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Literature summary for 4.1.99.2 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)

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

Inhibitors

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/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Citrobacter freundii P31013
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli strain SVS370/pTZTPL Citrobacter freundii

Substrates and Products (Substrate)

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

Synonyms Comment Organism
TPL
-
Citrobacter freundii
tyrosine phenol lyase
-
Citrobacter freundii

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

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

Ki Value [mM]

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