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Literature summary for 1.1.5.4 extracted from

  • Mellgren, E.M.; Kloek, A.P.; Kunkel, B.N.
    Mqo, a tricarboxylic acid cycle enzyme, is required for virulence of Pseudomonas syringae pv. tomato strain DC3000 on Arabidopsis thaliana (2009), J. Bacteriol., 191, 3132-3141.
    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 Pseudomonas syringae mutants lacking mqo function grow more slowly in culture than wild-type bacteria when dicarboxylates are the only available carbon source. Mqo may be required by DC3000 to meet nutritional requirements in the apoplast and may provide insight into the mechanisms underlying the important, but poorly understood process of adaptation to the host environment ?
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Organism

Organism UniProt Comment Textmining
Pseudomonas syringae Q887Z4 pv. tomato strain DC3000. Tn5 transposon insertion mutants (the Tn5 insertion disrupts the malate:quinone oxidoreductase gene) with reduced virulence on Arabidopsis thaliana
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information mutants lacking mqo function grow more slowly in culture than wild-type bacteria when dicarboxylates are the only available carbon source. Mqo may be required by DC3000 to meet nutritional requirements in the apoplast and may provide insight into the mechanisms underlying the important, but poorly understood process of adaptation to the host environment Pseudomonas syringae ?
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Synonyms

Synonyms Comment Organism
malate:quinone oxidoreductase
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Pseudomonas syringae
Mqo
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Pseudomonas syringae