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Literature summary for 1.3.1.12 extracted from
- The binding of tyrosine and NAD+ to chorismate mutase/prephenate dehydrogenase from Escherichia coli K12 and the effects of these ligands on the activity and self-association of the enzyme. Analysis in terms of a model (1983), J. Biol. Chem., 258, 3114-3120.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| L-tyrosine | - |
Escherichia coli |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| additional information | - |
formation of higher MW aggregates in presence of tyrosine and NAD+ | Escherichia coli |
| 78000 | 100000 | chorismate mutase-prephenate dehydrogenase bifunctional enzyme, sedimentation equilibrium centrifugation | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| prephenate + NAD+ | Escherichia coli | biosynthesis of L-tyrosine | 4-hydroxyphenylpyruvate + NADH + CO2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| prephenate + NAD+ | - |
Escherichia coli | 4-hydroxyphenylpyruvate + NADH + CO2 | - |
? | |
| prephenate + NAD+ | biosynthesis of L-tyrosine | Escherichia coli | 4-hydroxyphenylpyruvate + NADH + CO2 | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| chorismate mutase-prephenate dehydrogenase bifunctional enzyme | complex with EC 5.4.99.5 | Escherichia coli |
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