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Literature summary for 1.2.5.1 extracted from
- Role of flavin in acetoin production by two bacterial pyruvate oxidases (1993), Arch. Biochem. Biophys., 300, 364-371.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
| Pediococcus pseudomonas | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| pyruvate + ubiquinone + H2O = acetate + CO2 + ubiquinol | enzyme also catalyzes the formation of acetoin from pyruvate and acetaldehyde | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| pyruvate + ferricyanide + H2O | enzyme also catalyzes the formation of acetoin from pyruvate and acetaldehyde | Escherichia coli | acetate + CO2 + ferrocyanide | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| POXEC | - |
Escherichia coli |
| pyruvate oxidase | enzyme also catalyzes the formation of acetoin from pyruvate and acetaldehyde | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| 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 | |
| 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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