4 * 36000, SDS-PAGE
36000
-
2 * 36000, s-MDH, SDS-PAGE
36000
x * 36517, cMDH, sequence calculation, x * 37340, C-terminally His-tagged cMDH, sequence calculation, x * 36000, His-tagged cMDH, SDS-PAGE
36000
x * 36517, calculated, x * 36000, SDS-PAGE, recombinant protein
36517
x * 36517, cMDH, sequence calculation, x * 37340, C-terminally His-tagged cMDH, sequence calculation, x * 36000, His-tagged cMDH, SDS-PAGE
36517
x * 36517, calculated, x * 36000, SDS-PAGE, recombinant protein
36675
2 * 36675, MALDI-TOF mass spectrometry
36675
4 * 36675, MALDI-TOF mass spectrometry
37000
-
subunit, SDS-PAGE
37000
-
4 * 37000, SDS-PAGE
37000
-
4 * 37000, SDS-PAGE
37000
-
1 * 39000 + 1 * 37000, SDS-PAGE
37000
-
2 * 37000, mitochondrial form, SDS-PAGE
38000
-
2 * 38000
38000
-
1 * 38000, SDS-PAGE under both nonreduced and reduced conditions
39000
-
-
39000
-
2 * 39000, SDS-PAGE
39000
-
1 * 39000 + 1 * 37000, SDS-PAGE
39500
x * 39500, SDS-PAGE
39500
-
2 * 39500, pH 7.0, SDS-PAGE
39500
-
4 * 39500, pH 8.0, SDS-PAGE
40000
-
4 * 40000, SDS-PAGE
40000
-
2 * 40000, SDS-PAGE
45000
-
2 * 45000, SDS-PAGE
45000
-
2 * 45000, gel filtration
47000
-
2 * 47000, or tetramer, SDS-PAGE
47000
-
or dimer, 4 * 47000, SDS-PAGE
56000
-
gel filtration
57000
-
-
60000
-
-
60000
-
sucrose density gradient centrifugation
60000
-
sucrose density gradient centrifugation
60000
-
sucrose density gradient centrifugation
61000
-
gel filtration
61000
recombinant enzyme, gel filtration
62000
-
m-MDH
62000
x * 62000, recombinant GST-tagged enzyme, SDS-PAGE
64000
-
native enzyme, gel filtration
64000
-
repeatedly frozen and thawed, most stable unit, gel filtration
65000
-
-
67000
-
-
67000
-
sedimentation equilibrium centrifugation
67000
about, recombinant detagged mature enzyme, gel filtration
68000
-
-
68000
-
mitochondrial isoform
68000
-
both isoenzymes, gel filtration
68000
-
both isoenzymes, gel filtration
69000
-
-
69400
-
m-MDH
70000
-
-
70000
recombinant enzyme, gel filtration
70000
-
various isoenzymes
70000
-
gel filtration, analytical Sephadex
70000
-
isoform MDH3, gel filtration
72000
-
-
72000
-
cross-linking experiment
72000
-
cytoplasmic isoform
72400
-
-
75000
-
-
75000
-
Svedberg equation
75000
-
dimeric isoform, gel filtration
76000
-
-
80000
-
-
84000
-
-
86860
-
-
90000
Coccochloris peniocystis
-
gel filtration
90000
-
dimeric enzyme form, gel filtration
90000
-
cytosolic MDH and mitochondrial MDH, gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
x * 35600, calculated from amino acid sequence
?
x * 62000, recombinant GST-tagged enzyme, SDS-PAGE
?
x * 32638, calculated from sequence
?
-
x * 32638, calculated from sequence
-
?
-
x * 37000, FLAG-tagged enzyme, SDS-PAGE
?
-
x * 32000-34000, SDS-PAGE
?
x * 32000-34000, SDS-PAGE
?
-
x * 50000, GST-tagged enzyme, SDS-PAGE
?
-
x * 35000, SDS-PAGE, x * 34689, sequence calculation
?
-
x * 35000, SDS-PAGE, x * 34689, sequence calculation
-
?
x * 36517, cMDH, sequence calculation, x * 37340, C-terminally His-tagged cMDH, sequence calculation, x * 36000, His-tagged cMDH, SDS-PAGE
?
x * 36517, calculated, x * 36000, SDS-PAGE, recombinant protein
?
-
x * 35000, recombinant enzyme, SDS-PAGE, x * 35560, plasma membrane-associated enzyme, sequence calculation
?
