Cloned (Comment) | Organism |
---|---|
- |
Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
C328V | oligo-nucleotide mutagenesis, expression in Escherichia coli strains, 20% reduction in the catalytic constant, 2-3fold increase in Km for the substrates, completely resistant to both spontaneous and Cu2+-catalysed inactivation | Escherichia coli |
C61V | oligo-nucleotide mutagenesis, expression in Escherichia coli strains, inactive, does not bind metal ions, resistant to metal attack, no subunit dissociation upon Cu2+ treatment | Escherichia coli |
H64L | oligo-nucleotide mutagenesis, expression in Escherichia coli strains, unstable to treatment with phosphoenolpyruvate, half-life of about 24 h at 0.4 mM compared to 6 days for the wild-type | Escherichia coli |
General Stability | Organism |
---|---|
Cu2+ and Fe2+ accelerates subunit dissociation | Escherichia coli |
metal-catalysed oxidation of the enzyme, the apoenzyme shows an exponentially decrease in activity with a half-life of about 1 day at 22°C, Cu2+ and Fe2+ accelerated the rate of inactivation and subunit dissociation, phosphoenolpyruvate and EDTA stabilize, mutants are insensitive | Escherichia coli |
phosphoenolpyruvate stabilizes | Escherichia coli |
spontaneous inactivation with a net loss of two of the seven thiol groups per subunit is restored by dithiothreitol | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | 0.02 mM, complete inactivation; Phe-sensitive isozyme, complete inactivation at 0.02 mM, destabilization of the enzymes quarternary structure; phosphoenolpyruvate protects | Escherichia coli | |
Fe2+ | 0.02 mM: 60% inactivation. 0.2 mM: 90% inactivation; Phe-sensitive isozyme, 60% inactivation at 0.02 mM, 90% inactivation at 0.2 mM; phosphoenolpyruvate protects | Escherichia coli | |
Phe | feed-back inhibition, Phe-sensitive isozyme; Phe-sensitive isozyme | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | Phe-sensitive isozyme: Mn2+, Co2+, Zn2+, Fe3+ have no effect | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O | Escherichia coli | first enzyme of the aromatic amino acid biosynthesis | 2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
phenylalanine-sensitive isozyme | - |
Purification (Comment) | Organism |
---|---|
Phe-sensitive isozyme, recombinant wild-type from overexpressing strain and recombinant mutants | Escherichia coli |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate | active site cysteines: Cys61 and Cys328 | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O | - |
Escherichia coli | 2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate | - |
? | |
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O | first enzyme of the aromatic amino acid biosynthesis | Escherichia coli | 2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Escherichia coli |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | - |
half-life: 1.2 days in absence of phosphoenolpyruvate, half-life: 4 days in presence of 1 mM phosphoenolpyruvate | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.8 | - |
assay at | Escherichia coli |