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Literature summary for 1.1.1.38 extracted from

  • Milne, J.A.; Cook, R.A.
    Role of metal cofactors in enzyme regulation. Differences in the regulatory properties of the Escherichia coli nicotinamide adenine dinucleotide specific malic enzyme depending on whether Mg2+ or Mn2+ serves as divalent cation (1979), Biochemistry, 18, 3605-3610.
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Inhibitors

Inhibitors Comment Organism Structure
ATP more effective in the presence of Mn2+ than in the presence of Mg2+, 50% inhibition with 1.6 mM Mn2+ and 3.9 mM in the presence of Mg2+ respectively Escherichia coli
CoA 50% inhibition with 0.75 mM CoA in the presence of Mg2+ and 3.4 mM in the presence of Mn2+ Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ complex sigmoidal saturation curve of free malate concentration in the presence of 5 mM Mg2+ Escherichia coli
Mn2+ hyperbolic saturation curve of free malate concentration in the presence of 0.3 mM Mn2+ Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-malate + NAD+ Escherichia coli
-
 CO2 + pyruvate + NADH
-
 ?
Oxaloacetate Escherichia coli
-
 CO2 + pyruvate
-
 ir

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-malate + NAD+
-
 Escherichia coli CO2 + pyruvate + NADH
-
 ?
(S)-malate + NAD+
-
 Escherichia coli CO2 + pyruvate + NADH
-
 r
Oxaloacetate
-
 Escherichia coli CO2 + pyruvate
-
 ir

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Escherichia coli