Cloned (Comment) | Organism |
---|---|
gene tpl, recombinant expression in Escherichia coli strain SVS370/pTZTPL | Citrobacter freundii |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
L-bishomotyrosine | - |
Citrobacter freundii | |
L-homotyrosine | - |
Citrobacter freundii | |
additional information | inhibition of tyrosine phenol-lyase by tyrosine homologues and their O-methyl derivatives, overview. Synthesis, and steady-state and pre-steady-state kinetic evaluations of L-homotyrosine and L-bishomotyrosine as possible mechanism-based inhibitors for TPL | Citrobacter freundii | |
O-methyl-L-bishomotyrosine | - |
Citrobacter freundii | |
O-methyl-L-homotyrosine | - |
Citrobacter freundii |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-tyrosine + H2O | Citrobacter freundii | - |
phenol + pyruvate + NH3 | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Citrobacter freundii | P31013 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme from Escherichia coli strain SVS370/pTZTPL | Citrobacter freundii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-tyrosine + H2O | - |
Citrobacter freundii | phenol + pyruvate + NH3 | - |
r | |
additional information | tyrosine phenol-lyase is a pyridoxal 5'-phosphate (PLP)-dependent bacterial enzyme that catalyzes the reversible hydrolytic cleavage of the Cbeta-Cgamma bond of L-Tyr to phenol and ammonium pyruvate. In addition to its physiological substrate L-Tyr, TPL also catalyzes the in vitro beta-elimination of substrates with good leaving groups on the beta-carbon, including L-serine, L-cysteine, S-(2-nitrophenyl)-L-cysteine, O-acetyl-L-serines, and S-alkyl-L-cysteines | Citrobacter freundii | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
TPL | - |
Citrobacter freundii |
tyrosine phenol lyase | - |
Citrobacter freundii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Citrobacter freundii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Citrobacter freundii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | dependent on | Citrobacter freundii |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | rapid-scanning stopped-flow experiments, steady-state and pre-steady-state inhibition kinetics | Citrobacter freundii | |
0.8 | - |
L-homotyrosine | pH 8.0, 30°C, recombinant enzyme | Citrobacter freundii | |
0.8 | - |
O-methyl-L-homotyrosine | pH 8.0, 30°C, recombinant enzyme | Citrobacter freundii | |
1.04 | - |
O-methyl-L-bishomotyrosine | pH 8.0, 30°C, recombinant enzyme | Citrobacter freundii | |
1.5 | - |
L-bishomotyrosine | pH 8.0, 30°C, recombinant enzyme | Citrobacter freundii |