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
-
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
- 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 (Substrates Products
Substrates Products on EC 4.1.99.2 - tyrosine phenol-lyase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-amino-2-(4-hydroxyphenyl)-ethyl phosphinic acid + H2O
phenol + ?
-
-
-
?
2,5-difluorotyrosine + H2O
2,5-difluorophenol + pyruvate + NH3
-
-
-
?
2,6-difluorotyrosine + H2O
2,6-difluorophenol + pyruvate + NH3
-
-
-
?
2-fluorotyrosine + H2O
2-fluorophenol + pyruvate + NH3
-
-
-
?
3,4-dihydroxyphenyl-L-alanine + H2O
pyrocatechol + NH3 + pyruvate
-
-
-
-
?
3,5-difluorotyrosine + H2O
3,5-difluorophenol + pyruvate + NH3
-
-
-
?
3-chloro-L-tyrosine + H2O
?
-
substrate of mutant M379V, not of the wild-type enzyme
-
-
?
3-chlorotyrosine + H2O
3-chlorophenol + pyruvate + NH3
-
-
-
?
3-fluoro-L-tyrosine + H2O
3-fluoro-phenol + pyruvate + NH3
-
-
?
3-fluoro-L-tyrosine + H2O
?
-
substrate of mutant M379V, not of the wild-type enzyme
-
-
?
3-fluorotyrosine + H2O
3-fluorophenol + pyruvate + NH3
-
-
-
?
3-methoxy-L-tyrosine + H2O
?
-
substrate of mutant M379V, not of the wild-type enzyme
-
-
?
3-methyl-L-tyrosine + H2O
?
-
substrate of mutant M379V, not of the wild-type enzyme
-
-
?
L-Ala + pyridoxal phosphate
pyridoxamine phosphate + keto acid
-
-
-
-
ir
L-alanine + H2O
?
-
wild-type enzyme forms the Ala quinonoid intermediate when incubated with L-Ala
-
-
?
L-cysteine + H2O
thiophenol + pyruvate + NH3
12% of the activity with L-tyrosine
-
-
r
L-DOPA + H2O
pyrocatechol + pyruvate + NH4+
42% of the activity with L-tyrosine
-
-
r
L-m-Tyr + pyridoxal phosphate
pyridoxamine phosphate + keto acid
-
-
-
-
ir
L-Phe + pyridoxal phosphate
pyridoxamine phosphate + keto acid
-
-
-
-
ir
L-phenylalanine + H2O
? + pyruvate + NH3
7% of the activity with L-tyrosine
-
-
r
L-Ser + pyridoxal phosphate
pyridoxamine phosphate + keto acid
-
-
-
-
ir
L-serine + H2O
pyruvate + NH3
9% of the activity with L-tyrosine
-
-
r
L-valine + H2O
? + pyruvate + NH3
6% of the activity with L-tyrosine
-
-
r
o-chlorophenol + H2O
?
-
substrate of mutant M379V, not of the wild-type enzyme
-
-
?
o-cresol + H2O
?
-
substrate of mutant M379V, not of the wild-type enzyme
-
-
?
o-methoxyphenol + H2O
?
-
substrate of mutant M379V, not of the wild-type enzyme
-
-
?
phenol + pyruvate + NH3
L-tyrosine + H2O
-
-
-
r
S-ethyl-L-cysteine + H2O
ethanethiol + pyruvate + NH3
-
-
-
r
S-methyl-L-cysteine + H2O
?
Symbiobacterium sp.
-
385% of activity compared to L-tyrosine
-
?
S-methyl-L-cysteine + H2O
methanthiol + pyruvate + NH3
13% of the activity with L-tyrosine
-
-
r
3,4-dihydroxyphenyl-L-Ala + H2O
pyrocatechol + NH3 + pyruvate
-
-
-
?
3,4-dihydroxyphenyl-L-Ala + H2O
pyrocatechol + NH3 + pyruvate
-
i.e. L-dopa
-
?
3,4-dihydroxyphenyl-L-Ala + H2O
pyrocatechol + NH3 + pyruvate
-
i.e. L-dopa
-
?
3-fluoro-L-tyrosine + H2O
3-fluorophenol + pyruvate + NH3
-
-
-
-
?
