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Literature summary for 2.5.1.19 extracted from

  • Huynh, Q.K.
    Reaction of 5-enol-pyruvoylshikimate-3-phosphate synthase with diethyl pyrocarbonate: evidence for an essential histidine residue (1987), Arch. Biochem. Biophys., 258, 233-239.
    View publication on PubMed
Search for more literature for 2.5.1.19

Inhibitors

Inhibitors Comment Organism Structure
diethyldicarbonate inactivation with a second-order rate constant of 220/M/min, subtstrates protect from inactivation, enzyme activity is recovered by treatment with hydroxylamine Escherichia coli
N-phosphonomethylglycine 0.01 mM, 50% inhibition Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic parameters of native and diethyldicarbonate-inactivated enzyme Escherichia coli
0.02
-
 shikimate 3-phosphate
-
 Escherichia coli
0.025
-
 phosphoenolpyruvate
-
 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 K-12
-

Reaction

Reaction Comment Organism Reaction ID
phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate proposed mechanism Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphoenolpyruvate + 3-phosphoshikimate
-
 Escherichia coli phosphate + 5-enolpyruvylshikimate 3-phosphate i.e. 5-O-(1-carboxyvinyl)-3-phosphoshikimate r

Temperature Optimum [°C]

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