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Literature summary extracted from

  • Do, Q.; Nguyen, G.T.; Phillips, R.S.
    Inhibition of tyrosine phenol-lyase by tyrosine homologues (2016), Amino Acids, 48, 2243-2251 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.99.2 gene tpl, recombinant expression in Escherichia coli strain SVS370/pTZTPL Citrobacter freundii

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.99.2 L-bishomotyrosine
-
 Citrobacter freundii
4.1.99.2 L-homotyrosine
-
 Citrobacter freundii
4.1.99.2 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
4.1.99.2 O-methyl-L-bishomotyrosine
-
 Citrobacter freundii
4.1.99.2 O-methyl-L-homotyrosine
-
 Citrobacter freundii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.99.2 L-tyrosine + H2O Citrobacter freundii
-
 phenol + pyruvate + NH3
-
 r

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 recombinant enzyme from Escherichia coli strain SVS370/pTZTPL 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
4.1.99.2 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

EC Number Synonyms Comment Organism
4.1.99.2 TPL
-
 Citrobacter freundii
4.1.99.2 tyrosine phenol lyase
-
 Citrobacter freundii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.99.2 30
-
 assay at Citrobacter freundii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.99.2 8
-
 assay at Citrobacter freundii

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.99.2 pyridoxal 5'-phosphate dependent on Citrobacter freundii

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.1.99.2 additional information
-
 additional information rapid-scanning stopped-flow experiments, steady-state and pre-steady-state inhibition kinetics Citrobacter freundii
4.1.99.2 0.8
-
 L-homotyrosine pH 8.0, 30°C, recombinant enzyme Citrobacter freundii
4.1.99.2 0.8
-
 O-methyl-L-homotyrosine pH 8.0, 30°C, recombinant enzyme Citrobacter freundii
4.1.99.2 1.04
-
 O-methyl-L-bishomotyrosine pH 8.0, 30°C, recombinant enzyme Citrobacter freundii
4.1.99.2 1.5
-
 L-bishomotyrosine pH 8.0, 30°C, recombinant enzyme Citrobacter freundii