-
x * 35000, recombinant enzyme, SDS-PAGE, x * 35560, plasma membrane-associated enzyme, sequence calculation
-
dimer
-
-
-
dimer
-
2 * 39500, pH 7.0, SDS-PAGE
dimer
-
crystal structure shows a compact homodimer with one coenzyme bound per subunit. The crystal structure reveals that the association of the dimers to form tetramers is prevented by several deletions, taking place at the level of two loops that are known to be essential for the tetramerization process within the LDH and malDH enzymes
dimer
-
2 * 35000, SDS-PAGE
dimer
-
2 * 35000, SDS-PAGE
-
dimer
-
2 * 34000, SDS-PAGE
dimer
-
2 * 34000, SDS-PAGE
dimer
-
2 * 36000, SDS-PAGE
dimer
-
2 * 34000, m-MDH, SDS-PAGE
dimer
-
2 * 36000, s-MDH, SDS-PAGE
dimer
-
2 * 34600, SDS-PAGE
dimer
-
1 * 39000 + 1 * 37000, SDS-PAGE
dimer
in the wild type the dimeric enzyme form is very unstable under low-salt conditions. The R207S/R292S mutation stabilizes the dimer sufficiently so that it can be observed and studied. The R207S/R292S mutant enzyme dissociates into dimers at 2 M NaCl, or at very low protein concentrations in 4 M NaCl above pH 7. This dimer is as active as the wild type tetramer at pH 8 but loses its activity at pH 7, without large changes in structure or association state
dimer
wild-type enzyme and R207S/R292S mutant enzyme can both exist as dimeric species depending on solvent conditions. F- and SO42-, as well as the NADH cofactor, stabilize the dimeric form of the wild-type protein
dimer
-
in the wild type the dimeric enzyme form is very unstable under low-salt conditions. The R207S/R292S mutation stabilizes the dimer sufficiently so that it can be observed and studied. The R207S/R292S mutant enzyme dissociates into dimers at 2 M NaCl, or at very low protein concentrations in 4 M NaCl above pH 7. This dimer is as active as the wild type tetramer at pH 8 but loses its activity at pH 7, without large changes in structure or association state
-
dimer
-
wild-type enzyme and R207S/R292S mutant enzyme can both exist as dimeric species depending on solvent conditions. F- and SO42-, as well as the NADH cofactor, stabilize the dimeric form of the wild-type protein
-
dimer
-
2 * 39000, SDS-PAGE
dimer
-
2 * 35000, SDS-PAGE
dimer
-
2 * 45000, SDS-PAGE
dimer
-
2 * 45000, SDS-PAGE
-
dimer
-
2 * 39400, SDS-PAGE
dimer
-
2 * 31350, SDS-PAGE
dimer
-
2 * 31350, SDS-PAGE
-
dimer
-
2 * 35600, cytoplasmic form, SDS-PAGE
dimer
-
2 * 37000, mitochondrial form, SDS-PAGE
dimer
2 * 35000, SDS-PAGE
dimer
-
2 * 35000, SDS-PAGE
dimer
-
2 * 27500, SDS-PAGE
dimer
-
2 * 27500, SDS-PAGE
-
dimer
-
2 * 47000, or tetramer, SDS-PAGE
dimer
-
2 * 47000, or tetramer, SDS-PAGE
-
dimer
-
2 * 90000-95000, fusion protein of MDH with mitochondrial citrate synthase, SDS-PAGE
dimer
-
2 * 40000, SDS-PAGE
dimer
2 * 36675, MALDI-TOF mass spectrometry
dimer
-
2 * 36675, MALDI-TOF mass spectrometry
-
dimer
-
-
286630, 286632, 286633, 286636, 286638, 286640, 286641, 286645, 286658, 286661, 286672, 286673, 286675
dimer
-
2 * 35000, SDS-PAGE
dimer
-
2 * 35000, SDS-PAGE
-
dimer
-
2 * 36000, SDS-PAGE
dimer
-
2 * 36000, SDS-PAGE
-
dimer
-
2 * 35000, SDS-PAGE
dimer
-
2 * 35000, SDS-PAGE
-
dimer
-
2 * 34500, SDS-PAGE
dimer
-
2 * 58000, SDS-PAGE
dimer
-
2 * 31600, SDS-PAGE
homodimer
-
2 * 35000, SDS-PAGE
homodimer
2 * 45600, full-length enzyme, SDS-PAGE, 2 * 36500, mature enzyme without transit peptide, SDS-PAGE and glutaraldehyde cross-linking of plNAD-MDH
homodimer
2 * 37500, calculated from amino acid sequence
homodimer
2 * 37000, SDS-PAGE. Thioredoxin-reversible homodimerization of isoform cytMDH1 through Cys330 disulfide formation protects the protein from overoxidation
homodimer
2 * 35000, SDS-PAGE
homodimer
2 * 32200, calculated from amino acid sequence
homodimer
-
2 * 36000, SDS-PAGE
homodimer
the dimer form dissociates to monomer at low enzyme concentration, and at low pH, and is active only in dimer form
homodimer
2 * 35000, recombinant enzyme, SDS-PAGE, 2 * 35800, about, sequence calculation
homodimer
-
2 * 35000, recombinant enzyme, SDS-PAGE, 2 * 35800, about, sequence calculation
-
homodimer
the active form of the Mtb MDH is a dimer. The His6-tag at the N-terminus of recombinant MDH does not inhibit the formation of a dimer by MDH
homodimer
-
the active form of the Mtb MDH is a dimer. The His6-tag at the N-terminus of recombinant MDH does not inhibit the formation of a dimer by MDH
-
homodimer
-
2 * 45000, gel filtration
homodimer
-
isoform MDH3, 2 * 35000, SDS-PAGE
homodimer
-
isoform MDH3, 2 * 35000, SDS-PAGE
-
homodimer
-
2 * 37200, SDS-PAGE
homodimer
-
x-ray crystallography
homodimer
-
2 * 32000, native enzyme, gel filtration
homodimer
2 * 36874.5, recombinant enzyme, sequence calculation
homodimer
-
2 * 35500, calculated from amino acid sequence
homooctamer
-
isoform MDH1, 8 * 35000, SDS-PAGE
homooctamer
-
isoform MDH1, 8 * 35000, SDS-PAGE
-
homotetramer
-
homotetramer
4 * 34700, His8-tagged enzyme, calculated from amino acid sequence
homotetramer
-
4 * 35000, recombinant enzyme, SDS-PAGE, 4 * 33200, about, sequence calculation
homotetramer
-
4 * 36100, calculated from amino acid sequence
homotetramer
-
isoform MDH2, 4 * 35000, SDS-PAGE
homotetramer
-
isoform MDH2, 4 * 35000, SDS-PAGE
-
monomer
the monomer is in an inactive molten globule-like state, which can be reactivated through a structural change induced by NADH binding that allows it to associate into active dimers
monomer
-
the monomer is in an inactive molten globule-like state, which can be reactivated through a structural change induced by NADH binding that allows it to associate into active dimers
-
monomer
-
1 * 38000, SDS-PAGE under both nonreduced and reduced conditions
tetramer
-
4 * 39500, pH 8.0, SDS-PAGE
tetramer
-
4 * 35000, SDS-PAGE
tetramer
-
4 * 33500, SDS-PAGE
tetramer
-
4 * 40000, SDS-PAGE
tetramer
-
4 * 40000, SDS-PAGE
-
tetramer
-
4 * 36000, SDS-PAGE
tetramer
4 * 32000, SDS-PAGE
tetramer
4 * 33000, SDS-PAGE
tetramer
-
4 * 32000, SDS-PAGE
tetramer
-
4 * 32000, SDS-PAGE
-
tetramer
-
4 * 35000, SDS-PAGE
tetramer
stabilized by ordered water molecule networks and intersubunit complex salt bridges locked in by bound solvent chloride and sodium ions
