Information on EC 4.1.99.2 - tyrosine phenol-lyase

New: Word Map on EC 4.1.99.2
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
4.1.99.2
-
RECOMMENDED NAME
GeneOntology No.
tyrosine phenol-lyase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-tyrosine + H2O = phenol + pyruvate + NH3
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha,beta-elimination
beta-elimination
-
-
racemization
transamination
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
tyrosine metabolism
-
-
Tyrosine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
L-tyrosine phenol-lyase (deaminating; pyruvate-forming)
A pyridoxal-phosphate protein. The enzyme cleaves a carbon-carbon bond, releasing phenol and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. The enzyme also slowly catalyses similar reactions with D-tyrosine, S-methyl-L-cysteine, L-cysteine, L-serine and D-serine.
CAS REGISTRY NUMBER
COMMENTARY hide
9059-31-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Aeromonas phenologenes
ATCC 29063
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
NRRL B-2643
-
-
Manually annotated by BRENDA team
SV370
-
-
Manually annotated by BRENDA team
ATCC21434
-
-
Manually annotated by BRENDA team
Pantoea agglomerans NRRL B-3466
NRRL B-3466
-
-
Manually annotated by BRENDA team
Pseudomonas pelurida
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Pseudomonas trifolii
-
-
-
Manually annotated by BRENDA team
Symbiobacterium sp.
Symbiobacterium sp. SMH1
SMH1
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
tyrosine phenol lyase catalyses the biosynthesis of L-tyrosine/L-DOPA from ammonium, pyruvate and phenolic substrates through the reverse of alpha- and beta-elimination reaction
physiological function
-
hyper-3,4-dihydroxyphenyl-L-alanine-producing strain by a mutant TyrR, an activator of tpl, whereby highest productivity is obtained for the strain grown under non-induced conditions, which is 30fold higher than that obtained for tyrosine-induced wild-type cells
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-amino-2-(4-hydroxyphenyl)-ethyl phosphinic acid + H2O
phenol + ?
show the reaction diagram
-
-
-
?
2,5-difluorotyrosine + H2O
2,5-difluorophenol + pyruvate + NH3
show the reaction diagram
-
-
-
?
2,6-difluorotyrosine + H2O
2,6-difluorophenol + pyruvate + NH3
show the reaction diagram
-
-
-
?
2-bromo-L-Tyr + H2O
2-bromophenol + pyruvate + NH3
show the reaction diagram
-
-
-
r
2-bromophenol + pyruvate + NH3
2-bromo-L-Tyr + H2O
show the reaction diagram
-
-
-
r
2-chloro-L-Tyr + H2O
2-chlorophenol + pyruvate + NH3
show the reaction diagram
2-chlorophenol + pyruvate + NH3
2-chloro-L-Tyr + H2O
show the reaction diagram
-
-
-
r
2-fluoro-L-Tyr + H2O
2-fluorophenol + pyruvate + NH3
show the reaction diagram
2-fluorophenol + pyruvate + NH3
2-fluoro-L-Tyr + H2O
show the reaction diagram
-
-
-
r
2-fluorotyrosine + H2O
2-fluorophenol + pyruvate + NH3
show the reaction diagram
-
-
-
?
2-methoxy-L-Tyr + H2O
2-methoxyphenol + pyruvate + NH3
show the reaction diagram
-
-
-
r
2-methoxyphenol + pyruvate + NH3
2-methoxy-L-Tyr + H2O
show the reaction diagram
-
-
-
r
2-methyl-L-Tyr + H2O
2-methylphenol + pyruvate + NH3
show the reaction diagram
-
-
-
r
2-methylphenol + pyruvate + NH3
2-methyl-L-Tyr + H2O
show the reaction diagram
-
-
-
r
3,4-dihydroxyphenyl-L-Ala + H2O
pyrocatechol + NH3 + pyruvate
show the reaction diagram
3,4-dihydroxyphenyl-L-alanine
?
show the reaction diagram
Symbiobacterium sp.
-
-
-
?
3,4-dihydroxyphenyl-L-alanine + H2O
pyrocatechol + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
3,5-difluorotyrosine + H2O
3,5-difluorophenol + pyruvate + NH3
show the reaction diagram
-
-
-
?
