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Literature summary extracted from

  • Wang, A.Y.; Chang, Y.Y.; Cronan, J.E., Jr.
    Role of the tetrameric structure of Escherichia coli pyruvate oxidase in enzyme activation and lipid binding (1991), J. Biol. Chem., 266, 10959-10966.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.2.5.1 A533T in native gel electrophoresis, mutant enzymes show differing electrophoretic mobilities. A533T mobility is similar to wild-type, and slower than Y549Term Escherichia coli
1.2.5.1 A553V in native gel electrophoresis, mutant enzymes show differing electrophoretic mobilities. A553V mobility is similar to wild-type, and slower than Y549Term Escherichia coli
1.2.5.1 E564P in native gel electrophoresis, mutant enzymes show differing electrophoretic mobilities. E564P has the slowest mobilityamong the mutants tested Escherichia coli
1.2.5.1 R572E in native gel electrophoresis, mutant enzymes show differing electrophoretic mobilities. R572E has the fastest mobility among the mutants tested Escherichia coli
1.2.5.1 R572G in native gel electrophoresis, mutant enzymes show differing electrophoretic mobilities. R572G shows a midway mobility Escherichia coli
1.2.5.1 R572K in native gel electrophoresis, mutant enzymes show differing electrophoretic mobilities. R572K mobility is similar to wild-type, and slower than Y549Term Escherichia coli
1.2.5.1 R572Term deletion of last amino acid. In native gel electrophoresis, mutant enzymes show differing electrophoretic mobilities. R572Term shows a midway mobility Escherichia coli
1.2.5.1 W570Term deletion of last three amino acids. In native gel electrophoresis, mutant enzymes show differing electrophoretic mobilities.. W570Term shows a midway mobility Escherichia coli
1.2.5.1 Y549Term deletion of last 24 amino acids. In native gel electrophoresis, mutant enzymes show differing electrophoretic mobilities.. Y549Term shows a midway mobility Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.5.1 Mg2+ as cofactor Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.5.1 62000
-
 4 * 62000, SDS-PAGE Escherichia coli
1.2.5.1 240000
-
 PAGE Escherichia coli

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 + ferricyanide + H2O
-
 Escherichia coli acetate + CO2 + ferrocyanide
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.5.1 More when two poxB gene alleles coexist in cells either on a single plasmid or on two compatible plasmids, heterotetrameric species are formed in addition to homotetramers. The concentration of tetramer species varies according to the concentrations of the different subunit present. The distribution of each tetramer species seems virtually identical to those theoretically expected based on random mixing. The intrinsic activity of pyruvate oxidase is not affected by interactions among the four subunits. Each subunit of the tetramer catalyzes the oxidase reaction independently Escherichia coli
1.2.5.1 tetramer 4 * 62000, SDS-PAGE Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.2.5.1 EC 1.2.2.2 formerly Escherichia coli
1.2.5.1 pyruvate oxidase
-
 Escherichia coli
1.2.5.1 pyruvate:ubiquinone-8-oxidoreductase
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.5.1 thiamine diphosphate
-
 Escherichia coli