tetramer
the active tetrameric mutant enzyme R207S/R292S dissociates under certain conditions to active dimers and under other conditions to inactive dimers. These dimers further dissociate into folded monomers which eventually unfold. In 4 M NaCl (pH 8) and for the protein concentration range above 5 mg/ml, the R207S/R292S mutant enzyme is predominantly a tetramer
tetramer
-
stabilized by ordered water molecule networks and intersubunit complex salt bridges locked in by bound solvent chloride and sodium ions
-
tetramer
-
the active tetrameric mutant enzyme R207S/R292S dissociates under certain conditions to active dimers and under other conditions to inactive dimers. These dimers further dissociate into folded monomers which eventually unfold. In 4 M NaCl (pH 8) and for the protein concentration range above 5 mg/ml, the R207S/R292S mutant enzyme is predominantly a tetramer
-
tetramer
4 * 33500, about, sequence calculation
tetramer
-
4 * 33500, about, sequence calculation
-
tetramer
-
4 * 32000, SDS-PAGE
tetramer
-
4 * 32000, SDS-PAGE
-
tetramer
-
4 * 21550, SDS-PAGE
tetramer
4 * 33292, calculated, 4 * 35086, MALDI-TOF
tetramer
-
4 * 33292, calculated, 4 * 35086, MALDI-TOF
-
tetramer
-
4 * 33000, SDS-PAGE
tetramer
-
4 * 35000, native enzyme, SDS-PAGE
tetramer
-
4 * 37000, SDS-PAGE
tetramer
-
4 * 37000, SDS-PAGE
-
tetramer
-
4 * 37000, SDS-PAGE
-
tetramer
-
4 * 36000, SDS-PAGE
tetramer
-
4 * 36000, SDS-PAGE
-
tetramer
-
or dimer, 4 * 47000, SDS-PAGE
tetramer
-
or dimer, 4 * 47000, SDS-PAGE
-
tetramer
-
4 * 37000, SDS-PAGE
tetramer
-
4 * 37000, SDS-PAGE
-
tetramer
4 * 36675, MALDI-TOF mass spectrometry
tetramer
-
4 * 36675, MALDI-TOF mass spectrometry
-
tetramer
-
4 * 34000, SDS-PAGE
tetramer
-
4 * 36600, SDS-PAGE
tetramer
-
4 * 34000, SDS-PAGE
tetramer
-
4 * 31600, SDS-PAGE
tetramer
-
4 * 35300, SDS-PAGE
trimer
-
-
additional information
-
oligomeric states of MDHs, overview
additional information
-
oligomeric states of MDHs, overview
additional information
-
oligomeric states of MDHs, overview
additional information
-
oligomeric states of MDHs, overview
-
additional information
-
increasing the pH from 7.0 to 8.5 causes association of dimers with formation of tetramers, while lowering of pH to 6.0 is accompanied by dissociation of enzyme dimers with formation of MDH monomers
additional information
-
increasing the pH from 7.0 to 8.5 causes association of dimers with formation of tetramers, while lowering of pH to 6.0 is accompanied by dissociation of enzyme dimers with formation of MDH monomers
-
additional information
-
oligomeric states of MDHs, overview
additional information
-
oligomeric states of MDHs, overview
additional information
-
oligomeric states of MDHs, overview
additional information
-
oligomeric states of MDHs, overview
additional information
the Ignicoccus islandicus MaDH amino-acid sequence predicts two domains: a NAD(P)-binding Rossmann-fold domain (residues 7 to 138) and a LDH C-terminal-like domain (residues 146 to 308), MalDH quaternary structure analysis and comparison, overview
additional information
-
the Ignicoccus islandicus MaDH amino-acid sequence predicts two domains: a NAD(P)-binding Rossmann-fold domain (residues 7 to 138) and a LDH C-terminal-like domain (residues 146 to 308), MalDH quaternary structure analysis and comparison, overview
additional information
-
the Ignicoccus islandicus MaDH amino-acid sequence predicts two domains: a NAD(P)-binding Rossmann-fold domain (residues 7 to 138) and a LDH C-terminal-like domain (residues 146 to 308), MalDH quaternary structure analysis and comparison, overview
-
additional information
-
oligomeric states of MDHs, overview
additional information
-
oligomeric states of MDHs, overview
additional information
-
oligomeric states of MDHs, overview
additional information
-
enzyme activity and electrophoretic pattern of MDH and lactate dehydrogenase, EC 1.1.1.27, compared in relation to heat and urea inactivation, overview
additional information
-
oligomeric states of MDHs, overview
additional information
-
peptide mass fingerprinting, overview
additional information
structure analysis and comparison, MALDI-TOF mass spectrometry, overview
additional information
-
oligomeric states of MDHs, overview
additional information
-
structure analysis and comparison, MALDI-TOF mass spectrometry, overview
-
additional information
structure analysis, overview. Similar to other MDHs, a protomer of TtMDH has the N-terminal NAD binding domain and C-terminal catalytic domain and consists of 12 helices and 11 beta-strands. The N-terminal NAD binding domain (residue 1-156) is an open twisted structure with the classical Rossmann fold composed of a parallel six-stranded beta-sheet (beta1-beta6) and four alpha-helices (alpha1-alpha4). The C-terminal catalytic domain comprises an antiparallel twisted five-stranded sheet (beta7-beta11) surrounded by eight alpha-helices
additional information
-
structure analysis, overview. Similar to other MDHs, a protomer of TtMDH has the N-terminal NAD binding domain and C-terminal catalytic domain and consists of 12 helices and 11 beta-strands. The N-terminal NAD binding domain (residue 1-156) is an open twisted structure with the classical Rossmann fold composed of a parallel six-stranded beta-sheet (beta1-beta6) and four alpha-helices (alpha1-alpha4). The C-terminal catalytic domain comprises an antiparallel twisted five-stranded sheet (beta7-beta11) surrounded by eight alpha-helices
additional information
-
oligomeric states of MDHs, overview
additional information
-
oligomeric states of MDHs, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
C125S
-
the mutant of isoform cyMDH1 shows slightly increased activity compared to the wild type enzyme. The mutant of isoform cyMDH2 shows slightly decreased activity compared to the wild type enzyme
C131S
-
the mutant of isoform cyMDH3 shows decreased activity compared to the wild type enzyme
C155S
-
the mutant of isoform cyMDH1 shows slightly increased activity compared to the wild type enzyme. The mutant of isoform cyMDH2 shows slightly decreased activity compared to the wild type enzyme
