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Literature summary for 2.5.1.54 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
Search for more literature for 2.5.1.54

Inhibitors

Inhibitors Comment Organism Structure
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
Phe Phe-sensitive isozyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2
-
 phosphoenolpyruvate Phe-sensitive isozyme, pH 6.8, 25°C Escherichia coli
21
-
 phosphoenolpyruvate Phe-sensitive isozyme, pH 6.8, 25°C Escherichia coli
21
-
 phosphoenolpyruvate sensitive to metal ion 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 in the shikimic pathway leading to biosynthesis of aromatic amino acids 2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AB91 phenylalanine-sensitive isozyme
-

Reaction

Reaction Comment Organism Reaction ID
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate sequential mechanism Escherichia coli
a
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate first substrate is phosphoenolpyruvate Escherichia coli
a
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]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
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

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

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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