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Literature summary extracted from
- Identifying groups Involved in the binding of prephenate to prephenate dehydrogenase from Escherichia coli (1999), Biochemistry, 38, 4782-4793.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.3.1.12 | - |
Escherichia coli |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.3.1.12 | R294Q | chorismate mutase-prephenate dehydrogenase bifunctional enzyme, R294Q substitution reduces the affinity of the enzyme for prephenate, Arg294 interacts electrostatically with the ring carboxylate at C1 of prephenate | Escherichia coli |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.3.1.12 | 0.045 | 0.09 | prephenate | - |
Escherichia coli |  |
| 1.3.1.12 | 0.103 | - |
NAD+ | wild-type enzyme | Escherichia coli | |
| 1.3.1.12 | 0.38 | - |
NAD+ | mutant form R294Q | Escherichia coli | |
| 1.3.1.12 | 5 | - |
prephenate | mutant form R294Q | 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+ | - |
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 |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.3.1.12 | 0.417 | - |
NAD+ | mutant form R294Q | Escherichia coli | |
| 1.3.1.12 | 0.417 | - |
prephenate | mutant form R294Q | Escherichia coli | |
| 1.3.1.12 | 0.45 | - |
NAD+ | wild-type enzyme | Escherichia coli | |
| 1.3.1.12 | 0.45 | - |
prephenate | wild-type enzyme | Escherichia coli | |
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Release 2023.1 (January 2023)
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