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Literature summary extracted from
- Structures of apo- and holo-tyrosine phenol-lyase reveal a catalytically critical closed conformation and suggest a mechanism for activation by K+ ions (2006), Biochemistry, 45, 7544-7552.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 4.1.99.2 | hanging drop vapour diffusion method with 50 mM potassium phosphate (pH 8.0), 2 mM DTT, 0.2 M KCl, and 32.5% (w/v) PEG2000 for the apo-enzyme, and 50 mM triethanolamine buffer (pH 8.0), containing 0.5 mM PLP, 2 mM DTT, 0.4-0.8 M KCl, and 35-38% (w/v) PEG5000 for the holo-enzyme | Citrobacter freundii |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.1.99.2 | K+ | catalytically important | Citrobacter freundii |  |
| 4.1.99.2 | additional information | divalent cations (Mg2+, Ca2+, Ba2+, and Sr2+) do not activate TPL | Citrobacter freundii |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.1.99.2 | Citrobacter freundii | P31013 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.1.99.2 | - |
Citrobacter freundii |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.99.2 | L-tyrosine + H2O | - |
Citrobacter freundii | phenol + pyruvate + NH3 | - |
r | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.1.99.2 | tetramer | x-ray crystallography | Citrobacter freundii |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.1.99.2 | L-tyrosine phenol-lyase | - |
Citrobacter freundii |
| 4.1.99.2 | TPL | - |
Citrobacter freundii |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.1.99.2 | 8.2 | - |
- |
Citrobacter freundii |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.1.99.2 | 6 | - |
decrease of the enzymatic activity at pH 6.0 | Citrobacter freundii |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.1.99.2 | pyridoxal 5'-phosphate | - |
Citrobacter freundii | |
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Release 2023.1 (January 2023)
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