3-bromo-L-Tyr + H2O
3-bromophenol + pyruvate + NH3
show the reaction diagram
-
-
-
r
3-bromo-L-tyrosine + H2O
3-bromophenol + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
3-bromophenol + pyruvate + NH3
3-bromo-L-Tyr + H2O
show the reaction diagram
-
-
-
r
3-chloro-L-Ala + H2O
?
show the reaction diagram
3-chloro-L-Tyr + H2O
3-chlorophenol + pyruvate + NH3
show the reaction diagram
-
-
-
r
3-chloro-L-tyrosine + H2O
3-chlorophenol + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
3-chloro-L-tyrosine + H2O
?
show the reaction diagram
-
substrate of mutant M379V, not of the wild-type enzyme
-
-
?
3-chlorophenol + pyruvate + NH3
3-chloro-L-Tyr + H2O
show the reaction diagram
-
-
-
r
3-chlorotyrosine + H2O
3-chlorophenol + pyruvate + NH3
show the reaction diagram
-
-
-
?
3-fluoro-L-Tyr + H2O
3-fluorophenol + pyruvate + NH3
show the reaction diagram
3-fluoro-L-tyrosine
3-fluorophenol + pyruvate + NH3
show the reaction diagram
-
-
-
?
3-fluoro-L-tyrosine + H2O
3-fluoro-phenol + pyruvate + NH3
show the reaction diagram
-
-
?
3-fluoro-L-tyrosine + H2O
3-fluorophenol + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
3-fluoro-L-tyrosine + H2O
?
show the reaction diagram
-
substrate of mutant M379V, not of the wild-type enzyme
-
-
?
3-fluorophenol + pyruvate + NH3
3-fluoro-L-Tyr + H2O
show the reaction diagram
-
-
-
r
3-fluorotyrosine + H2O
3-fluorophenol + pyruvate + NH3
show the reaction diagram
-
-
-
?
3-iodo-L-tyrosine + H2O
3-iodophenol + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
3-methoxy-L-tyrosine + H2O
?
show the reaction diagram
-
substrate of mutant M379V, not of the wild-type enzyme
-
-
?
3-methyl-L-Tyr + H2O
3-methylphenol + pyruvate + NH3
show the reaction diagram
-
-
-
r
3-methyl-L-tyrosine + H2O
?
show the reaction diagram
-
substrate of mutant M379V, not of the wild-type enzyme
-
-
?
3-methylphenol + pyruvate + NH3
3-methyl-L-Tyr + H2O
show the reaction diagram
-
-
-
r
Ala + H2O
?
show the reaction diagram
allothreonine + ?
Gly + ?
show the reaction diagram
-
-
-
-
beta-chloro-L-alanine
?
show the reaction diagram
beta-chloro-L-alanine + H2O
?
show the reaction diagram
catechol + pyruvate + NH3
3,4-dihydroxyphenyl-L-alanine
show the reaction diagram
catechol + pyruvate + NH3
L-dihydroxyphenylalanine
show the reaction diagram
catechol + pyruvic acid
L-dopa + H2O
show the reaction diagram
-
-
-
-
-
D-serine + H2O
?
show the reaction diagram
Symbiobacterium sp.
-
at 11% the rate of L-tyrosine
-
?
D-tyrosine + H2O
phenol + pyruvate + NH3
show the reaction diagram
L-2-aminoadipate + H2O
?
show the reaction diagram
L-3-4 dihydroxyphenylalanine + H2O
catechol + pyruvate + NH3
show the reaction diagram
L-Ala + pyridoxal phosphate
pyridoxamine phosphate + keto acid
show the reaction diagram
-
-
-
-
ir
L-alanine + H2O
?
show the reaction diagram
-
wild-type enzyme forms the Ala quinonoid intermediate when incubated with L-Ala
-
-
?
L-Asp + H2O
formate + pyruvate + NH3
show the reaction diagram
L-asparagine + H2O
?
show the reaction diagram
-
-
-
-
?
L-Cys + H2O
? + pyruvate + NH3
show the reaction diagram
L-cysteine + H2O
?
show the reaction diagram
L-cystine + H2O
? + pyruvate + NH3
show the reaction diagram
L-Glu + H2O
?
show the reaction diagram
L-m-Tyr + pyridoxal phosphate
pyridoxamine phosphate + keto acid
show the reaction diagram
-
-
-
-
ir
L-Met + H2O
?
show the reaction diagram
-
-
-
-
?
