Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli XL-1 Blue cells | Citrobacter freundii |
Protein Variants | Comment | Organism |
---|---|---|
T15A | exhibits a 2fold improved activity towards 3,4-dihydroxyphenyl-L-alanine | Citrobacter freundii |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
3,4-dihydroxyphenyl-L-alanine | inactivated by a Pictet-Spengler reaction between the cofactor and 3,4-dihydroxyphenyl-L-alanine, on treatment with excess pyridoxal-5'-phosphate the inactivated enzymes recovers over 80% of the original activity | Citrobacter freundii |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.22 | - |
L-tyrosine | mutant enzyme T15A, in 0.1 M potassium phosphate buffer (pH 8.0) at 30°C | Citrobacter freundii | |
0.24 | - |
L-tyrosine | wild type enzyme, in 0.1 M potassium phosphate buffer (pH 8.0) at 30°C | Citrobacter freundii | |
3.2 | - |
3,4-dihydroxyphenyl-L-alanine | wild type enzyme, in 0.1 M potassium phosphate buffer (pH 8.0) at 30°C | Citrobacter freundii | |
4.6 | - |
3,4-dihydroxyphenyl-L-alanine | mutant enzyme T15A, at 30°C | Citrobacter freundii |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
52000 | - |
SDS-PAGE | Citrobacter freundii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Citrobacter freundii | - |
- |
- |
Purification (Comment) | Organism |
---|---|
Resource Q ion exchange chromatography and Phenyl Superose Phenyl Superose column chromatography | Citrobacter freundii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3,4-dihydroxyphenyl-L-alanine + H2O | - |
Citrobacter freundii | pyrocatechol + NH3 + pyruvate | - |
? | |
L-tyrosine + H2O | - |
Citrobacter freundii | phenol + pyruvate + NH3 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
L-tyrosine phenol-lyase | - |
Citrobacter freundii |
TPL | - |
Citrobacter freundii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | - |
native enzyme, using 3,4-dihydroxyphenyl-L-alanine as a substrate | Citrobacter freundii |
45 | - |
mutant enzyme T15A, using 3,4-dihydroxyphenyl-L-alanine as a substrate | Citrobacter freundii |
55 | - |
native enzyme, using L-tyrosine as a substrate | Citrobacter freundii |
60 | - |
mutant enzyme T15A, using L-tyrosine as a substrate | Citrobacter freundii |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
15 | 80 | at 18°C the enzyme activity is about 20% of the maximal activity, when heated for 20 min, the wild type enzyme remains stable up to 55°C in a 0.1 M potassium phosphate buffer (pH 8.0), the half-inactivation temperature is calculated to be 62.2°C | Citrobacter freundii |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.31 | - |
3,4-dihydroxyphenyl-L-alanine | wild type enzyme, in 0.1 M potassium phosphate buffer (pH 8.0) at 30°C | Citrobacter freundii | |
0.68 | - |
3,4-dihydroxyphenyl-L-alanine | mutant enzyme T15A, at 30°C | Citrobacter freundii | |
1.2 | - |
L-tyrosine | mutant enzyme T15A, in 0.1 M potassium phosphate buffer (pH 8.0) at 30°C | Citrobacter freundii | |
1.8 | - |
L-tyrosine | wild type enzyme, in 0.1 M potassium phosphate buffer (pH 8.0) at 30°C | Citrobacter freundii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | Km: 0.002 mM | Citrobacter freundii |