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Literature summary for 4.1.99.2 extracted from

  • Demidkina, T.V.; Faleev, N.G.; Papisova, A.I.; Bazhulina, N.P.; Kulikova, V.V.; Gollnick, P.D.; Phillips, R.S.
    Aspartic acid 214 in Citrobacter freundii tyrosine phenol-lyase ensures sufficient C--H-acidity of the external aldimine intermediate and proper orientation of the cofactor at the active site (2006), Biochim. Biophys. Acta, 1764, 1268-1276.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli SVS370 cells Citrobacter freundii

Protein Variants

Protein Variants Comment Organism
D214A mutant does not catalyze the decomposition of L-Tyr and 3-fluoro-L-Tyr Citrobacter freundii
D214N mutant does not catalyze the decomposition of L-Tyr and 3-fluoro-L-Tyr Citrobacter freundii

Inhibitors

Inhibitors Comment Organism Structure
L-Asp
-
Citrobacter freundii
L-Glu
-
Citrobacter freundii
L-homoserine
-
Citrobacter freundii
L-Met
-
Citrobacter freundii
L-Phe
-
Citrobacter freundii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.1
-
S-(o-nitrophenyl)-L-Cys wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
0.1
-
3-fluoro-L-Tyr wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
0.2
-
L-Tyr wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
0.2
-
S-benzyl-L-Cys wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
1.32
-
S-(o-nitrophenyl)-L-Cys mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
1.86
-
S-(o-nitrophenyl)-L-Cys mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
2
-
3-chloro-L-Ala wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
3.4
-
S-methyl-L-Cys wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
5.1
-
S-benzyl-L-Cys mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
7
-
S-benzyl-L-Cys mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
11.4
-
3-chloro-L-Ala mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
13.3
-
3-chloro-L-Ala mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
13.4
-
S-methyl-L-Cys mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
50
-
S-methyl-L-Cys mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii

Metals/Ions

Metals/Ions Comment Organism Structure
K+ activating Citrobacter freundii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
51400
-
4 * 51400 Citrobacter freundii

Organism

Organism UniProt Comment Textmining
Citrobacter freundii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation Citrobacter freundii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-chloro-L-Ala + H2O
-
Citrobacter freundii ?
-
?
3-fluoro-L-tyrosine + H2O
-
Citrobacter freundii 3-fluorophenol + pyruvate + NH3
-
?
L-tyrosine + H2O
-
Citrobacter freundii phenol + pyruvate + NH3
-
?
S-(o-nitrophenyl)-L-Cys + H2O
-
Citrobacter freundii ? + pyruvate + NH3
-
?
S-benzyl-L-Cys + H2O
-
Citrobacter freundii ? + pyruvate + NH3
-
?
S-methyl-L-Cys + H2O
-
Citrobacter freundii ? + pyruvate + NH3
-
?

Subunits

Subunits Comment Organism
homotetramer 4 * 51400 Citrobacter freundii

Synonyms

Synonyms Comment Organism
TPL
-
Citrobacter freundii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0016
-
S-methyl-L-Cys mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
0.0052
-
S-methyl-L-Cys mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
0.0065
-
3-chloro-L-Ala mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
0.0067
-
S-benzyl-L-Cys mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
0.02
-
3-chloro-L-Ala mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
0.02
-
S-benzyl-L-Cys mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
0.024
-
S-(o-nitrophenyl)-L-Cys mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
0.041
-
S-(o-nitrophenyl)-L-Cys mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
0.5
-
S-benzyl-L-Cys wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
0.7
-
3-chloro-L-Ala wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
0.9
-
S-methyl-L-Cys wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
1.4
-
3-fluoro-L-Tyr wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
3.5
-
L-Tyr wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
5.1
-
S-(o-nitrophenyl)-L-Cys wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii

Cofactor

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

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.73
-
L-Met wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C, using L-Tyr as a substrate Citrobacter freundii
0.73
-
L-Met wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C, using S-(o-nitrophenyl)-L-Cys as a substrate Citrobacter freundii
1.33
-
L-homoserine wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C, using L-Tyr as a substrate Citrobacter freundii
1.33
-
L-homoserine wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C, using S-(o-nitrophenyl)-L-Cys as a substrate Citrobacter freundii
1.7
-
L-Phe wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C, using L-Tyr as a substrate Citrobacter freundii
1.7
-
L-Phe wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C, using S-(o-nitrophenyl)-L-Cys as a substrate Citrobacter freundii
3
-
L-Asp mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
3.5
-
L-Asp wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C, using L-Tyr as a substrate Citrobacter freundii
3.5
-
L-Asp wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C, using S-(o-nitrophenyl)-L-Cys as a substrate Citrobacter freundii
3.6
-
L-Asp mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
4.2
-
L-Met mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
5
-
L-Glu wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C, using L-Tyr as a substrate Citrobacter freundii
5
-
L-Glu wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C, using S-(o-nitrophenyl)-L-Cys as a substrate Citrobacter freundii
11
-
L-Met mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
17
-
L-Phe mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
22
-
L-Phe mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
66
-
L-Glu mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
69
-
L-homoserine mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
82
-
L-homoserine mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii
100
-
L-Glu mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C Citrobacter freundii