L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
L-Phe + H2O
?
show the reaction diagram
L-Phe + pyridoxal phosphate
pyridoxamine phosphate + keto acid
show the reaction diagram
-
-
-
-
ir
L-phenylalanine + H2O
?
show the reaction diagram
-
low activity
-
-
?
L-Ser + phenol
L-Tyr + H2O
show the reaction diagram
L-Ser + pyridoxal phosphate
pyridoxamine phosphate + keto acid
show the reaction diagram
-
-
-
-
ir
L-Ser + pyrocatechol
3,4-dihydroxyphenyl-L-Ala + H2O
show the reaction diagram
L-serine + H2O
?
show the reaction diagram
Symbiobacterium sp.
-
-
-
?
L-Tyr + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-tyrosine + H2O
3,4-dihydroxyphenyl-L-alanine
show the reaction diagram
L-tyrosine + H2O
phenol + pyruvate + NH3
show the reaction diagram
L-valine + H2O
?
show the reaction diagram
-
-
-
-
?
O-benzoyl-L-Ser + H2O
?
show the reaction diagram
O-benzyl-L-Ser + H2O
?
show the reaction diagram
-
-
-
?
o-chlorophenol + H2O
?
show the reaction diagram
-
substrate of mutant M379V, not of the wild-type enzyme
-
-
?
o-cresol + H2O
?
show the reaction diagram
-
substrate of mutant M379V, not of the wild-type enzyme
-
-
?
o-methoxyphenol + H2O
?
show the reaction diagram
-
substrate of mutant M379V, not of the wild-type enzyme
-
-
?
phenol + pyruvate + NH3
Tyr + H2O
show the reaction diagram
pyrocatechol + pyruvate + NH3
3,4-dihydroxyphenyl-L-Ala + H2O
show the reaction diagram
resorcinol + pyruvate + NH3
2,4-dihydroxyphenyl-L-Ala
show the reaction diagram
-
-
-
?
S-(2-nitrophenyl)-L-cysteine
?
show the reaction diagram
-
-
-
-
?
S-(o-nitrophenyl)-L-Cys + H2O
?
show the reaction diagram
-
-
-
-
-
S-(o-nitrophenyl)-L-Cys + H2O
? + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
S-(o-nitrophenyl)-L-cysteine
?
show the reaction diagram
S-(o-nitrophenyl)-L-cysteine + H2O
?
show the reaction diagram
S-benzyl-L-Cys + H2O
? + pyruvate + NH3
show the reaction diagram
S-benzyl-L-cysteine
?
show the reaction diagram
S-benzyl-L-cysteine
? + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
S-ethyl-L-Cys + H2O
?
show the reaction diagram
-
-
-
-
?
S-ethyl-L-cysteine
?
show the reaction diagram
S-ethyl-L-cysteine
? + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
S-ethyl-L-cysteine + H2O
?
show the reaction diagram
-
-
-
?
S-methyl-L-Cys + H2O
? + pyruvate + NH3
show the reaction diagram
S-methyl-L-cysteine
?
show the reaction diagram
S-methyl-L-cysteine
? + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
S-methyl-L-cysteine + H2O
?
show the reaction diagram
Symbiobacterium sp.
-
385% of activity compared to L-tyrosine
-
?
S-o-nitrophenyl-L-cysteine + H2O
?
show the reaction diagram
-
-
-
-
?
Ser + H2O
? + pyruvate + NH3
show the reaction diagram
Thr + ?
