Activating Compound | Comment | Organism | Structure |
---|---|---|---|
L-Phe | allosteric activator, activation above 0.1 mM | Mycobacterium tuberculosis | |
L-Trp | allosteric activator, activation above 0.1 mM | Mycobacterium tuberculosis | |
L-Tyr | allosteric activator, activation above 0.1 mM | Mycobacterium tuberculosis |
Cloned (Comment) | Organism |
---|---|
the catalytic and regulatory domains of prephenate dehydratase are individually cloned in the NdeI/XhoI sites of pET23a vector and expressed in Escherichia coli BL21(DE3) | Mycobacterium tuberculosis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
L-Phe | at concentration up to 0.1 mM | Mycobacterium tuberculosis | |
L-Trp | at concentration up to 0.1 mM | Mycobacterium tuberculosis | |
L-Tyr | at concentration up to 0.1 mM | Mycobacterium tuberculosis | |
NaCl | enzyme activity is completely abolished in the presence of 200 mM and higher concentrations of NaCl | Mycobacterium tuberculosis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.5 | - |
prephenate | - |
Mycobacterium tuberculosis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
prephenate | Mycobacterium tuberculosis | key regulator enzyme in L-phenylalanine biosynthesis | phenylpyruvate + H2O + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
catalytic and regulatory domains of prephenate dehydratase, individually cloned in the NdeI/XhoI sites of pET23a vector and expressed in Escherichia coli BL21(DE3) | Mycobacterium tuberculosis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
prephenate | key regulator enzyme in L-phenylalanine biosynthesis | Mycobacterium tuberculosis | phenylpyruvate + H2O + CO2 | - |
? | |
prephenate | the enzyme is absolutely dependent on the presence of catalytic as well as the regulatory domains for optimum enzyme activity. The enzyme is monofunctional and does not possess any chorismate mutase activity | Mycobacterium tuberculosis | phenylpyruvate + H2O + CO2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | - |
Mycobacterium tuberculosis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | 42 | - |
Mycobacterium tuberculosis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | 7 | - |
Mycobacterium tuberculosis |