C161S
-
the mutant of isoform cyMDH3 shows decreased activity compared to the wild type enzyme
C252S
-
the mutant of isoform cyMDH1 shows strongly decreased activity compared to the wild type enzyme. The mutant of isoform cyMDH2 shows slightly decreased activity compared to the wild type enzyme
C258S
-
the mutant of isoform cyMDH3 shows decreased activity compared to the wild type enzyme
C279S
-
the mutant of isoform cyMDH3 shows wild type activity
C292S
-
the mutant of isoform cyMDH1 shows slightly increased activity compared to the wild type enzyme. The mutant of isoform cyMDH2 shows slightly decreased activity compared to the wild type enzyme
C298S
-
the mutant of isoform cyMDH3 shows wild type activity
C2S
-
the mutant of isoform cyMDH3 shows strongly increased activity compared to the wild type enzyme
C330S
-
the mutant of isoform cyMDH1 shows slightly decreased activity compared to the wild type enzyme and is not inhibited by diamide. The mutant of isoform cyMDH2 shows decreased activity compared to the wild type enzyme and is not inhibited by diamide
C336S
-
the mutant of isoform cyMDH3 shows wild type activity
C79S
-
the mutant of isoform cyMDH1 shows slightly increased activity compared to the wild type enzyme. The mutant of isoform cyMDH2 shows slightly decreased activity compared to the wild type enzyme
C85S
-
the mutant of isoform cyMDH3 shows slightly decreased activity compared to the wild type enzyme
E165K
increase in temperature-optimum to 65°C, compared to 60°C for the wild-type enzyme. Maximal specific activity at temperature optimum is increased by about 30% compared to wild-type enzyme. Melting temperature at pH 4.4 is by 4.6°C, melting temperature at pH 6.0 is increased by 12.0°C and melting temperature at pH 7.5 is increased by 23.9°C compared to wild-type enzyme, mutation stabilizes to such an extent that disruption of the inter-dimer electrostatic network around residue 165 no longer limits kinetic thermal stability
E165Q
increase in temperature-optimum to 65°C, compared to 60°C for the wild-type enzyme. Maximal specific activity at temperature optimum is increased by about 30% compared to wild-type enzyme. Melting temperature at pH 4.4 is by 5.4°C, melting temperature at pH 6.0 is increased by 11.2°C and melting temperature at pH 7.5 is increased by 23.6°C compared to wild-type enzyme, mutation stabilizes to such an extent that disruption of the inter-dimer electrostatic network around residue 165 no longer limits kinetic thermal stability
F144I
site-directed mutagenesis, inactive mutant
G210A
site-directed mutagenesis, the mutant shows 30% reduced activity compared to the wild-type enzyme
G210A/V214I
site-directed mutagenesis, the double mutant shows a 2.2fold increase in lacatate dehydrogenase activity compared to the wild-type enzyme
I12V/R81Q/M85E/G210A/V214I
construction of a pentamutant by site-directed mutagenesis, whose substrate specificity is switched from malate dehydrogenase to that of lactate dehydrogenase, EC 1.1.1.27, the mutant shows highly reduced activity compared to the wild-type enzyme, overview
N122D
site-directed mutagenesis, inactive mutant
R81Q
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
V214I
site-directed mutagenesis, the mutant's activity is not affected
G210A
-
site-directed mutagenesis, the mutant shows 30% reduced activity compared to the wild-type enzyme
-
I12V/R81Q/M85E/G210A/V214I
-
construction of a pentamutant by site-directed mutagenesis, whose substrate specificity is switched from malate dehydrogenase to that of lactate dehydrogenase, EC 1.1.1.27, the mutant shows highly reduced activity compared to the wild-type enzyme, overview
-
N122D
-
site-directed mutagenesis, inactive mutant
-
R81Q
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
V214I
-
site-directed mutagenesis, the mutant's activity is not affected
-
E243R
mutation does not affect enzyme activity. The mutant enzyme is more halophilic than the wild-type protein. It is more sensitive to temperature and requires significantly higher concentrations of NaCl or KCl for equivalent stability
E267R
the numbering is not equivalent to the numbering of UniProt. The E267R mutation points into a central ordered water cavity, disrupting protein-solvent interactions. The mutant enzyme requires higher concentrations of the solvent salt for stability similar to that of the wild type
K205A
site-directed mutagenesis, the oligomeric state of the mutant changes with the nature of the anion bound, the mutant is dimeric or tetrameric, overview
R100Q
the mutant enzyme has considerably higher specificity for pyruvate than for oxaloacetate. Whereas the Km value for pyruvate is increased about 2fold, that for oxaloacetate increases 30fold. The R100Q mutant is not subjected to substrate inhibition, at least not at substrate concentrations up to 30 mM, and the highest kcat value is obtained at the lowest salt concentration used (0.15 M NaCl)
E243R
-
mutation does not affect enzyme activity. The mutant enzyme is more halophilic than the wild-type protein. It is more sensitive to temperature and requires significantly higher concentrations of NaCl or KCl for equivalent stability
-
E267R
-
the numbering is not equivalent to the numbering of UniProt. The E267R mutation points into a central ordered water cavity, disrupting protein-solvent interactions. The mutant enzyme requires higher concentrations of the solvent salt for stability similar to that of the wild type
-
R100Q
-
the mutant enzyme has considerably higher specificity for pyruvate than for oxaloacetate. Whereas the Km value for pyruvate is increased about 2fold, that for oxaloacetate increases 30fold. The R100Q mutant is not subjected to substrate inhibition, at least not at substrate concentrations up to 30 mM, and the highest kcat value is obtained at the lowest salt concentration used (0.15 M NaCl)
-
H187Y
-
catalytically inactive
E145A
the mutant shows severely reduced activity compared to the wild type enzyme
H172A
the mutant shows severely reduced activity compared to the wild type enzyme
N120A
