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Literature summary 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

EC Number Inhibitors Comment Organism Structure
1.3.1.12 2-hydroxyphenylacetate
-
 Escherichia coli
1.3.1.12 adamantane analogues
-
 Escherichia coli
1.3.1.12 chorismate analogues
-
 Escherichia coli
1.3.1.12 citrate
-
 Escherichia coli
1.3.1.12 Diethylmalonate
-
 Escherichia coli
1.3.1.12 malonate
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.12 Escherichia coli
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3.1.12 52 101
-
 Escherichia coli

Substrates and Products (Substrate)

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

Synonyms

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