2-oxobutanoate + ?
show the reaction diagram
Tyr + H2O
phenol + pyruvate + NH3
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-3-4 dihydroxyphenylalanine + H2O
catechol + pyruvate + NH3
show the reaction diagram
L-tyrosine + H2O
phenol + pyruvate + NH3
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
divalent cations (Mg2+, Ca2+, Ba2+, and Sr2+) do not activate TPL
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-dihydroxybenzene
-
cleavage of Tyr
1,3-dihydroxybenzene
-
cleavage of Tyr
1-amino-2-(4-hydroxyphenyl)-ethyl phosphinic acid
-
-
1-amino-2-(4-hydroxyphenyl)-ethyl phosphonic acid
-
-
2-Aminophenol
-
cleavage of Tyr
2-aza-L-tyrosine
-
competitive
2-bromophenol
-
cleavage of Tyr
2-chlorophenol
-
cleavage of Tyr
2-Fluorophenol
-
cleavage of Tyr
2-iodophenol
-
cleavage of Tyr
2-Methylphenol
-
cleavage of Tyr
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
3-Aminophenol
-
cleavage of Tyr
3-aza-L-tyrosine
-
competitive
3-bromophenol
-
cleavage of Tyr
3-chlorophenol
-
cleavage of Tyr
3-Fluorophenol
-
cleavage of Tyr
3-iodophenol
-
cleavage of Tyr
3-methylphenol
-
cleavage of Tyr
4-Aminophenol
-
cleavage of Tyr
4-hydroxypyridine
-
cleavage of Tyr
D-Ala
-
competitive
L-homoserine
-
-
L-m-Tyr
-
competitive
L-phenylalanine
per(2,3,6-tri-O-methyl)-alpha-cyclodextrin
-
non-competitive
per(2,3,6-tri-O-methyl)-beta-cyclodextrin
-
non-competitive
per(2,3,6-tri-O-methyl)-gamma-cyclodextrin
-
non-competitive
Phenol
pyrocatechol
-
inhibits pyruvate formation from L-Tyr, mixed type
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.08
1-amino-2-(4-hydroxyphenyl)-ethyl phosphinic acid
-
pH 9.0
3.5
2-bromo-L-Tyr
-
-
0.7
2-Chloro-L-Tyr
-
-
0.35
2-fluoro-L-Tyr
-
-
1.6
2-methoxy-L-Tyr
-
-
3.7
2-Methyl-L-Tyr
-
-
3.2 - 9.9
3,4-dihydroxyphenyl-L-alanine
1.4
3-bromo-L-Tyr
-
-
1.7 - 46
3-chloro-L-Ala
3
3-Chloro-L-Tyr
-
-
0.1 - 1.2
3-fluoro-L-Tyr
4.1
3-methyl-L-Tyr
-
-
6.1
Ala
-
beta-elimination
12
beta-chloro-L-alanine
Symbiobacterium sp.
-
pH 7.2, 60C
40
catechol
-
-
32
D-Ala
11 - 103
L-Ala
0.21 - 54
L-Asp
5.3
L-Glu
-
mutant enzyme R100T/V283R
0.94
L-m-Tyr
-
transamination
0.0915
L-Met
-
-
0.196 - 2
L-Phe
11 - 28.6
L-Ser
0.054 - 2.2
L-Tyr
0.19 - 0.446
L-tyrosine
0.8 - 2.9
O-benzoyl-L-Ser
0.21
p-L-Tyr
-
-
4.15
Phe
-
beta-elimination
5.1 - 110
pyruvate
0.1 - 1.86
S-(o-nitrophenyl)-L-Cys
0.27 - 0.36
S-(o-nitrophenyl)-L-cysteine
0.05 - 7
S-benzyl-L-Cys
0.3 - 6.6
S-ethyl-L-Cys
0.52 - 56.4
S-methyl-L-Cys
3.2 - 5.5
S-methyl-L-cysteine
34 - 51
Ser
0.24
Tyr
-
beta-elimination
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.31 - 0.68
3,4-dihydroxyphenyl-L-alanine
0.0065 - 3
3-chloro-L-Ala
0.18 - 1.4
3-fluoro-L-Tyr
0.00153
Ala
Citrobacter intermedius
-
beta-elimination
0.004 - 0.01
D-Ala
0.03
L-Ala
Citrobacter freundii
-
wild-type enzyme
0.00268
L-m-Tyr
Citrobacter intermedius
-
transamination
0.015
L-Met
Citrobacter freundii
-
-
0.748 - 6.08
L-Phe
0.07 - 0.17
L-Ser
0.11 - 3.7
L-Tyr
0.00013 - 1.8
L-tyrosine
0.15 - 8.3
O-benzoyl-L-Ser
