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Literature summary extracted from

  • Parker, E.J.; Bulloch, E.M.M.; Jameson, G.B.; Abell, C.
    Substrate deactivation of phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase by erythrose 4-phosphate (2001), Biochemistry, 40, 14821-14828.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.54 D-erythrose 4-phosphate Phe-sensitive isozyme: in absence of phosphoenolpyruvate the enzyme is inhibited via formation of a covalent binding to Lys186 via a slow Schiff base reaction, mechanism Escherichia coli
2.5.1.54 Phe Phe-sensitive isozyme Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.54 2
-
 phosphoenolpyruvate Phe-sensitive isozyme, pH 6.8, 25°C Escherichia coli
2.5.1.54 21
-
 phosphoenolpyruvate Phe-sensitive isozyme, pH 6.8, 25°C Escherichia coli
2.5.1.54 21
-
 phosphoenolpyruvate sensitive to metal ion Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.54 phosphoenolpyruvate + D-erythrose 4-phosphate + H2O Escherichia coli first enzyme in the shikimic pathway leading to biosynthesis of aromatic amino acids 2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.54 Escherichia coli P0AB91 phenylalanine-sensitive isozyme
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.5.1.54 phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate sequential mechanism Escherichia coli
a
2.5.1.54 phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate first substrate is phosphoenolpyruvate Escherichia coli
a
2.5.1.54 phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate Lys186 is involved in hydrogen bonding with phosphoenolpyruvate Escherichia coli
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.5.1.54 additional information
-
 metal ions are removed form the buffer solution via Chelex 100 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.54 phosphoenolpyruvate + D-erythrose 4-phosphate + H2O binds 1 molecule D-erythrose 4-phosphate per subunit Escherichia coli 2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
 ir
2.5.1.54 phosphoenolpyruvate + D-erythrose 4-phosphate + H2O first enzyme in the shikimic pathway leading to biosynthesis of aromatic amino acids Escherichia coli 2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.54 ? x * 38009-38014, Phe-sensitive isozyme, electron mass spectroscopy and amino acid sequence determination Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.5.1.54 25
-
 assay at Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5.1.54 71
-
 phosphoenolpyruvate Phe-sensitive isozyme, pH 6.8, 25°C Escherichia coli
2.5.1.54 71
-
 D-erythrose 4-phosphate Phe-sensitive isozyme, pH 6.8, 25°C Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.54 6.8
-
 assay at Escherichia coli