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Literature summary extracted from
- Role of flavin in acetoin production by two bacterial pyruvate oxidases (1993), Arch. Biochem. Biophys., 300, 364-371.
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.2.5.1 | Escherichia coli | - |
- |
- |
| 1.2.5.1 | Pediococcus pseudomonas | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.2.5.1 | - |
Escherichia coli |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 1.2.5.1 | pyruvate + ubiquinone + H2O = acetate + CO2 + ubiquinol | enzyme also catalyzes the formation of acetoin from pyruvate and acetaldehyde | Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.2.5.1 | pyruvate + ferricyanide + H2O | enzyme also catalyzes the formation of acetoin from pyruvate and acetaldehyde | Escherichia coli | acetate + CO2 + ferrocyanide | - |
? |  |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.2.5.1 | POXEC | - |
Escherichia coli |
| 1.2.5.1 | pyruvate oxidase | enzyme also catalyzes the formation of acetoin from pyruvate and acetaldehyde | Escherichia coli |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.2.5.1 | FAD | role for FAD in acetoin formation is based on a structural requirement. In the acetoin reaction, FAD does not participate in a redox function | Escherichia coli | |
| 1.2.5.1 | FAD | role for FAD in acetoin formation is based on a structural requirement. In the acetoin reaction, FAD does not participate in a redox function | Pediococcus pseudomonas | |
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Release 2023.1 (January 2023)
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