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5'-AMP
isozyme NAD-ME2, competitive versus NAD+, mixed inhibition versus (S)-malate
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
fructose 6-phosphate
competitive versus (S)-malate, 70% inhibition at 2.5 mM
L-aspartate
-
slightly competitive to malate, only slight inhibition below pH 6.0
Lu3+
-
strong inhibition, reversible slow-binding mechanism, reversible structural interconversion to the Mn2+-binding form, metal binding site structure
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
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
(S)-malate
isozyme NAD-ME2, competitive
acetyl-CoA
-
-
acetyl-CoA
enzyme activity is allosterically regulated by acetyl-CoA, almost complete inhibition at 0.05 mM
acetyl-CoA
-
potent inhibitor
ATP
-
-
ATP
-
the enzyme is competitively inhibited by ATP up to 10fold. Addition of 1 mM or 5 mM fumarate reverses ATP-dependent inhibition of the enzyme to 55 or 70% of its maximum activity, respectively
ATP
-
competitive with respect to (S)-malate
bicarbonate
Amaranthus edulis
-
-
EDTA
-
-
EDTA
complete inhibition at 0.1 mM
malonate
-
-
NADH
isozyme NAD-ME2, competitive versus NAD+, mixed inhibition versus (S)-malate. NADH shows competitive and mixed-type inhibition versus NAD+ and (S)-malate with chimeric mutant NAD-ME1q; NADH shows competitive and mixed-type inhibition versus NAD+ and (S)-malate with chimeric mutant NAD-ME1q
NADH
Crassula argentea
-
product inhibition
NEM
-
-
oxalate
-
very tight binding inhibitor of the NAD-malic enzyme
oxaloacetate
-
-
oxaloacetate
competitive versus (S)-malate, 20% inhibition at 2.5 mM
phosphoenolpyruvate
-
-
phosphoenolpyruvate
Crassula argentea
-
activates at low concentrations, deactivation at high concentrations
pyruvate
isozyme NAD-ME2, uncompetitive versus NAD+, mixed inhibition versus (S)-malate. Pyruvate inhibition is uncompetitive with respect to NAD+ and mixed with respect to (S)-malate for the chimeric mutant NAD-ME1q; pyruvate inhibition is uncompetitive with respect to NAD+ and mixed with respect to (S)-malate for the chimeric mutant NAD-ME1q
pyruvate
Crassula argentea
-
product inhibition
Tartrate
substrate analogue, isozyme NAD-ME2, uncompetitive versus NAD+, competitive versus (S)-malate
Tartronate
-
binding site structure at the active site, competitive
additional information
product inhibition patterns of isozyme NAD-ME2, overview; product inhibition patterns of isozyme NAD-ME2, overview
-
additional information
product inhibition patterns of isozyme NAD-ME2, overview; product inhibition patterns of isozyme NAD-ME2, overview
-
additional information
-
product inhibition patterns of isozyme NAD-ME2, overview; product inhibition patterns of isozyme NAD-ME2, overview
-
additional information
Mnium undulatum
-
keeping plants in CO2-free air suppresses the activities of NAD-ME
-
additional information
-
keeping plants in CO2-free air suppresses the activities of NAD-ME
-
additional information
-
keeping plants in CO2-free air suppresses the activities of NAD-ME
-
additional information
-
keeping plants in CO2-free air suppresses the activities of NAD-ME
-
additional information
-
water stress reduces the enzyme activity in vivo
-