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Literature summary for 4.1.99.2 extracted from

  • Lee, S.G.; Hong, S.P.; Kim, D.Y.; Song, J.J.; Ro, H.S.; Sung, M.H.
    Inactivation of tyrosine phenol-lyase by Pictet-Spengler reaction and alleviation by T15A mutation on intertwined N-terminal arm (2006), FEBS J., 273, 5564-5573.
    View publication on PubMed
Search for more literature for 4.1.99.2

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli XL-1 Blue cells Citrobacter freundii

Protein Variants

Protein Variants Comment Organism
T15A exhibits a 2fold improved activity towards 3,4-dihydroxyphenyl-L-alanine Citrobacter freundii

Inhibitors

Inhibitors Comment Organism Structure
3,4-dihydroxyphenyl-L-alanine inactivated by a Pictet-Spengler reaction between the cofactor and 3,4-dihydroxyphenyl-L-alanine, on treatment with excess pyridoxal-5'-phosphate the inactivated enzymes recovers over 80% of the original activity Citrobacter freundii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.22
-
 L-tyrosine mutant enzyme T15A, in 0.1 M potassium phosphate buffer (pH 8.0) at 30°C Citrobacter freundii
0.24
-
 L-tyrosine wild type enzyme, in 0.1 M potassium phosphate buffer (pH 8.0) at 30°C Citrobacter freundii
3.2
-
 3,4-dihydroxyphenyl-L-alanine wild type enzyme, in 0.1 M potassium phosphate buffer (pH 8.0) at 30°C Citrobacter freundii
4.6
-
 3,4-dihydroxyphenyl-L-alanine mutant enzyme T15A, at 30°C Citrobacter freundii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
52000
-
 SDS-PAGE Citrobacter freundii

Organism

Organism UniProt Comment Textmining
Citrobacter freundii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Resource Q ion exchange chromatography and Phenyl Superose Phenyl Superose column chromatography Citrobacter freundii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3,4-dihydroxyphenyl-L-alanine + H2O
-
 Citrobacter freundii pyrocatechol + NH3 + pyruvate
-
 ?
L-tyrosine + H2O
-
 Citrobacter freundii phenol + pyruvate + NH3
-
 ?

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
 native enzyme, using 3,4-dihydroxyphenyl-L-alanine as a substrate Citrobacter freundii
45
-
 mutant enzyme T15A, using 3,4-dihydroxyphenyl-L-alanine as a substrate Citrobacter freundii
55
-
 native enzyme, using L-tyrosine as a substrate Citrobacter freundii
60
-
 mutant enzyme T15A, using L-tyrosine as a substrate Citrobacter freundii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
15 80 at 18°C the enzyme activity is about 20% of the maximal activity, when heated for 20 min, the wild type enzyme remains stable up to 55°C in a 0.1 M potassium phosphate buffer (pH 8.0), the half-inactivation temperature is calculated to be 62.2°C Citrobacter freundii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.31
-
 3,4-dihydroxyphenyl-L-alanine wild type enzyme, in 0.1 M potassium phosphate buffer (pH 8.0) at 30°C Citrobacter freundii
0.68
-
 3,4-dihydroxyphenyl-L-alanine mutant enzyme T15A, at 30°C Citrobacter freundii
1.2
-
 L-tyrosine mutant enzyme T15A, in 0.1 M potassium phosphate buffer (pH 8.0) at 30°C Citrobacter freundii
1.8
-
 L-tyrosine wild type enzyme, in 0.1 M potassium phosphate buffer (pH 8.0) at 30°C Citrobacter freundii

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate Km: 0.002 mM Citrobacter freundii