Any feedback?
Literature summary extracted from
- Reconstitution of native Escherichia coli pyruvate oxidase from apoenzyme monomers and FAD (1982), J. Biol. Chem., 257, 12878-12886.
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.2.5.1 | cell membrane | cell membrane-associated | Escherichia coli | - |
- |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.2.5.1 | pyruvate + ferricytochrome b1 + H2O | Escherichia coli | - |
acetate + CO2 + ferrocytochrome b1 | - |
? |  |
| 1.2.5.1 | pyruvate + ubiquinone-6 + H2O | Escherichia coli | - |
acetate + CO2 + ubiquinol-6 | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.2.5.1 | Escherichia coli | - |
- |
- |
Renatured (Commentary)
| EC Number | Renatured (Comment) | Organism |
|---|---|---|
| 1.2.5.1 | reconstitution of the native enzymatically active protein can be accomplished by incubating equimolar concentrations of apomonomers and FAD at pH 6.5. The second order reaction of apomonomers with FAD to form an initial monomer-FAD complex is fast. The rate-limiting step for enzymatic reactivation appears to be the folding of the polypeptide chain in the monomer-FAD complex to reconstitute the three-dimensional FAD binding site prior to subunit reassociation. The subsequent formation of native tetramers proceeds via an essentially irreversible dimer assembly pathway | 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 | - |
? | |
| 1.2.5.1 | pyruvate + ferricytochrome b1 + H2O | - |
Escherichia coli | acetate + CO2 + ferrocytochrome b1 | - |
? | |
| 1.2.5.1 | pyruvate + ubiquinone-6 + H2O | - |
Escherichia coli | acetate + CO2 + ubiquinol-6 | - |
? | |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.2.5.1 | FAD | - |
Escherichia coli | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
