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
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results (Reaction
Reaction on EC 4.1.99.2 - tyrosine phenol-lyase
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REACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
L-tyrosine + H2O = phenol + pyruvate + NH3
mechanism
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L-tyrosine + H2O = phenol + pyruvate + NH3
mechanism
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L-tyrosine + H2O = phenol + pyruvate + NH3
single-base racemization mechanism, proceeds with retention of configuration at C-beta
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L-tyrosine + H2O = phenol + pyruvate + NH3
mechanism appears to require two bases, one of which abstracts the proton from the 2-position of the substrate to form a quinonoid intermediate and the second of which acting in concert with proton transfer from the first group to C-1 of the phenolic ring, abstracts the substrate hydroxyl group to facilitate cyclohexadienone formation and subsequent elimination of phenol
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L-tyrosine + H2O = phenol + pyruvate + NH3
mechanism appears to require two bases, one of which abstracts the proton from the 2-position of the substrate to form a quinonoid intermediate and the second of which acting in concert with proton transfer from the first group to C-1 of the phenolic ring, abstracts the substrate hydroxyl group to facilitate cyclohexadienone formation and subsequent elimination of phenol
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L-tyrosine + H2O = phenol + pyruvate + NH3
NH3 is the first substrate which interacts with bound pyridoxal 5'-phosphate, pyruvate is the second substrate
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L-tyrosine + H2O = phenol + pyruvate + NH3
reversible cleavage of the Cbeta-Cgamma bond of L-tyrosine in the final stage of the beta-elimination, via intermediates: internal aldimine, external aldimine, quinoid, ketoquinoid, alpha-aminoacrylate, and internal aldimine, stepwise mechanism, overview
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L-tyrosine + H2O = phenol + pyruvate + NH3
an active site base is essential for activity, and alpha-deuterated substrate exhibits modest primary isotope effects on kcat and kcat/Km, suggesting that substrate deprotonation is partially rate-limiting. Pre-steady state kinetics with enzyme TPL show rapid formation of external aldimine intermediate, followed by deprotonation to give a quinonoid intermediate absorbing at about 500 nm. The mechanism of TPL requires both substrate strain and acid/base catalysis, and substrate strain is probably responsible for the very high substrate specificity of TPL. Acid-base catalysis mechanism of TPL, overview
L-tyrosine + H2O = phenol + pyruvate + NH3
mechanism of alpha,beta-elimination of L-tyrosine catalyzed by enzyme TPL
L-tyrosine + H2O = phenol + pyruvate + NH3
mechanism of alpha,beta-elimination of L-tyrosine catalyzed by enzyme TPL, detailed overview
L-tyrosine + H2O = phenol + pyruvate + NH3
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