the mutant shows severely reduced activity compared to the wild type enzyme
R148A
the mutant shows severely reduced activity compared to the wild type enzyme
R82A
the mutant shows severely reduced activity compared to the wild type enzyme
R88A
the mutant shows severely reduced activity compared to the wild type enzyme
T218A
the mutant shows severely reduced activity compared to the wild type enzyme
H229Q
mutant enzyme is less resistant to heat denaturation than the wild-type enzyme
Q229H
mutant enzyme is more resistant to heat denaturation than the wild-type enzyme
H229Q
-
mutant enzyme is less resistant to heat denaturation than the wild-type enzyme
-
Q229H
-
mutant enzyme is more resistant to heat denaturation than the wild-type enzyme
-
V114H
decrease in thermal stability, decrease in KM-value and kcat
V144N
decrease in thermal stability
R183a
-
dimeric mutant with almost wild type activity
R214G
-
dimeric mutant with almost wild type activity
R207S/R292S
site-directed mutagenesis, the oligomeric state of the mutant changes with the nature of the anion bound, the mutant is dimeric or tetrameric, overview
R207S/R292S
the numbering is not equivalent to the numbering of UniProt. The active tetrameric mutant enzyme R207S/R292S dissociates under certain conditions to active dimers and under other conditions to inactive dimers. These dimers further dissociate into folded monomers which eventually unfold. The mutant enzyme requires higher salt concentrations than the wild type for stability. Thermal inactivation starts at 35°C, whereas the wild type is stable up to 60°C. At 4 M NaCl (pH 8) the kinetics of unfolding of the mutant is measured by following the fluorescence emission during incubation at various temperatures. The process is biphasic between 35 and 48 °C, while the thermal deactivation kinetics of the wild type protein is first-order
R207S/R292S
the numbering is not equivalent to the numbering of UniProt. The mutations, located at the dimer-dimer interface, disrupt two inter-dimeric salt bridge clusters that are essential for wild-type tetramer stabilisation. Association of active dimers into tetramers is weakened
R207S/R292S
-
the numbering is not equivalent to the numbering of UniProt. The active tetrameric mutant enzyme R207S/R292S dissociates under certain conditions to active dimers and under other conditions to inactive dimers. These dimers further dissociate into folded monomers which eventually unfold. The mutant enzyme requires higher salt concentrations than the wild type for stability. Thermal inactivation starts at 35°C, whereas the wild type is stable up to 60°C. At 4 M NaCl (pH 8) the kinetics of unfolding of the mutant is measured by following the fluorescence emission during incubation at various temperatures. The process is biphasic between 35 and 48 °C, while the thermal deactivation kinetics of the wild type protein is first-order
-
R207S/R292S
-
the numbering is not equivalent to the numbering of UniProt. The mutations, located at the dimer-dimer interface, disrupt two inter-dimeric salt bridge clusters that are essential for wild-type tetramer stabilisation. Association of active dimers into tetramers is weakened
-
additional information
-
construction of enzyme-deficient mutants by pmdh1 and pmdh2 genes disruption by T-DNA insertion, mutant seedlings mobilize their triacylglycerol very slowly and growth are insensitive to 2,4-dichlorophenoxybutyric acid, phenotype, overview
additional information
construction of knockout single and double mutants, homozygous T-DNA insertion lines for single and double mutations, for the highly expressed mMDH1 and lower expressed mMDH2 isozymes, mmdh1mmdh2 mutant has no detectable mMDH activity but is viable, albeit small and slow growing. Quantitative proteome analysis of mitochondria shows changes in other mitochondrial NAD-linked dehydrogenases, indicating a reorganization of such enzymes in the mitochondrial matrix, phenotypes, overview. Complementation of mmdh1mmdh2 with an mMDH cDNA recovers mMDH activity, suppressed respiratory rate, ameliorated changes to photorespiration, and increases plant growth
additional information
construction of knockout single and double mutants, homozygous T-DNA insertion lines for single and double mutations, for the highly expressed mMDH1 and lower expressed mMDH2 isozymes, mmdh1mmdh2 mutant has no detectable mMDH activity but is viable, albeit small and slow growing. Quantitative proteome analysis of mitochondria shows changes in other mitochondrial NAD-linked dehydrogenases, indicating a reorganization of such enzymes in the mitochondrial matrix, phenotypes, overview. Complementation of mmdh1mmdh2 with an mMDH cDNA recovers mMDH activity, suppressed respiratory rate, ameliorated changes to photorespiration, and increases plant growth
additional information
-
characterization of defined mutants lacking the non-proton-pumping NADH dehydrogenase Ndh (DELTAndh) and/or one of the alternative NADH-oxidizing enzymes, L-lactate dehydrogenase LdhA (DELTAldhA) and malate dehydrogenase Mdh (DELTAmdh). Together with the menaquinone-dependent L-lactate dehydrogenase LldD and malate:quinone oxidoreductase Mqo, the LdhA-LldD and Mdh-Mqo couples can functionally replace Ndh activity. In glucose minimal medium the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio, in line with Ndh being the major enzyme for NADH oxidation. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant, supporting an active role of the alternative Mdh-Mqo and LdhA-LldD systems in NADH oxidation and menaquinone reduction. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type, probably due to a higher activity of the menaquinone-dependent L-lactate dehydrogenase LldD. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR, suggesting that ldhA repression by the transcriptional regulator SugR prevented growth on L-lactate medium. Attempts to construct a DELTAndh/DELTAmdh/DELTAldhA triple mutant are not successful, suggesting that Ndh, Mdh and LdhA cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
additional information