3.9
O-benzyl-L-Cys
Citrobacter freundii
P31013
wild-type enzyme
-
0.0008
Phe
Citrobacter intermedius
-
beta-elimination
0.024 - 9.7
S-(o-nitrophenyl)-L-Cys
0.0091 - 7.4
S-(o-nitrophenyl)-L-cysteine
0.02
S-benzoyl-L-Cys
Citrobacter freundii
-
mutant enzyme H343A
0.0012 - 0.52
S-benzyl-L-Cys
0.000217 - 3.88
S-ethyl-L-Cys
0.000383 - 0.9
S-methyl-L-Cys
0.001 - 0.012
Ser
0.2
Tyr
Citrobacter intermedius
-
beta-elimination
additional information
additional information
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.44
1-amino-2-(4-hydroxyphenyl)-ethyl phosphinic acid
-
-
100
1-amino-2-(4-hydroxyphenyl)-ethyl phosphonic acid
-
-
0.135 - 3.4
2-aza-L-tyrosine
3 - 3.6
L-Asp
5 - 100
L-Glu
1.33 - 82
L-homoserine
0.73 - 11
L-Met
1.7 - 22
L-Phe
2
L-phenylalanine
-
pH 8.0, 30C
7
L-tryptophan
-
pH 8.0, 30C
0.2
L-tyrosine
-
pH 8.0, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0022
-
in strain S12TPL3-delta-hpd mutant (4-hydroxyphenylpyruvate dioxygenase knockout), harvested in logarithmic phase
0.0053
-
in strain S12TPL3, in presence of 1 mM phenol
0.0078
-
in strain S12TPL3, harvested in logarithmic phase
0.017
-
at the 24 h culture phase, wild-type strain
0.0232
-
in strain S12TPL3, without phenol
0.031
-
at the 24 h culture phase, wild-type strain
0.032
-
at the 12 h culture phase, wild-type strain
0.058
-
at the 12 h culture phase, vgb- strain
0.067
-
at the 24 h culture phase, vgb- strain
0.08
-
at the 12 h culture phase, vgb+ strain
0.098
-
at the 24 h culture phase, vgb- strain
0.371
-
at the 24 h culture phase, vgb+ strain
0.513
-
at the 24 h culture phase, vgb+ strain
1.1
-
purified enzyme, pH 8.5, 30C
2.8
Aeromonas phenologenes
-
-
10
-
pH 7.8, 30C
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
Symbiobacterium sp.
-
-
8 - 9
-
phenol as substrate
8.5 - 9
-
synthesis of L-Tyr from pyruvate, ammonia and phenol
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9.2
Symbiobacterium sp.
-
pH 6.5: about 45% of maximal activity, pH 9.2: about 40% of maximal activity
7 - 9.5
Aeromonas phenologenes
-
pH 7.0: about 25% of maximal activity, pH 9.5: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
native enzyme, using 3,4-dihydroxyphenyl-L-alanine as a substrate
55
-
native enzyme, using L-tyrosine as a substrate
55 - 60
Symbiobacterium sp.
-
-
60
-
mutant enzyme T15A, using L-tyrosine as a substrate
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 55
-
activity range, profile, overview
37 - 75
Symbiobacterium sp.
-
37C: about 65% of maximal activity, 75C: about 45% of maximal activity
60 - 85
-
about 35% of maximal activity at 60C and 85C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
Symbiobacterium sp.
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
wild-type S12 and its mutant strains S12TPL3 (optimized for phenol production)
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
-
SDS-PAGE
159000
-
calculation from diffusion and sedimentation data
200000
-
gel filtration
202000
Symbiobacterium sp.