3-fluoro-L-tyrosine + H2O
3-fluorophenol + pyruvate + NH3
-
-
-
r
3-fluoro-L-tyrosine + H2O
3-fluorophenol + pyruvate + NH3
3-fluoro-L-tyrosine also is a good substrate for the wild-type enzyme
-
-
r
beta-chloro-L-alanine + H2O
?
Symbiobacterium sp.
-
500% of activity compared to L-tyrosine
-
?
beta-chloro-L-alanine + H2O
?
-
500% of activity compared to L-tyrosine
-
?
catechol + pyruvate + NH3
3,4-dihydroxyphenyl-L-alanine
-
TPL is well-correlated to cytoplasmic 3,4-dihydroxyphenyl-L-alanine levels
-
-
r
catechol + pyruvate + NH3
3,4-dihydroxyphenyl-L-alanine
-
TPL is well-correlated to cytoplasmic 3,4-dihydroxyphenyl-L-alanine levels
-
-
r
D-tyrosine + H2O
phenol + pyruvate + NH3
Symbiobacterium sp.
-
at 7% the rate of L-tyrosine
-
?
D-tyrosine + H2O
phenol + pyruvate + NH3
-
at 7% the rate of L-tyrosine
-
?
L-2-aminoadipate + H2O
?
-
no activity with wild-type enzyme, activity with mutant enzyme R100T/V283R
-
-
?
L-2-aminoadipate + H2O
?
-
no activity with wild-type enzyme, activity with mutant enzyme R100T/V283R
-
-
?
L-3-4 dihydroxyphenylalanine + H2O
catechol + pyruvate + NH3
-
L-dopa
-
-
r
L-3-4 dihydroxyphenylalanine + H2O
catechol + pyruvate + NH3
-
L-DOPA, alpha-beta elimination
-
-
r
L-3-4 dihydroxyphenylalanine + H2O
catechol + pyruvate + NH3
-
L-dopa
-
-
r
L-Asp + H2O
formate + pyruvate + NH3
-
no activity with wild-type enzyme, activity with mutant enzyme R100T/V283R
-
?
L-Asp + H2O
formate + pyruvate + NH3
-
no activity with wild-type enzyme, activity with mutant enzyme R100T/V283R
-
?
L-Glu + H2O
?
-
no activity with wild-type enzyme, activity with mutant enzyme R100T/V283R
-
-
?
L-Glu + H2O
?
-
no activity with wild-type enzyme, activity with mutant enzyme R100T/V283R
-
-
?
L-Ser + phenol
L-Tyr + H2O
-
-
-
?
L-Ser + pyrocatechol
3,4-dihydroxyphenyl-L-Ala + H2O
-
-
i.e. L-dopa
?
L-Ser + pyrocatechol
3,4-dihydroxyphenyl-L-Ala + H2O
-
-
-
?
L-tryptophan + H2O
indole + pyruvate + NH3
8% of the activity with L-tyrosine, reaction of EC 4.1.99.1
-
-
r
L-tryptophan + H2O
indole + pyruvate + NH3
Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131
8% of the activity with L-tyrosine, reaction of EC 4.1.99.1
-
-
r
L-tyrosine + H2O
3,4-dihydroxyphenyl-L-alanine
-
TPL is well-correlated to cytoplasmic 3,4-dihydroxyphenyl-L-alanine levels
-
-
?
L-tyrosine + H2O
3,4-dihydroxyphenyl-L-alanine
-
TPL is well-correlated to cytoplasmic 3,4-dihydroxyphenyl-L-alanine levels
-
-
?
L-tyrosine + H2O
phenol + pyruvate + NH3
-
-
-
-
?
L-tyrosine + H2O
phenol + pyruvate + NH3
-
-
-
r
L-tyrosine + H2O
phenol + pyruvate + NH3
-
alpha-beta elimination
-
-
r
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, overview
-
-
r
L-tyrosine + H2O
phenol + pyruvate + NH3
very high substrate specificity of TPL
-
-
r
L-tyrosine + H2O
phenol + pyruvate + NH3
high activity with the wild-type enzyme
-
-
r
L-tyrosine + H2O
phenol + pyruvate + NH3
-
alpha-beta elimination
-
-
r
L-tyrosine + H2O
phenol + pyruvate + NH3
-
-
-
r
L-tyrosine + H2O
phenol + pyruvate + NH3
L-tyrosine is the physiological substrate of enzyme Fn-TPL
-
-
r
L-tyrosine + H2O
phenol + pyruvate + NH3
alpha,beta-elimination of L-tyrosine, best substrate
-
-
r
L-tyrosine + H2O
phenol + pyruvate + NH3
Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131
-
-
-
r
L-tyrosine + H2O
phenol + pyruvate + NH3
Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131
L-tyrosine is the physiological substrate of enzyme Fn-TPL
-
-
r
L-tyrosine + H2O
phenol + pyruvate + NH3
Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131
alpha,beta-elimination of L-tyrosine, best substrate
-
-
r
pyrocatechol + pyruvate + NH3
3,4-dihydroxyphenyl-L-Ala + H2O
-
-
-
?
