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Literature summary for 1.1.5.4 extracted from

  • van der Rest, M.E.; Frank, C.; Molenaar, D.
    Functions of the membrane-associated and cytoplasmic malate dehydrogenases in the citric acid cycle of Escherichia coli (2000), J. Bacteriol., 182, 6892-6899.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli NAD-dependent malate dehydrogenase (MDH, EC 1.1.1.37) does not repress mqo expression. MQO and MDH are active at the same time in Escherichia coli. No significant role for MQO in malate oxidation in wild-type Escherichia coli. Comparing growth of the mdh single mutant to that of the double mutant containing mdh and mqo deletions indicates that MQO partly takes over the function of MDH in an mdh mutant ?
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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Source Tissue

Source Tissue Comment Organism Textmining
additional information expression of the mqo gene and, consequently, MQO activity are regulated by carbon and energy source for growth. In batch cultures, MQO activity is highest during exponential growth and decreases sharply after onset of the stationary phase Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information NAD-dependent malate dehydrogenase (MDH, EC 1.1.1.37) does not repress mqo expression. MQO and MDH are active at the same time in Escherichia coli. No significant role for MQO in malate oxidation in wild-type Escherichia coli. Comparing growth of the mdh single mutant to that of the double mutant containing mdh and mqo deletions indicates that MQO partly takes over the function of MDH in an mdh mutant Escherichia coli ?
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Synonyms

Synonyms Comment Organism
malate:quinone oxidoreductase encoded by the gene mqo (previously called yojH) Escherichia coli
Mqo
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Escherichia coli