-
gel filtration
220000
-
native enzyme, native PAGE
380000
Aeromonas phenologenes
-
gel filtration, nnon-denaturing PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
tetramer
additional information
-
N-terminal sequences comparisons, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method with 50 mM potassium phosphate (pH 8.0), 2 mM DTT, 0.2 M KCl, and 32.5% (w/v) PEG2000 for the apo-enzyme, and 50 mM triethanolamine buffer (pH 8.0), containing 0.5 mM PLP, 2 mM DTT, 0.4-0.8 M KCl, and 35-38% (w/v) PEG5000 for the holo-enzyme
-
in complex with L-methionine and L-phenylalanine, wild type and mutant Y71F
-
purified wild-type enzyme in ternary complex with pyridine N-oxide and the L-Ala quinonoid reaction intermediate by soaking wild-type TPL crystals in the stabilization solution containing 40% w/v PEG 5000 MME, 50 mM triethanolamine, pH 8.0, 0.25 M KCl, 0.2 mM pyridoxal 5'-phosphate, 0.5 mM dithiothreitol, with 100 mM L-Ala and a saturating concentration of pyridine N-oxide for 20 s, and purified Y71F or F448H mutant enzymes with bound substrate in quinoid intermediate state by soaking the crystals in the same stabilizing solution but with addition of 10 mM 3-fluoro-L-Tyr for 30 s, X-ray diffraction structure determination and analysis at 2.05-2.25 A resolution
-
the quinonoid intermediates of tyrosine phenol-lyase with L-alanine and L-methionine are trapped in the crystalline state and their structures are determined at 1.9 A and 1.95 A resolution, respectively
-
tyrosine phenol-lyase complexed with 3-(4'-hydroxyphenyl)propionic acid
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
decrease of the enzymatic activity at pH 6.0
678198
6 - 11
-
25C, 48 h
33465
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 80
-
at 18C the enzyme activity is about 20% of the maximal activity, when heated for 20 min, the wild type enzyme remains stable up to 55C in a 0.1 M potassium phosphate buffer (pH 8.0), the half-inactivation temperature is calculated to be 62.2C
35
-
purified native enzyme, half-life is 130 min
45
-
purified native enzyme, half-life is 52 min
55
-
purified native enzyme, half-life is 10 min
60
Aeromonas phenologenes
-
10 min, about 45% loss of activity
85
-
20 min, about 25% loss of activity
90
-
20 min, about 90% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
liposomal encapsulation increases stability of the enzyme at 4C for 3 weeks and at temperatures up to 61C, little protection against trypsin and no protection against whole mouse plasma in vitro
-
mutant enzyme A13V loses 50% of its catalytic activity in 3 M urea, wild-type enzyme completely loses activity
-
not stable to freezing and thawing
Aeromonas phenologenes
-
the enzyme maintains its original activity at phenol concentrations below 75 mM
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
2C, 0.02 M phosphate buffer + mercaptoethanol, pH 7.0, 1 week, 50% loss of activity
Aeromonas phenologenes
-
40C, in the presence of 75 mM phenol at pH 8.5, 18h, no loss of activity
-
4C, 3 days, negligible activity after 3 days
-
stable against 0.2% sodium dodecylsulfate
Symbiobacterium sp.
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation
-
mutant enzyme A13V
-
mutant enzyme His343Ala
-
native enzyme 35fold to homogeneity by ammonium sulfate fractionation, dialysis, and hydrophobic interaction chromatography
-
partial
partial purification by methanol treatment
-
Resource Q ion exchange chromatography and Phenyl Superose Phenyl Superose column chromatography
-
wild-type protein and mutants T451A/A13V/E83K and T129I/A13V purified to homogeneity with purification yields of over 40%
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli strain BL21
-
expressed in Escherichia coli SVS370 cells
-
expressed in Escherichia coli XL-1 Blue cells
-
expression in Escherichia coli
expression in Escherichia coli, fusion to the lac and tac promoters, erpressed at high levels in the presence of isopropyl-beta-D-thiogalactopyranoside or lactose as inducer
-
gene tpl, expression of wild-type and mutant enzymes in Escherichia coli strain SVS 370
-
plasmid pHCE IIB-TPL ligated at 4C for 24 h with a T4 DNA ligase, products electrotransformed into Escherichia coli JM83
-
Targeted gene disruptions are performed. Gene replacement vectors for the hpd, pobA, phhA, and aroP1 genes are created from pJQ200SK with different primers. Vectors are used to mutate the selected genes in Pseudomonas putida S12TPL3c by homologous recombination.