characterization of defined mutants lacking the non-proton-pumping NADH dehydrogenase Ndh (DELTAndh) and/or one of the alternative NADH-oxidizing enzymes, L-lactate dehydrogenase LdhA (DELTAldhA) and malate dehydrogenase Mdh (DELTAmdh). Together with the menaquinone-dependent L-lactate dehydrogenase LldD and malate:quinone oxidoreductase Mqo, the LdhA-LldD and Mdh-Mqo couples can functionally replace Ndh activity. In glucose minimal medium the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio, in line with Ndh being the major enzyme for NADH oxidation. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant, supporting an active role of the alternative Mdh-Mqo and LdhA-LldD systems in NADH oxidation and menaquinone reduction. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type, probably due to a higher activity of the menaquinone-dependent L-lactate dehydrogenase LldD. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR, suggesting that ldhA repression by the transcriptional regulator SugR prevented growth on L-lactate medium. Attempts to construct a DELTAndh/DELTAmdh/DELTAldhA triple mutant are not successful, suggesting that Ndh, Mdh and LdhA cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
additional information
-
characterization of defined mutants lacking the non-proton-pumping NADH dehydrogenase Ndh (DELTAndh) and/or one of the alternative NADH-oxidizing enzymes, L-lactate dehydrogenase LdhA (DELTAldhA) and malate dehydrogenase Mdh (DELTAmdh). Together with the menaquinone-dependent L-lactate dehydrogenase LldD and malate:quinone oxidoreductase Mqo, the LdhA-LldD and Mdh-Mqo couples can functionally replace Ndh activity. In glucose minimal medium the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio, in line with Ndh being the major enzyme for NADH oxidation. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant, supporting an active role of the alternative Mdh-Mqo and LdhA-LldD systems in NADH oxidation and menaquinone reduction. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type, probably due to a higher activity of the menaquinone-dependent L-lactate dehydrogenase LldD. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR, suggesting that ldhA repression by the transcriptional regulator SugR prevented growth on L-lactate medium. Attempts to construct a DELTAndh/DELTAmdh/DELTAldhA triple mutant are not successful, suggesting that Ndh, Mdh and LdhA cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
-
additional information
-
characterization of defined mutants lacking the non-proton-pumping NADH dehydrogenase Ndh (DELTAndh) and/or one of the alternative NADH-oxidizing enzymes, L-lactate dehydrogenase LdhA (DELTAldhA) and malate dehydrogenase Mdh (DELTAmdh). Together with the menaquinone-dependent L-lactate dehydrogenase LldD and malate:quinone oxidoreductase Mqo, the LdhA-LldD and Mdh-Mqo couples can functionally replace Ndh activity. In glucose minimal medium the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio, in line with Ndh being the major enzyme for NADH oxidation. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant, supporting an active role of the alternative Mdh-Mqo and LdhA-LldD systems in NADH oxidation and menaquinone reduction. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type, probably due to a higher activity of the menaquinone-dependent L-lactate dehydrogenase LldD. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR, suggesting that ldhA repression by the transcriptional regulator SugR prevented growth on L-lactate medium. Attempts to construct a DELTAndh/DELTAmdh/DELTAldhA triple mutant are not successful, suggesting that Ndh, Mdh and LdhA cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
-
additional information
-
characterization of defined mutants lacking the non-proton-pumping NADH dehydrogenase Ndh (DELTAndh) and/or one of the alternative NADH-oxidizing enzymes, L-lactate dehydrogenase LdhA (DELTAldhA) and malate dehydrogenase Mdh (DELTAmdh). Together with the menaquinone-dependent L-lactate dehydrogenase LldD and malate:quinone oxidoreductase Mqo, the LdhA-LldD and Mdh-Mqo couples can functionally replace Ndh activity. In glucose minimal medium the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio, in line with Ndh being the major enzyme for NADH oxidation. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant, supporting an active role of the alternative Mdh-Mqo and LdhA-LldD systems in NADH oxidation and menaquinone reduction. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type, probably due to a higher activity of the menaquinone-dependent L-lactate dehydrogenase LldD. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR, suggesting that ldhA repression by the transcriptional regulator SugR prevented growth on L-lactate medium. Attempts to construct a DELTAndh/DELTAmdh/DELTAldhA triple mutant are not successful, suggesting that Ndh, Mdh and LdhA cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
-
additional information
-
characterization of defined mutants lacking the non-proton-pumping NADH dehydrogenase Ndh (DELTAndh) and/or one of the alternative NADH-oxidizing enzymes, L-lactate dehydrogenase LdhA (DELTAldhA) and malate dehydrogenase Mdh (DELTAmdh). Together with the menaquinone-dependent L-lactate dehydrogenase LldD and malate:quinone oxidoreductase Mqo, the LdhA-LldD and Mdh-Mqo couples can functionally replace Ndh activity. In glucose minimal medium the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio, in line with Ndh being the major enzyme for NADH oxidation. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant, supporting an active role of the alternative Mdh-Mqo and LdhA-LldD systems in NADH oxidation and menaquinone reduction. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type, probably due to a higher activity of the menaquinone-dependent L-lactate dehydrogenase LldD. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR, suggesting that ldhA repression by the transcriptional regulator SugR prevented growth on L-lactate medium. Attempts to construct a DELTAndh/DELTAmdh/DELTAldhA triple mutant are not successful, suggesting that Ndh, Mdh and LdhA cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
