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Literature summary for 1.1.1.38 extracted from

  • Cook, R.A.
    Distinct metal cofactor-induced conformational states in the NAD-specific malic enzyme of Escherichia coli as revealed by proteolysis studies (1983), Biochim. Biophys. Acta, 749, 198-203.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
aspartate
-
Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
acetyl-CoA allosteric inhibition Escherichia coli
ATP allosteric inhibition Escherichia coli
CoA allosteric inhibition Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ stabilizes two distinct conformational states of the enzyme, which differ in response to various substrate and effector concentrations Escherichia coli
Mn2+ stabilizes two distinct conformational states of the enzyme, which differ in response to various substrate and effector concentrations 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

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Escherichia coli