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Literature summary for 1.3.1.12 extracted from

  • Sampathkumar, P.; Morrison, J.F.
    Chorismate mutase-prephenate dehydrogenase from Escherichia coli. Kinetic mechanism of the prephenate dehydrogenase reaction (1982), Biochim. Biophys. Acta, 702, 212-219.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
bovine serum albumin formation of an enzyme-albumin complex with MW of 150000 Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
4-hydroxyphenylpyruvate
-
Escherichia coli
AMP
-
Escherichia coli
NADH
-
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
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
prephenate + NAD+ mechanism, kinetic studies 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