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 | Comment | Organism | Structure |
---|---|---|---|
L-tyrosine | feed-back inhibition of both enzyme activities | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Km of enzyme fragments | Escherichia coli |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
additional information | proteolytic digestion of recombinant wild-type enzyme by papain, pH 6.8, 37°C | Escherichia coli |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged wild-type enzyme and enzyme fragments | Escherichia coli |
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 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 | 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 | 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 | 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 | Comment | Organism |
---|---|---|
T-protein | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
about, assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Escherichia coli |