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Literature summary extracted from
- Chorismate mutase-prephenate dehydrogenase from Escherichia coli. Kinetic mechanism of the prephenate dehydrogenase reaction (1982), Biochim. Biophys. Acta, 702, 212-219.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.3.1.12 | bovine serum albumin | formation of an enzyme-albumin complex with MW of 150000 | Escherichia coli |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.3.1.12 | 4-hydroxyphenylpyruvate | - |
Escherichia coli |  |
| 1.3.1.12 | AMP | - |
Escherichia coli | |
| 1.3.1.12 | NADH | - |
Escherichia coli | |
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+ | mechanism, kinetic studies | Escherichia coli | 4-hydroxyphenylpyruvate + NADH + CO2 | - |
? | |
| 1.3.1.12 | prephenate + NAD+ | biosynthesis of L-tyrosine | Escherichia coli | 4-hydroxyphenylpyruvate + NADH + CO2 | - |
? | |
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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