1.1.1.39: malate dehydrogenase (decarboxylating)

This is an abbreviated version, for detailed information about malate dehydrogenase (decarboxylating), go to the full flat file.

Reaction

(S)-malate
+
NAD+
=
pyruvate
+
CO2
+
NADH

Synonyms

AZC3656 protein, dehydrogenase, malate, diphosphate nucleotide dependent malic enzyme, DMA, DME, m-NAD-ME, malic enzyme, malic enzyme 2, malic enzyme-NAD, ME, ME-NAD, ME2, mitochondrial malic enzyme, mitochondrial NAD(P)+-dependent malic enzyme, mitochondrial NAD+-dependent malic enzyme, mitochondrial NAD-malic enzyme, NAD(P)+-malic enzyme, NAD+-dependent malic enzyme, NAD-dependent malic enzyme, NAD-malic enzyme, NAD-ME, NAD-ME1, NAD-ME2, NAD-MEH, NAD-preferring malic enzyme, NAD-preferring ME, NAD-specific malic enzyme, pyruvic-malic carboxylase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.39 malate dehydrogenase (decarboxylating)

Inhibitors

Inhibitors on EC 1.1.1.39 - malate dehydrogenase (decarboxylating)

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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(S)-malate
2-Ketoglutarate
-
-
5'-AMP
-
isozyme NAD-ME2, competitive versus NAD+, mixed inhibition versus (S)-malate
acetyl-CoA
bicarbonate
Bromopyruvate
-
-
Ca2+
inhibits 30% at 1 mM and 60% at 10 mM
citrate
Crassula argentea
-
competitive
Cl-
Crassula argentea
-
-
CO2
-
chimeric mutant NAD-ME1q, mixed inhibition versus NAD+ and (S)-malate; isozyme NAD-ME2 and chimeric mutant NAD-ME1q, mixed inhibition versus NAD+ and (S)-malate
DL-isocitrate
-
-
fructose 6-phosphate
competitive versus (S)-malate, 70% inhibition at 2.5 mM
hydroquinone
-
-
L-asparatate
-
-
L-aspartate
-
slightly competitive to malate, only slight inhibition below pH 6.0
Li+
slight inhibition
Lu3+
-
strong inhibition, reversible slow-binding mechanism, reversible structural interconversion to the Mn2+-binding form, metal binding site structure
malonate
Mn2+
-
inhibits the reductive carboxylation reaction, inhibitory effect is about 20fold reduced by binding of fumarate and L-malate
Na+
complete inhibition at 10 mM, no effect by Na+ at 1 mM
oxalate
oxaloacetate
phosphoenolpyruvate
pyruvate
Tartrate
Tartronate
Urea
-
denaturation, in 3-5 M urea, the enzyme undergoes a reversible tetramer-dimer-monomer quaternary structural change in an acidic pH environment, which resulted in a molten globule state that is prone to aggregate, Mn2+ protects, overview
additional information
-