4.1.99.2: tyrosine phenol-lyase
This is an abbreviated version!
For detailed information about tyrosine phenol-lyase, go to the full flat file.
Word Map on EC 4.1.99.2
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4.1.99.2
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triptolide
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citrobacter
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threatened
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preterm
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two-photon
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luminescence
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freundii
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topless
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tripterygium
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wilfordii
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nitroxide
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quinonoid
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hook
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labour
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erwinia
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herbicola
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co-repressors
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nanorods
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tempol
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beta-elimination
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disaturated
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3,4-dihydroxyphenyl-l-alanine
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tryptophanase
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aldimine
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indole-lyase
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phillips
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tocolysis
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triepoxide
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synthesis
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photoluminescence
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degradation
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biotechnology
- 4.1.99.2
- triptolide
- citrobacter
-
threatened
-
preterm
-
two-photon
-
luminescence
- freundii
-
topless
- tripterygium
- wilfordii
-
nitroxide
-
quinonoid
-
hook
-
labour
- erwinia
- herbicola
-
co-repressors
-
nanorods
-
tempol
-
beta-elimination
-
disaturated
- 3,4-dihydroxyphenyl-l-alanine
- tryptophanase
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aldimine
-
indole-lyase
-
phillips
-
tocolysis
-
triepoxide
- synthesis
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photoluminescence
- degradation
- biotechnology
Reaction
Synonyms
beta-tyrosinase, Fn-TPL, L-tyrosine phenol-lyase, phenol-lyase, tyrosine, TnaA, TPL, tyrosine phenol lyase, tyrosine phenol-lyase, tyrosine-phenol lyase
ECTree
4.1.99.2 tyrosine phenol-lyaseAdvanced search results
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results (KM Value
KM Value on EC 4.1.99.2 - tyrosine phenol-lyase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
15.62
pyrocatechol
recombinant enzyme, L-DOPA formation is measured from dicatechol, pyruvate, and ammonium, pH 8.5, 20°C
3.2
3,4-dihydroxyphenyl-L-alanine
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wild type enzyme, in 0.1 M potassium phosphate buffer (pH 8.0) at 30°C
2
3-chloro-L-Ala
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wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C
11.4
3-chloro-L-Ala
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mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C
13.3
3-chloro-L-Ala
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mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C
0.1
3-fluoro-L-Tyr
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wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C
0.1
3-fluoro-L-tyrosine
recombinant wild-type enzyme, pH 8.0, 30°C
2.12
beta-chloro-L-alanine
recombinant wild-type enzyme, pH 8.0, 30°C
0.2
L-Tyr
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wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C
0.18
L-tyrosine
recombinant enzyme, pH 8.5, 20°C
0.22
L-tyrosine
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mutant enzyme T15A, in 0.1 M potassium phosphate buffer (pH 8.0) at 30°C
0.24
L-tyrosine
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wild type enzyme, in 0.1 M potassium phosphate buffer (pH 8.0) at 30°C
3.6
phenol
recombinant enzyme, L-tyrosine formation is measured from phenol, pyruvate, and ammonium, pH 8.5, 20°C
0.21
S-(2-nitrophenyl)-L-cysteine
recombinant wild-type enzyme, pH 8.0, 30°C
2.2
S-(2-nitrophenyl)-L-cysteine
recombinant mutant S51A, pH 8.0, 30°C
0.1
S-(o-nitrophenyl)-L-Cys
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wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C
1.32
S-(o-nitrophenyl)-L-Cys
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mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C
1.86
S-(o-nitrophenyl)-L-Cys
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mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C
0.2
S-benzyl-L-Cys
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wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C
5.1
S-benzyl-L-Cys
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mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C
7
S-benzyl-L-Cys
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mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C
0.12
S-Benzyl-L-cysteine
recombinant wild-type enzyme, pH 8.0, 30°C
1.57
S-ethyl-L-cysteine
recombinant wild-type enzyme, pH 8.0, 30°C
3.4
S-methyl-L-Cys
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wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C
13.4
S-methyl-L-Cys
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mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C
50
S-methyl-L-Cys
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mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C
2.32
S-methyl-L-cysteine
recombinant wild-type enzyme, pH 8.0, 30°C
additional information
additional information
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pH-independent kinetic constants for substrates bearing small substituents
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additional information
additional information
steady-state kinetics
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additional information
additional information
pre-steady state kinetics and steady state kinetic study, overview. TPL from Citrobacter freundii exhibits two basic pKas, with an average value of 7.8, in the pH dependence of kcat/Km, and kcat is pH-independent. The TPL reaction shows primary isotope effects of about 3 on kcat and 2 on kcat/Km for both enzymes, also suggesting that steps involving transfer of the alpha-proton are partially rate-limiting. The primary isotope effect increases to 5.4 and 3.8, respectively, for kcat and kcat/Km with alpha-[2H]-3-fluoro-L-tyrosine with H343A TPL, compared to 3.9 and 2.2 for wild-type TPL. Stopped-flow measurements, the reaction of TPL with L-tyrosine and 3-fluoro-L-tyrosine in the stopped-flow spectrophotometer also shows rapid formation of quinonoid intermediate
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additional information
additional information
pre-steady-state kinetic and steady-state kinetics, kinetic analysis of recombinant wild-type and mutant enzymes, stopped-flow kinetics of enzyme mutant F448A
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