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Literature summary extracted from
- Exhaustive mutagenesis of six secondary active-site residues in Escherichia coli chorismate mutase shows the importance of hydrophobic side chains and a helix N-capping position for stability and catalysis (2007), Biochemistry, 46, 6883-6891.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 5.4.99.5 | analysis | As an intramolecular reaction that appears to be catalyzed without intermediate steps, covalent catalysis, or modification of the reaction pathway, the chorismate-prephenate rearrangement has become an important model system for theoretical approaches to the study of enzyme catalysis | Escherichia coli |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.4.99.5 | - |
Escherichia coli |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 5.4.99.5 | additional information | EcCM active-site residues (Leu7, Ala32, Val35, Asp48, Ile81, Val85) that mutated in our previous computational design experiment. Each of the 114 variants tested for complementation of the chorismate mutase deficiency of the auxotrophic Escherichia coli KA12/pKIMP-UAUC system. 34% of all single mutants are scored as biological active | Escherichia coli |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.4.99.5 | additional information | - |
additional information | The Km of the active complementations (position 7, 32, 35, 48, 81 and 85) is shown | Escherichia coli |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.4.99.5 | Chorismate | Escherichia coli | - |
Prephenate | - |
? |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.4.99.5 | Escherichia coli | P0A9J8 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.4.99.5 | - |
Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.4.99.5 | Chorismate | - |
Escherichia coli | Prephenate | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.4.99.5 | chorismate mutase | - |
Escherichia coli |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.5 | 37 | - |
assay at | Escherichia coli |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.5 | additional information | - |
The melting point of the active complementations (changes in position 7, 32, 35, 48, 81 and 85) is shown | Escherichia coli |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.4.99.5 | additional information | - |
additional information | The kcat of the active complementations (position 7, 32, 35, 48, 81 and 85) is shown | Escherichia coli |
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