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Literature summary extracted from

  • Grabau, C.; Cronan, J.E., Jr.
    In vivo function of Escherichia coli pyruvate oxidase specifically requires a functional lipid binding site (1986), Biochemistry, 25, 3748-3751.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.2.5.1 additional information expression of a truncated gene lacking the last 24 amino acids of the C-terminus, thus being closely analogous to the activated species produced in vitro by limited chymotrypsin cleavage. The truncated protein is fully active in vitro in the absence of lipid, and its activity is not further increased by addition of lipid activators. The truncated enzyme fails to bind Triton X-114. Strains producing the truncated protein are devoid of oxidase activity in vivo Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.5.1 pyruvate + ubiquinone-8 + H2O Escherichia coli
-
 acetate + CO2 + ubiquinol-8
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.5.1 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.5.1 pyruvate + ubiquinone-8 + H2O
-
 Escherichia coli acetate + CO2 + ubiquinol-8
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.2.5.1 pyruvate oxidase
-
 Escherichia coli