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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | as cofactor | Escherichia coli |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
62000 | - |
4 * 62000, SDS-PAGE | Escherichia coli |
240000 | - |
PAGE | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyruvate + ferricyanide + H2O | - |
Escherichia coli | acetate + CO2 + ferrocyanide | - |
? |
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 | Comment | Organism |
---|---|---|
EC 1.2.2.2 | formerly | Escherichia coli |
pyruvate oxidase | - |
Escherichia coli |
pyruvate:ubiquinone-8-oxidoreductase | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
thiamine diphosphate | - |
Escherichia coli |