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Literature summary for 1.2.5.1 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
Search for more literature for 1.2.5.1

Protein Variants

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

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + ferricyanide + H2O
-
 Escherichia coli acetate + CO2 + ferrocyanide
-
 ?

Subunits

Subunits Comment Organism
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
tetramer 4 * 62000, SDS-PAGE Escherichia coli

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate
-
 Escherichia coli