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
-
aldimine
-
indole-lyase
-
phillips
-
tocolysis
-
triepoxide
- synthesis
-
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
results (
results (KI Value
KI Value on EC 4.1.99.2 - tyrosine phenol-lyase
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Ki VALUE [mM] 
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
3
L-Asp
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mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C
3.5
L-Asp
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wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C, using L-Tyr as a substrate
3.5
L-Asp
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wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C, using S-(o-nitrophenyl)-L-Cys as a substrate
3.6
L-Asp
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mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C
5
L-Glu
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wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C, using L-Tyr as a substrate
5
L-Glu
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wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C, using S-(o-nitrophenyl)-L-Cys as a substrate
66
L-Glu
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mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C
100
L-Glu
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mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C
1.33
L-homoserine
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wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C, using L-Tyr as a substrate
1.33
L-homoserine
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wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C, using S-(o-nitrophenyl)-L-Cys as a substrate
69
L-homoserine
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mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C
82
L-homoserine
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mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C
0.73
L-Met
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wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C, using L-Tyr as a substrate
0.73
L-Met
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wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C, using S-(o-nitrophenyl)-L-Cys as a substrate
4.2
L-Met
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mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C
11
L-Met
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mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C
1.7
L-Phe
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wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C, using L-Tyr as a substrate
1.7
L-Phe
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wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C, using S-(o-nitrophenyl)-L-Cys as a substrate
17
L-Phe
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mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C
22
L-Phe
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mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C
additional information
additional information
rapid scanning stopped-flow kinetic experiments, kinetics
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additional information
additional information
rapid-scanning stopped-flow experiments, steady-state and pre-steady-state inhibition kinetics
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