-
the plasmid pTZTPL is constructed for expression of the protein in Escherichia coli SVS370 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
L-tyrosine addition only has a positive effect in terms of TPL induction for cell cultures harvested after 12 h
L-tyrosine induces the enzyme, liquid paraffin as oxygen vector has a stimulatory effect on the enzyme synthesis
TyrR is the transcriptional activator of Tpl. Amino acid substitutions of TyrR, V67A, Y72C and E201G in the N-terminal domain, N324D in the central domain, A503T in the C-terminal domain, all enhance Tpl expression
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D214A
-
mutant does not catalyze the decomposition of L-Tyr and 3-fluoro-L-Tyr
D214N
-
mutant does not catalyze the decomposition of L-Tyr and 3-fluoro-L-Tyr
E69D/K256R
-
no activity with L-Tyr, turnover-number for S-(o-nitrophenyl)-L-cysteine is 1.5fold lower than the wild-type value, turnover-number for S-ethyl-L-Cys is 11fold lower than the wild-type value
F36V
-
changed substrate specificity
F448V
-
changed substrate specificity
H343A
-
all substrates for alpha,beta-elimination, except S-ethyl-L-Cys, exhibit lower turnover number values with the mutant enzyme than with the wild-type enzyme. The mutant shows slower rates of deuterium isotope exchange for L-Phe and L-Met than does the wild type enzyme. The turnover-number for 3-fluoro-L-Tyr is pH-dependent for the mutant enzyme, whereas it is pH-independent for the wild-type enzyme. His343 does play an important function in catalysis, possibly by facilitating the conformational change from an open' to closed' form when substrates bind
K256A
-
turnover-number for L-Tyr is 3500fold lower than wild-type value, turnover-number for S-(o-nitrophenyl)-L-cysteine is 560fold lower than the wild-type value, turnover-number for S-ethyl-L-Cys is 1560fold lower than the wild-type value, activity is not increased by addition of monovalent cations, K+, Na+, Li+, Rb+, or NH4+
K256H
-
turnover-number for L-Tyr is 26923fold lower than wild-type value, turnover-number for S-(o-nitrophenyl)-L-cysteine is 189fold lower than the wild-type value, turnover-number for S-ethyl-L-Cys is 443fold lower than the wild-type value, activity is not increased by addition of monovalent cations, K+, Na+, Li+, Rb+, or NH4+
K256R
-
turnover-number for L-Tyr is 29fold lower than wild-type value, turnover-number for S-(o-nitrophenyl)-L-cysteine is 30fold lower than the wild-type value, turnover-number for S-ethyl-L-Cys is 195fold lower than the wild-type value
M288V
-
changed substrate specificity
M379V
-
changed substrate specificity; site-directed mutagenesis, the mutant is active with o-cresol, o-methoxyphenol, and o-chlorophenol, as well as 3-methyl-, 3-methoxy-, 3 -fluoro, and 3-chloro-L-tyrosine in contrast to the wild-type enzyme
N185A
-
2% residual activtiy with L-tyrosine or 3-fluoro-L-tyrosine, N185 stabilizes reaction intermediate
T124D/F448H
-
very little activity with L-tyrosine, significant activity with S-(o-nitrophenyl)-L-cysteine, S-alkyl-L-cysteine and beta-chloro-L-alanine
T125S
-
changed substrate specificity
T15A
-
exhibits a 2fold improved activity towards 3,4-dihydroxyphenyl-L-alanine
R100T/V283R
A13V
-
mutant exhibits higher temperature and denaturant stability than wild-type enzyme
A13V/E83K
-
increases the thermal stability of the enzyme
A13V/E83K/I457F
-
increases the thermal stability of the enzyme
A13V/I457F
-
increases the thermal stability of the enzyme
A13V/T407A
-
increases the thermal stability of the enzyme
A196T/T451A
-
increases the activity of the enzyme
E42D/T129I
-
increases the activity of the enzyme
E83K
-
increases the thermal stability of the enzyme
T129I
-
increases the activity of the enzyme
T129I/A13V
-
increases the activity and thermal stability of the enzyme
T129I/A13V/E83K/T407A
-
increases the activity and thermal stability of the enzyme
T129I/V262A
-
increases the activity of the enzyme
T407A
-
increases the thermal stability of the enzyme
T451A/A13V/E83K
-
increases the activity and thermal stability of the enzyme
T451A/A13V/E83K/T407A
-
increases the activity and thermal stability of the enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
degradation
synthesis
Show AA Sequence (230 entries)
Please use the Sequence Search for a certain query.