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Literature summary for 1.3.1.12 extracted from

  • Christopherson, R.I.; Heyde, E.; Morrison, J.F.
    Chorismate mutase-prephenate dehydrogenase from Escherichia coli: spatial relationship of the mutase and dehydrogenase sites (1983), Biochemistry, 22, 1650-1656.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
2-hydroxyphenylacetate
-
Escherichia coli
adamantane analogues
-
Escherichia coli
chorismate analogues
-
Escherichia coli
citrate
-
Escherichia coli
Diethylmalonate
-
Escherichia coli
malonate
-
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
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
52 101
-
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