Literature summary for 1.2.5.1 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.

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Protein Variants

Protein Variants	Comment	Organism
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

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
pyruvate oxidase	-	Escherichia coli

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Release 2023.1 (January 2023)