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Literature summary for 1.3.1.12 extracted from

  • Smith, G.D.; Roberts, D.V.; Daday, A.
    Affinity chromatography and inhibition of chorismate mutase-prephenate dehydrogenase by derivatives of phenylalanine and tyrosine (1977), Biochem. J., 165, 121-126.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
N-benzenesulfonyl-L-phenylalanine
-
Escherichia coli
N-Benzyloxycarbonyl-L-phenylalanine
-
Escherichia coli
N-Toluene-p-sulfonyl-L-p-aminophenylalanine
-
Escherichia coli
N-Toluene-p-sulfonyl-L-phenylalanine
-
Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
prephenate + NAD+ Escherichia coli biosynthesis of L-tyrosine 4-hydroxyphenylpyruvate + NADH + CO2
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
chorismate mutase-prephenate dehydrogenase bifunctional enzyme Escherichia coli
one-step procedure by affinity chromatography Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
prephenate + NAD+
-
Escherichia coli 4-hydroxyphenylpyruvate + NADH + CO2
-
?
prephenate + NAD+ biosynthesis of L-tyrosine Escherichia coli 4-hydroxyphenylpyruvate + NADH + CO2
-
?

Synonyms

Synonyms Comment Organism
chorismate mutase-prephenate dehydrogenase bifunctional enzyme complex with EC 5.4.99.5 Escherichia coli