pyrocatechol + pyruvate + NH3
3,4-dihydroxyphenyl-L-Ala + H2O
-
-
-
?
pyrocatechol + pyruvate + NH3
3,4-dihydroxyphenyl-L-Ala + H2O
-
-
-
?
pyrocatechol + pyruvate + NH4+
L-DOPA + H2O
-
-
-
r
pyrocatechol + pyruvate + NH4+
L-DOPA + H2O
Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131
-
-
-
r
S-(2-nitrophenyl)-L-cysteine + H2O
2-nitrobenzenethiolate + pyruvate + NH3
-
-
-
r
S-(2-nitrophenyl)-L-cysteine + H2O
2-nitrobenzenethiolate + pyruvate + NH3
best substrate for the wild-type enzyme
-
-
r
S-(o-nitrophenyl)-L-cysteine + H2O
?
Symbiobacterium sp.
-
250% of activity compared to L-tyrosine
-
?
S-(o-nitrophenyl)-L-cysteine + H2O
?
-
250% of activity compared to L-tyrosine
-
?
Tyr + H2O
phenol + pyruvate + NH3
-
L-Tyr
-
-
?
additional information
?
-
-
mechanism of alpha-proton isotope exchange in amino acids catalysed by tyrosine phenol-lyase
-
-
?
additional information
?
-
-
alanine, arginine, aspartate, cysteine, glutamine, glutamate, glycine, histidine, isoleucine, leucine, lysine, proline, serine, threonine, tryptophan are poor or no substrates, substrate specificity of purified tyrosine phenol lyase, overview
-
-
?
additional information
?
-
-
substrate 3-fluoro-L-tyrosine is converted only to the quinoid reaction intermediate, structure determination of 3-fluoro-L-tyrosine bound to enzyme mutant Y71F with open active site and mutant F448H with closed active site, overview
-
-
?
additional information
?
-
-
substrate specificity with 3-substituted tyrosines, the wild-type enzyme shows a narrow substrate spectrum, overview. Mutant M379V converts several L-tyrosine derivatives to the correspondent products
-
-
?
additional information
?
-
fragment of active site structure of the quinonoid complex of wild-type enzyme TPL with L-alanine, overview
-
-
?
additional information
?
-
of the common S-alkyl-L-cysteine substrates, S-ethyl-L-cysteine has the most favorable kinetic properties with TPL
-
-
?
additional information
?
-
tyrosine phenol-lyase is a pyridoxal 5'-phosphate (PLP)-dependent bacterial enzyme that catalyzes the reversible hydrolytic cleavage of the Cbeta-Cgamma bond of L-Tyr to phenol and ammonium pyruvate. In addition to its physiological substrate L-Tyr, TPL also catalyzes the in vitro beta-elimination of substrates with good leaving groups on the beta-carbon, including L-serine, L-cysteine, S-(2-nitrophenyl)-L-cysteine, O-acetyl-L-serines, and S-alkyl-L-cysteines
-
-
?
additional information
?
-
-
adaptive enzyme responsible for cells' growth on media with L-Tyr as the sole source of carbon
-
-
?
additional information
?
-
low activity of Fn-TPL is observed toward natural amino acids including L-serine, L-cysteine, L-phenylalanine, L-valine, L-tryptophan, no activity with L-threonine, L-glutamine, L-alanine, D-alanine, L-arginine, L-leucine, L-histidine, L-aspartic acid, L-methionine, and D-methionine
-
-
?
additional information
?
-
Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131
low activity of Fn-TPL is observed toward natural amino acids including L-serine, L-cysteine, L-phenylalanine, L-valine, L-tryptophan, no activity with L-threonine, L-glutamine, L-alanine, D-alanine, L-arginine, L-leucine, L-histidine, L-aspartic acid, L-methionine, and D-methionine
-
-
?
