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Literature summary for 4.2.1.51 extracted from

  • Friedrich, B.; Friedrich, C.G.; Schlegel, H.G.
    Purification and properties of chorismate mutase-prephenate dehydratase and prephenate dehydrogenase from Alcaligenes eutrophus (1976), J. Bacteriol., 126, 712-722.
    View publication on PubMedView publication on EuropePMC
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Inhibitors

Inhibitors Comment Organism Structure
Cu2+ 0.1 mM, 100% inhibition Cupriavidus necator
Fe2+ 0.1 mM, 85% inhibition Cupriavidus necator
Hg2+ 0.1 mM, 94% inhibition Cupriavidus necator
Ni2+ 0.1 mM, 83% inhibition Cupriavidus necator
Zn2+ 0.1 mM, 58% inhibition Cupriavidus necator

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
144000
-
 ultracentrifugation Cupriavidus necator
187000
-
 gel filtration Cupriavidus necator

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
prephenate Cupriavidus necator
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Cupriavidus necator
-
-
-

Purification (Commentary)

Purification (Comment) Organism
bifunctional enzyme, chorismate mutase:prephenate dehydratase Cupriavidus necator

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
24.9
-
-
 Cupriavidus necator

Storage Stability

Storage Stability Organism
-20°C, 50 mM phosphate buffer, pH 7.4, 0.7 mg protein/ml, stable for 10 months Cupriavidus necator

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
prephenate
-
 Cupriavidus necator phenylpyruvate + H2O + CO2
-
 ?
prephenate
-
 Cupriavidus necator ?
-
 ?