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Literature summary extracted from

  • Yamaguchi, M.
    Studies on regulatory functions of malic enzymes. IV. Effects of sulfhydryl group modification on the catalytic function of NAD-linked malic enzyme from Escherichia coli (1979), J. Biochem., 86, 325-333.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.1.1.38 5,5'-dithiobis(2-nitrobenzoic acid) 0.5 mM, 2.7fold increase in oxaloacetate reduction activity Escherichia coli
1.1.1.38 N-ethylmaleimide 1 mM, 8.9fold increase in oxaloacetate reduction activity Escherichia coli
1.1.1.38 p-chloromercuribenzoate 0.02 mM, 2.5fold increase in oxaloacetate reduction activity Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.38 5,5'-dithiobis(2-nitrobenzoic acid) inhibition of decarboxylation activity Escherichia coli
1.1.1.38 iodoacetate inhibition of decarboxylation activity Escherichia coli
1.1.1.38 N-ethylmaleimide L-malate and tartronate strongly protect the enzyme in the presence of MnCl2 and NAD+, 80% inhibition of decarboxylation activity, 10fold increase in reduction activity Escherichia coli
1.1.1.38 p-(chloromercuri)benzoate
-
Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.38 0.025
-
NADH reduction of oxaloacetate Escherichia coli
1.1.1.38 0.063
-
NAD+ decarboxylation of L-malate Escherichia coli
1.1.1.38 0.45
-
L-malate decarboxylation of L-malate Escherichia coli
1.1.1.38 2.1
-
oxaloacetate reduction of oxaloacetate Escherichia coli
1.1.1.38 4.8
-
oxaloacetate decarboxylation of oxaloacetate Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.38 (S)-malate + NAD+ Escherichia coli
-
CO2 + pyruvate + NADH
-
?
1.1.1.38 Oxaloacetate Escherichia coli
-
CO2 + pyruvate
-
ir
1.1.1.38 oxaloacetate + NADH Escherichia coli
-
L-malate + NAD+
-
?
1.1.1.38 pyruvate + NADH + H+ Escherichia coli
-
L-lactate + NAD+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.38 Escherichia coli
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.38 0.07
-
pyruvate reduction Escherichia coli
1.1.1.38 1.7
-
oxaloacetate reduction Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.38 (S)-malate + NAD+
-
Escherichia coli CO2 + pyruvate + NADH
-
?
1.1.1.38 (S)-malate + NAD+
-
Escherichia coli CO2 + pyruvate + NADH
-
r
1.1.1.38 Oxaloacetate
-
Escherichia coli CO2 + pyruvate
-
ir
1.1.1.38 oxaloacetate + NADH
-
Escherichia coli L-malate + NAD+
-
?
1.1.1.38 oxaloacetate + NADH divalent metal ions are required Escherichia coli (S)-malate + NAD+
-
?
1.1.1.38 pyruvate + NADH + H+
-
Escherichia coli (S)-lactate + NAD+
-
?
1.1.1.38 pyruvate + NADH + H+
-
Escherichia coli L-lactate + NAD+
-
?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.38 4
-
oxaloacetate reduction Escherichia coli
1.1.1.38 5
-
pyruvate reduction Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.38 NAD+
-
Escherichia coli