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Literature summary extracted from
- Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by chorismate mutase-prephenate dehydrogenase from Escherichia coli (1998), Biochemistry, 37, 15703-15712.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.3.1.12 | T7 expression system | Escherichia coli |
| 5.4.99.5 | expression in Escherichia coli | Escherichia coli |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.3.1.12 | H131A | chorismate mutase-prephenate dehydrogenase bifunctional enzyme, mutant enzyme retains 10% of dehydrogenase activity and 30% mutase activity compared to the wild-type enzyme, His131 is not an essential residue whose protonation state is critical for catalysis or substrate binding | Escherichia coli |
| 1.3.1.12 | H189N | chorismate mutase-prephenate dehydrogenase bifunctional enzyme, mutant enzyme shows less than 0.01% the activity of wild-type mutase and dehydrogenase | Escherichia coli |
| 1.3.1.12 | H197N | chorismate mutase-prephenate dehydrogenase bifunctional enzyme, mutant enzyme exhibits no significant dehydrogenase activity, retains nearly wild-type mutase activity and unaltered Michaelis constants for chorismate, prephenate and NAD+ | Escherichia coli |
| 1.3.1.12 | K37A | chorismate mutase-prephenate dehydrogenase bifunctional enzyme, mutant protein poorly expressed, no detectable mutase or dehydrogenase activity, structural changes may result in its inactivity and instability | Escherichia coli |
| 1.3.1.12 | K37Q | chorismate mutase-prephenate dehydrogenase bifunctional enzyme, mutant enzyme exhibits no mutase activity while retaining wild-type dehydrogenase activity | Escherichia coli |
| 5.4.99.5 | H131A | 30% activity compared to wild-type enzyme | Escherichia coli |
| 5.4.99.5 | H153N | lower turnover and higher KM than wild-type enzyme | Escherichia coli |
| 5.4.99.5 | H189N | much lower turnover than wild-type enzyme | Escherichia coli |
| 5.4.99.5 | H197N | lower turnover and higher KM than wild-type enzyme | Escherichia coli |
| 5.4.99.5 | H239N | lower turnover and higher KM than wild-type enzyme | Escherichia coli |
| 5.4.99.5 | H245N | lower turnover and higher KM than wild-type enzyme | Escherichia coli |
| 5.4.99.5 | H257A | lower turnover and higher KM than wild-type enzyme | Escherichia coli |
| 5.4.99.5 | H265A | lower turnover and higher KM than wild-type enzyme | Escherichia coli |
| 5.4.99.5 | H347N | lower turnover than wild-type enzyme | Escherichia coli |
| 5.4.99.5 | K37A | more poorly expressed than wild-type, inactive and instable | Escherichia coli |
| 5.4.99.5 | K37Q | no activity | Escherichia coli |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.4.99.5 | prephenate | competitive inhibition | 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 | 0.054 | 0.055 | prephenate | mutant forms K37Q and H197N | Escherichia coli | |
| 1.3.1.12 | 0.103 | - |
NAD+ | wild-type enzyme | Escherichia coli | |
| 1.3.1.12 | 0.128 | 0.141 | NAD+ | mutant forms H197N and K37Q | Escherichia coli | |
| 5.4.99.5 | 0.041 | - |
chorismate | 30°C, pH 7.2, mutant H347N | Escherichia coli | |
| 5.4.99.5 | 0.045 | - |
chorismate | 30°C, pH 7.2, wild-type | Escherichia coli | |
| 5.4.99.5 | 0.051 | - |
chorismate | 30°C, pH 7.2, mutant H153N | Escherichia coli | |
| 5.4.99.5 | 0.053 | - |
chorismate | 30°C, pH 7.2, mutant H131A | Escherichia coli | |
| 5.4.99.5 | 0.068 | - |
chorismate | 30°C, pH 7.2, mutant H197N | Escherichia coli | |
| 5.4.99.5 | 0.098 | - |
chorismate | 30°C, pH 7.2, mutant H257A | Escherichia coli | |
| 5.4.99.5 | 0.099 | - |
chorismate | 30°C, pH 7.2, mutant H265A | Escherichia coli | |
| 5.4.99.5 | 0.126 | - |
chorismate | 30°C, pH 7.2, mutant H239N | Escherichia coli | |
| 5.4.99.5 | 0.225 | - |
chorismate | 30°C, pH 7.2, mutant H245N | 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 | - |
? | |
| 5.4.99.5 | Chorismate | Escherichia coli | biosynthesis of aromatic amino acids | Prephenate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.3.1.12 | Escherichia coli | - |
- |
- |
| 5.4.99.5 | Escherichia coli | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.3.1.12 | chorismate mutase-prephenate dehydrogenase bifunctional enzyme | Escherichia coli |
| 1.3.1.12 | wild-type and mutant enzyme | Escherichia coli |
| 5.4.99.5 | - |
Escherichia coli |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.3.1.12 | additional information | - |
- |
Escherichia coli |
Storage Stability
| EC Number | Storage Stability | Organism |
|---|---|---|
| 1.3.1.12 | 4°C, ammonium sulfate precipitate | 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 | - |
? | |
| 5.4.99.5 | Chorismate | - |
Escherichia coli | Prephenate | - |
? | |
| 5.4.99.5 | Chorismate | biosynthesis of aromatic amino acids | Escherichia coli | Prephenate | - |
? | |
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 |
| 5.4.99.5 | chorismate mutase | - |
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 | 0.00005 | - |
prephenate | mutant enzyme H197N | Escherichia coli | |
| 1.3.1.12 | 0.0000583 | - |
NAD+ | mutant enzyme H197N | Escherichia coli | |
| 1.3.1.12 | 0.367 | - |
NAD+ | mutant enzyme K37Q | Escherichia coli | |
| 1.3.1.12 | 0.383 | - |
prephenate | mutant enzyme K37Q | 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 | |
| 5.4.99.5 | additional information | - |
additional information | turnover of mutant H189N enzyme is lower than 0.0025 per second | Escherichia coli | |
| 5.4.99.5 | additional information | - |
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide | turnover of mutant H189N enzyme is lower than 0.0025 per second | Escherichia coli | |
| 5.4.99.5 | 2.3 | - |
chorismate | 30°C, pH 7.2, mutant H239N | Escherichia coli | |
| 5.4.99.5 | 4.8 | - |
chorismate | 30°C, pH 7.2, mutant H245N | Escherichia coli | |
| 5.4.99.5 | 6 | - |
chorismate | 30°C, pH 7.2, mutant H347N | Escherichia coli | |
| 5.4.99.5 | 7.2 | - |
chorismate | 30°C, pH 7.2, mutant H131A | Escherichia coli | |
| 5.4.99.5 | 8 | - |
chorismate | 30°C, pH 7.2, mutant H257A | Escherichia coli | |
| 5.4.99.5 | 10 | - |
chorismate | 30°C, pH 7.2, mutant H153N | Escherichia coli | |
| 5.4.99.5 | 15 | - |
chorismate | 30°C, pH 7.2, mutant H265A | Escherichia coli | |
| 5.4.99.5 | 16 | - |
chorismate | 30°C, pH 7.2, mutant H197N | Escherichia coli | |
| 5.4.99.5 | 27 | - |
chorismate | 30°C, pH 7.2, wild-type | Escherichia coli | |
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