-
additional information
-
characterization of defined mutants lacking the non-proton-pumping NADH dehydrogenase Ndh (DELTAndh) and/or one of the alternative NADH-oxidizing enzymes, L-lactate dehydrogenase LdhA (DELTAldhA) and malate dehydrogenase Mdh (DELTAmdh). Together with the menaquinone-dependent L-lactate dehydrogenase LldD and malate:quinone oxidoreductase Mqo, the LdhA-LldD and Mdh-Mqo couples can functionally replace Ndh activity. In glucose minimal medium the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio, in line with Ndh being the major enzyme for NADH oxidation. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant, supporting an active role of the alternative Mdh-Mqo and LdhA-LldD systems in NADH oxidation and menaquinone reduction. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type, probably due to a higher activity of the menaquinone-dependent L-lactate dehydrogenase LldD. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR, suggesting that ldhA repression by the transcriptional regulator SugR prevented growth on L-lactate medium. Attempts to construct a DELTAndh/DELTAmdh/DELTAldhA triple mutant are not successful, suggesting that Ndh, Mdh and LdhA cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
-
additional information
-
characterization of defined mutants lacking the non-proton-pumping NADH dehydrogenase Ndh (DELTAndh) and/or one of the alternative NADH-oxidizing enzymes, L-lactate dehydrogenase LdhA (DELTAldhA) and malate dehydrogenase Mdh (DELTAmdh). Together with the menaquinone-dependent L-lactate dehydrogenase LldD and malate:quinone oxidoreductase Mqo, the LdhA-LldD and Mdh-Mqo couples can functionally replace Ndh activity. In glucose minimal medium the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio, in line with Ndh being the major enzyme for NADH oxidation. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant, supporting an active role of the alternative Mdh-Mqo and LdhA-LldD systems in NADH oxidation and menaquinone reduction. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type, probably due to a higher activity of the menaquinone-dependent L-lactate dehydrogenase LldD. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR, suggesting that ldhA repression by the transcriptional regulator SugR prevented growth on L-lactate medium. Attempts to construct a DELTAndh/DELTAmdh/DELTAldhA triple mutant are not successful, suggesting that Ndh, Mdh and LdhA cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
-
additional information
MdcyMDH overexpression contributed to malate accumulation in the apple callus and tomato
additional information
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MdcyMDH overexpression contributed to malate accumulation in the apple callus and tomato
additional information
MdcyMDH overexpression favourably contributes to cell and plant growth and confers stress tolerance both in the apple callus and tomato
additional information
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MdcyMDH overexpression favourably contributes to cell and plant growth and confers stress tolerance both in the apple callus and tomato
additional information
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isozyme Mdh1 overexpression in yeast extends life span of the organism requiring respiration and the Sir2 family, while the mdh1DELTAaat1DELTA double mutation blocks CR-mediated life span extension and also prevents the characteristic decrease in the NADH levels in the cytosolic/nuclear pool, overview
additional information
isozyme Mdh1 overexpression in yeast extends life span of the organism requiring respiration and the Sir2 family, while the mdh1DELTAaat1DELTA double mutation blocks CR-mediated life span extension and also prevents the characteristic decrease in the NADH levels in the cytosolic/nuclear pool, overview
additional information
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adsorption of the enzyme in 30 nm diameter Au nanoparticles for synthesis of bioconjugates, MDH:Au stoichiometry and kinetic parameters determined for MDH:Au, citrate synthase CS:Au, and three types of dual-activity MDH/CS:Au bioconjugates, method development, overview. The number of enzyme molecules adsorbed per particle is dependent upon the enzyme concentration in solution, with multilayers forming at high enzyme:Au solution ratios. The specific activity of adsorbed enzyme increases with increasing number adsorbed per particle for CS:Au, but is less sensitive to stoichiometry for MDH:Au
additional information
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construction of a bienzymatic biosensor for malic acid based on malate dehydrogenase and transaminase immobilized onto a glassy carbon powder/carbon nanotubes/NAD+ composite electrode. In order to shift the conversion of malate to oxaloacetate, a reaction to convert oxaloacetate to L-aspartate is coupled to the main reaction, by reacting it with glutamic acid in the presence of glutamate oxaloacetate transaminase, GOT. The main reaction shifts to products, thus promoting the conversion of malate, thereby generating NADH, pH 10.0. Method overview
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-10 - 35
-
at MgCl concentrations below 0.5 M or CaCl concentrations below 0.35 M, the stability of the protein increases with decreasing temperature down to -10°C. At higher concentrations (0.8-1.5 M MgCl2 or 0.5-1.0 M CaCl2), the curves are bell-shaped with symmetric decreases in stability around 4°C
10 - 45
-
the parasite enzyme activity is not affected in a broad temperature range (from 10°C to 45°C), the enzyme is also stable at 20°C and 37°C over a 30 min period
101
half-life: more than 80 min. Marked stabilizing effect of 1 M K2HPO4 with an increase in thermostability of approximately 40% at 101°C
20
stable for at least 30 min
30 - 100
high thermal stability of TtMDH, that does not reach a completely denatured state even at near 100°C
30 - 60
