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Literature summary for 2.5.1.54 extracted from

  • Park, O.K.; Bauerle, R.
    Metal-catalyzed oxidation of phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli: inactivation and destabilization by oxidation of active-site cysteine (1999), J. Bacteriol., 181, 1636-1642.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Protein Variants

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

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

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

Metals/Ions Comment Organism Structure
additional information Phe-sensitive isozyme: Mn2+, Co2+, Zn2+, Fe3+ have no effect Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Escherichia coli
-
phenylalanine-sensitive isozyme
-

Purification (Commentary)

Purification (Comment) Organism
Phe-sensitive isozyme, recombinant wild-type from overexpressing strain and recombinant mutants Escherichia coli

Reaction

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 and Products (Substrate)

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Escherichia coli

Temperature Stability [°C]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
assay at Escherichia coli