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Literature summary for 1.3.1.12 extracted from

  • Christendat, D.; Turnbull, J.L.
    Identifying groups Involved in the binding of prephenate to prephenate dehydrogenase from Escherichia coli (1999), Biochemistry, 38, 4782-4793.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Protein Variants

Protein Variants Comment Organism
R294Q chorismate mutase-prephenate dehydrogenase bifunctional enzyme, R294Q substitution reduces the affinity of the enzyme for prephenate, Arg294 interacts electrostatically with the ring carboxylate at C1 of prephenate Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.045 0.09 prephenate
-
Escherichia coli
0.103
-
NAD+ wild-type enzyme Escherichia coli
0.38
-
NAD+ mutant form R294Q Escherichia coli
5
-
prephenate mutant form R294Q 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+
-
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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.417
-
NAD+ mutant form R294Q Escherichia coli
0.417
-
prephenate mutant form R294Q Escherichia coli
0.45
-
NAD+ wild-type enzyme Escherichia coli
0.45
-
prephenate wild-type enzyme Escherichia coli