the purified recombinant His6-tagged MDH from strain 20Z fully retains activity after 18 h exposure at 30-40°C, and has a 10% residual activity after 18 h exposure at 50°C. The enzyme loses 50% of its activity after 10 min heating at 60°C
30 - 70
-
the enzyme is active in a broader temperature range. It retains full activity after 18 h exposure at 30-60°C, exhibiting a 1 h half-life time at 70°C
37
stable for at least 30 min
38
-
retains 100% activity after 45 min incubation, only 50% activity remains after 15 min at 45°C
47
-
complete inactivation
49.9 - 54.7
the melting temperature of the reduced isoform cytMDH1 is 54.7°C, while the melting temperature of the oxidized isoform cytMDH1 drops by to 49.9°C
5 - 40
gradual decrease in activity above 40°C
5 - 60
purified His-tagged cMDH, high stability within this range
50.5
Tm, melting temperature
51
-
m-MDH, activity reduced to 50%
63
t1/2 is 510 min for the wild-type enzyme and 15 min for mutant enzyme E243R
68
melting temperature of wild-type enzyme at pH 7.5 is 67.8°C
78.5
purified His-tagged cMDH, high stability within this range
79
melting temperature of wild-type enzyme at pH 6.0 is 79.4°C
86
melting temperature of mutant enzyme E165Q at pH 4.4 is 85.8°C
91
melting temperature of mutant enzyme E165Q at pH 6.0 is 90.6°C, melting temperature of mutant enzyme E165Q at pH 7.5 or mutant enzyme E165K at pH 6.0 is 91.4°C
92
melting temperature of mutant enzyme E165K at pH 7.5 is 91.7°C
98
more than 90% residual activity after 6 h in boiling water. No significant change in CD spectra up to 100°C
35
-
half-life: 26 min
35
-
loses activity above
40
-
half-life: 3 min
40
-
loses its activity completely upon incubation for 10 min
40
20 min, purified recombinant enzyme, 82% activity remaining
42
midpoint of denaturation for the recombinant enzyme
42
half-life is 20.9 min for wild-type enzyme, 19.8 min for mutant enzyme V114H and 14.2 min for mutant enzyme V114N
42
half-life of mMDH is about 5 min
42
recombinant cytosolic isoenzyme c-MDH-S has a half-life of more than 500 min
42
recombinant cytosolic isoenzyme form cMDH-L has a half-life of 3 min
42
-
about 20% loss of activity of cytosolic enzyme form cMDH after 50 h, about 70% loss of activity of mitochondrial enzyme form mMDH after 10 min
45
-
-
45
30 min, 50% loss of activity, mutant enzyme R207S/R292S
45
-
after incubation for 50 min enzyme loses about 90% of its activity
45
midpoint of denaturation for the recombinant enzyme
47.5 - 57.5
after 60 min incubation at 47.5°C, the enzyme retains 95% of initial activity, after 60 min incubation at 52.5°C, the enzyme still possesses 65.5% residual activity. After incubation at 57.5°C for 60 min the enzyme retains a residual activity of 11.7%
47.5 - 57.5
after 60 min incubation at 47.5°C, the enzyme retains 92.6% of initial activity, after 60 min incubation at 59.9°C, the enzyme still possesses 65.5% residual activity. After incubation at 57.5°C for 60 min, the enzyme is almost fully inactivated
50
-
-
50
-
stable for 20 min, loses more than 95% activity when subjected to 55°C for the same period of time
50
-
stable for 20 min, loses more than 95% activity when subjected to 55°C for the same period of time
50
-
the half-lives of MDH isoforms A and B2 at 50°C are about 60 min and 5 min, respectively
50
-
half-life of isoform A1 is 34 min, half-life of isoform A2 is 16 min, half-life of isoform B is 4 min
50
-
thermostable up to for 15 min
50
complete inactivation of native enzyme after 1 h, complete inactivation of recombinant enzyme after 15 min, half-life is 30 min in absence of bovine serum albumin, less than 10% loss of activity after 30 min in presence of 0.2 mg/ml bovine serum albumin
50
-
purified recombinant enzyme, half-life is 160 min, recombinant enzyme
50
purified recombinant enzyme, 70% activity remaining after 20 min, 71% after 30 min, 60% after 90 min, and 50% after 120 min
55
-
s-MDH, activity reduced to 50%
55
-
purified recombinant enzyme, stable below 55°C, loss of 18% activity after 10 min
55
20 min, purified recombinant enzyme, 10% activity remaining
55
-
retains full activity for more than 2 h
60
5 min, about 80% loss of activity
60
10 min, complete inactivation
60
-
purified recombinant enzyme, loss of 47% activity after 10 min
60
20 min, purified recombinant enzyme, complete inactivation
60
-
quite heat-stable, stable up to, loses 50% of its original activity after 10 min at 77°C
60
-
5 min, 78% loss of activity
60
-
15 min, about 25% loss of activity
65
-
-
65
-
enzyme activity and electrophoretic pattern of MDH and lactate dehydrogenase, LDH EC 1.1.1.27, compared in relation to heat and urea inactivation, MDH is more sensitive than LDH, overview
65
-
extremely heat-stable, withstanding for over 1 h with no loss of activity
65
-
completely stable to 2 h
65
-
purified recombinant enzyme, loss of 80% activity after 10 min
70
-
5 min, 89% loss of activity
70
-
15 min, about 50% loss of activity
75
half-life at pH 7.5: 0.6 min for wild-type enzyme, 228 min for mutant enzyme E165Q, 338 min for mutant enzyme E165K
75
-
stable up to, but loses all activity when heated to 80°C for 20 min
75
30 min, 50% loss of activity, wild-type enzyme
75
-
15 min, 75% residual activity, purified enzyme
80
-
activity increases up to
80
melting temperature of wild-type enzyme at pH 4.4 is 80.4°C
80
-
15 min, no loss of activity, enzyme in crude extract
80
-
2 min, almost completely inactivated above 80°C
80
-
15 min, about 70% loss of activity
85
half-life at pH 7.5: 35 min for mutant enzyme E165Q, 46 min for mutant enzyme E165K
85
melting temperature of mutant enzyme E165K at pH 4.4
85
-
1 min, complete loss of activity
90
5 h, stable
90
-
remarkably heat stable without losing activity after incubation for 60 min, 50% activity lost after 30 min at 96°C
90
-
fully active for 1 h
additional information
-
-
additional information
-
activity of purified enzyme decreases continually from 4°C to 80°C
additional information
-
0.4 M myo-inositol raises the Tm-value of the enzyme by 3.4°C, pinitol increases Tm by 3.8°C, glucose has no effect
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