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Literature summary extracted from

  • Chen, S.; Vincent, S.; Wilson, D.B.; Ganem, B.
    Mapping of chorismate mutase and prephenate dehydrogenase domains in the Escherichia coli T-protein (2003), Eur. J. Biochem., 270, 757-763.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.1.12 gene tyrA, genetic mapping of chorismate mutase and prephenate dehydrogenase activity, expression of the wild-type enzyme, the 2 activity domains, and gene fragments exhibiting either chorismate mutase or prephenate dehydrogenase activity as His-tagged proteins and peptides in strain BL21(DE3), respectively Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.1.12 L-tyrosine feed-back inhibition of both enzyme activities Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.12 additional information
-
 additional information Km of enzyme fragments 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 second step in the biosynthesis of L-tyrosine 4-hydroxyphenylpyruvate + CO2 + NADH
-
 ?

Organism

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

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.3.1.12 additional information proteolytic digestion of recombinant wild-type enzyme by papain, pH 6.8, 37°C Escherichia coli

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.1.12 recombinant His-tagged wild-type enzyme and enzyme fragments Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
1.3.1.12 prephenate + NAD+ = 4-hydroxyphenylpyruvate + CO2 + NADH + H+ the T-protein is a bifunctional enzyme showing chorismate mutase, EC 5.4.99.5, and prephenate dehydrogenase activities at two separate active sites Escherichia coli
a

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 additional information
-
 activity of enzyme fragments Escherichia coli
1.3.1.12 25.2
-
 purified recombinant enzyme fragment comprising amino acid residues 93-373 Escherichia coli
1.3.1.12 55
-
 purified recombinant enzyme fragment comprising amino acid residues 96-373 Escherichia coli
1.3.1.12 98
-
 purified recombinant wild-type enzyme Escherichia coli

Storage Stability

EC Number Storage Stability Organism
1.3.1.12 -80°C, purified recombinant His-tagged wild-type enzyme, complete loss of activity when stored in 0.1 M sodium citrate, pH 7.5, 10% glycerol, 1 mM DTT, or moderate loss in activity when stored in 0.1 M MES, pH 7.5, 0.051 M N-ethylmorpholine, 0.01 M diethanolamine, 1 mM EDTA, 1 mM DTT, 10% glycerol, 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 + CO2 + NADH
-
 ?
1.3.1.12 prephenate + NAD+ second step in the biosynthesis of L-tyrosine Escherichia coli 4-hydroxyphenylpyruvate + CO2 + NADH
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.1.12 dimer wild-type full length enzyme and some enzyme fragments form homodimers Escherichia coli
1.3.1.12 More MW of recombinant enzyme fragments, overview, structural localization of the different enzyme activities on the enzyme molecule Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.3.1.12 T-protein
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.3.1.12 37
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.1.12 7.5
-
 about, assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.12 NAD+
-
 Escherichia coli