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Literature summary for 4.1.99.2 extracted from

  • Phillips, R.S.; Chen, H.Y.; Shim, D.; Lima, S.; Tavakoli, K.; Sundararaju, B.
    Role of lysine-256 in Citrobacter freundii tyrosine phenol-lyase in monovalent cation activation (2004), Biochemistry, 43, 14412-14419.
    View publication on PubMed
Search for more literature for 4.1.99.2

Protein Variants

Protein Variants Comment Organism
E69D/K256R no activity with L-Tyr, turnover-number for S-(o-nitrophenyl)-L-cysteine is 1.5fold lower than the wild-type value, turnover-number for S-ethyl-L-Cys is 11fold lower than the wild-type value Citrobacter freundii
K256A turnover-number for L-Tyr is 3500fold lower than wild-type value, turnover-number for S-(o-nitrophenyl)-L-cysteine is 560fold lower than the wild-type value, turnover-number for S-ethyl-L-Cys is 1560fold lower than the wild-type value, activity is not increased by addition of monovalent cations, K+, Na+, Li+, Rb+, or NH4+ Citrobacter freundii
K256H turnover-number for L-Tyr is 26923fold lower than wild-type value, turnover-number for S-(o-nitrophenyl)-L-cysteine is 189fold lower than the wild-type value, turnover-number for S-ethyl-L-Cys is 443fold lower than the wild-type value, activity is not increased by addition of monovalent cations, K+, Na+, Li+, Rb+, or NH4+ Citrobacter freundii
K256R turnover-number for L-Tyr is 29fold lower than wild-type value, turnover-number for S-(o-nitrophenyl)-L-cysteine is 30fold lower than the wild-type value, turnover-number for S-ethyl-L-Cys is 195fold lower than the wild-type value Citrobacter freundii

Organism

Organism UniProt Comment Textmining
Citrobacter freundii P31013
-
-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.00013
-
 L-tyrosine pH 8.0, 25°C, mutant enzyme K256H Citrobacter freundii
0.001
-
 L-tyrosine pH 8.0, 25°C, mutant enzyme K256A Citrobacter freundii
0.0025
-
 S-ethyl-L-Cys pH 8.0, 25°C, mutant enzyme K256A Citrobacter freundii
0.0088
-
 S-ethyl-L-Cys pH 8.0, 25°C, mutant enzyme K256H Citrobacter freundii
0.0091
-
 S-(o-nitrophenyl)-L-cysteine pH 8.0, 25°C, mutant enzyme K256A Citrobacter freundii
0.02
-
 S-ethyl-L-Cys pH 8.0, 25°C, mutant enzyme K256R Citrobacter freundii
0.027
-
 S-(o-nitrophenyl)-L-cysteine pH 8.0, 25°C, mutant enzyme K256H Citrobacter freundii
0.12
-
 L-tyrosine pH 8.0, 25°C, mutant enzyme K256R Citrobacter freundii
0.17
-
 S-(o-nitrophenyl)-L-cysteine pH 8.0, 25°C, mutant enzyme K256R Citrobacter freundii
0.37
-
 S-ethyl-L-Cys pH 8.0, 25°C, mutant enzyme E69D/K256R Citrobacter freundii
7.4
-
 S-(o-nitrophenyl)-L-cysteine pH 8.0, 25°C, mutant enzyme E69D/K256R Citrobacter freundii