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Literature summary for 4.1.99.2 extracted from

  • Phillips, R.S.; Demidkina, T.V.; Faleev, N.G.
    Structure and mechanism of tryptophan indole-lyase and tyrosine phenol-lyase (2003), Biochim. Biophys. Acta, 1647, 167-172.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
F448H very low activity with L-tyrosine, reduced activity with other substrates Citrobacter freundii
R381A dramatic decrease in activity with L-tyrosine, but little effect on activity with other substrates Citrobacter freundii
R381I dramatic decrease in activity with L-tyrosine, but little effect on activity with other substrates Citrobacter freundii
R381V dramatic decrease in activity with L-tyrosine, but little effect on activity with other substrates Citrobacter freundii
T124A dramatic decrease in activity with L-tyrosine Citrobacter freundii
T124D no detectable activity with L-tyrosine, but significant activity with other substrates with good leaving groups Citrobacter freundii
Y71F no detectable activity with L-tyrosine, but significant activity with other substrates with good leaving groups Citrobacter freundii

Inhibitors

Inhibitors Comment Organism Structure
L-phenylalanine
-
Citrobacter freundii
L-tryptophan
-
Citrobacter freundii
L-tyrosine
-
Citrobacter freundii

Organism

Organism UniProt Comment Textmining
Citrobacter freundii
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-chloro-L-alanine + H2O
-
Citrobacter freundii ?
-
r
L-tyrosine + H2O
-
Citrobacter freundii phenol + pyruvate + NH3
-
r
S-(o-nitrophenyl)-L-cysteine + H2O
-
Citrobacter freundii ?
-
r
S-ethyl-L-cysteine + H2O
-
Citrobacter freundii ?
-
?