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Literature summary extracted from
- Characterisation of the subunits of chorismate mutase-prephenate dehydrogenase from Escherichia coli K12 (1971), Biochim. Biophys. Acta, 229, 805-812.
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.3.1.12 | prephenate + NAD+ | Escherichia coli | biosynthesis of L-tyrosine | 4-hydroxyphenylpyruvate + NADH + CO2 | - |
? |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.3.1.12 | Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.3.1.12 | prephenate + NAD+ | - |
Escherichia coli | 4-hydroxyphenylpyruvate + NADH + CO2 | - |
? | |
| 1.3.1.12 | prephenate + NAD+ | biosynthesis of L-tyrosine | Escherichia coli | 4-hydroxyphenylpyruvate + NADH + CO2 | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.3.1.12 | dimer | 2 * 39000-42000, SDS-PAGE | Escherichia coli |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.3.1.12 | chorismate mutase-prephenate dehydrogenase bifunctional enzyme | complex with EC 5.4.99.5 | Escherichia coli |
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Release 2023.1 (January 2023)
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