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Literature summary for 1.2.5.1 extracted from

  • Schreiner, M.E.; Riedel, C.; Holatko, J.; Patek, M.; Eikmanns, B.J.
    Pyruvate:quinone oxidoreductase in Corynebacterium glutamicum: molecular analysis of the pqo gene, significance of the enzyme, and phylogenetic aspects (2006), J. Bacteriol., 188, 1341-1350.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pyruvate + a quinone Corynebacterium glutamicum
-
acetate + CO2 + a quinol
-
?

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + a quinone
-
Corynebacterium glutamicum acetate + CO2 + a quinol
-
?
pyruvate + oxidized 2,6-dichloroindophenol activity assayed photometrically by monitoring the reduction of 2,6-dichloroindophenol, pH 6.0, 40°C Corynebacterium glutamicum acetate + CO2 + reduced 2,6-dichloroindophenol
-
?

Synonyms

Synonyms Comment Organism
pqo
-
Corynebacterium glutamicum
pyruvate:quinone oxidoreductase
-
Corynebacterium glutamicum

General Information

General Information Comment Organism
physiological function inactivation of the chromosomal pqo gene leads to the absence of pyruvate:quinone oxidoreductase activity. Growth and amino acid production are not affected under either condition tested. Introduction of plasmid-bound pqo into a pyruvate dehydrogenase complex-negative strain partially relieves the growth phenotype of this mutant, indicating that high pyruvate:quinone oxidoreductase activity can compensate for the function of the pyruvate dehydrogenase complex Corynebacterium glutamicum