Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.3.1.12 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)

Cloned (Comment) Organism
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

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Km of enzyme fragments Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Posttranslational Modification

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

Purification (Commentary)

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

Reaction

Reaction Comment Organism Reaction ID
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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
activity of enzyme fragments Escherichia coli
25.2
-
purified recombinant enzyme fragment comprising amino acid residues 93-373 Escherichia coli
55
-
purified recombinant enzyme fragment comprising amino acid residues 96-373 Escherichia coli
98
-
purified recombinant wild-type enzyme Escherichia coli

Storage Stability

Storage Stability Organism
-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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
prephenate + NAD+
-
Escherichia coli 4-hydroxyphenylpyruvate + CO2 + NADH
-
?
prephenate + NAD+ second step in the biosynthesis of L-tyrosine Escherichia coli 4-hydroxyphenylpyruvate + CO2 + NADH
-
?

Subunits

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

Synonyms

Synonyms Comment Organism
T-protein
-
Escherichia coli

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Escherichia coli