Information on EC 4.1.99.2 - tyrosine phenol-lyase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
4.1.99.2
-
RECOMMENDED NAME
GeneOntology No.
tyrosine phenol-lyase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-tyrosine + H2O = phenol + pyruvate + NH3
show the reaction diagram
-
-
-
-
L-tyrosine + H2O = phenol + pyruvate + NH3
show the reaction diagram
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
-
L-tyrosine + H2O = phenol + pyruvate + NH3
show the reaction diagram
single-base racemization mechanism, proceeds with retention of configuration at C-beta
-
L-tyrosine + H2O = phenol + pyruvate + NH3
show the reaction diagram
NH3 is the first substrate which interacts with bound pyridoxal 5'-phosphate, pyruvate is the second substrate
-
L-tyrosine + H2O = phenol + pyruvate + NH3
show the reaction diagram
mechanism
-
L-tyrosine + H2O = phenol + pyruvate + NH3
show the reaction diagram
mechanism
-
L-tyrosine + H2O = phenol + pyruvate + NH3
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
alpha,beta-elimination
-
-
-
-
alpha,beta-elimination
-
-
alpha,beta-elimination
-
-
alpha,beta-elimination
Citrobacter freundii MTCC 2424
-
-
-
beta-elimination
-
-
racemization
-
-
-
-
racemization
Citrobacter freundii MTCC 2424
-
-
-
transamination
-
-
-
-
transamination
-
-
transamination
Citrobacter freundii MTCC 2424
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Tyrosine metabolism
-
SYSTEMATIC NAME
IUBMB Comments
L-tyrosine phenol-lyase (deaminating; pyruvate-forming)
A pyridoxal-phosphate protein. The enzyme also slowly catalyses pyruvate formation from D-tyrosine, S-methyl-L-cysteine, L-cysteine, L-serine and D-serine.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
beta-tyrosinase
-
-
-
-
L-tyrosine phenol-lyase
-
-
-
-
L-tyrosine phenol-lyase
-
-
L-tyrosine phenol-lyase
-
-
phenol-lyase, tyrosine
-
-
-
-
TPL
-
-
-
-
TPL
Citrobacter freundii NRRL B-2643
-
-
-
TPL
Pantoea agglomerans NRRL B-3466
-
-
-
tyrosine phenol lyase
-
-
tyrosine phenol lyase
P31013
-
tyrosine phenol lyase
Citrobacter freundii MTCC 2424
P31013
-
-
tyrosine phenol-lyase
-
-
tyrosine phenol-lyase
Citrobacter freundii NRRL B-2643
-
-
-
tyrosine phenol-lyase
-
-
tyrosine phenol-lyase
Pantoea agglomerans NRRL B-3466
-
-
-
tyrosine phenol-lyase
-
-
tyrosine-phenol lyase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9059-31-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Aeromonas phenologenes
ATCC 29063
-
-
Manually annotated by BRENDA team
NRRL B-2643
-
-
Manually annotated by BRENDA team
strain MTCC 2424
UniProt
Manually annotated by BRENDA team
wild type enzyme and mutant enzyme H343A
-
-
Manually annotated by BRENDA team
wild type enzyme and mutant enzymes R381A, R381V and R381I
UniProt
Manually annotated by BRENDA team
wild-type enzyme and mutant enzyme Y71F
-
-
Manually annotated by BRENDA team
Citrobacter freundii MTCC 2424
strain MTCC 2424
UniProt
Manually annotated by BRENDA team
Citrobacter freundii NRRL B-2643
NRRL B-2643
-
-
Manually annotated by BRENDA team
Escherichia intermedia A-21
-
-
Manually annotated by BRENDA team
Escherichia intermedia A-21; formerly Escherichia intermedia
-
-
Manually annotated by BRENDA team
formerly Escherichia intermedia
-
-
Manually annotated by BRENDA team
SV370; wild-type enzyme, mutant enzyme R100T, mutant enzyme R100T/V283R
-
-
Manually annotated by BRENDA team
Escherichia coli SV370
SV370
-
-
Manually annotated by BRENDA team
ATCC21434
-
-
Manually annotated by BRENDA team
NRRL B-3466
-
-
Manually annotated by BRENDA team
Pantoea agglomerans ATCC21434
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
Pseudomonas trifolii
-
-
-
Manually annotated by BRENDA team
Symbiobacterium sp.
SC-1
-
-
Manually annotated by BRENDA team
Symbiobacterium sp.
SMH1
-
-
Manually annotated by BRENDA team
Symbiobacterium sp. SMH1
SMH1
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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 ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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-chloro-L-Tyr + H2O
2-chlorophenol + pyruvate + NH3
show the reaction diagram
-
-
-
r
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-fluoro-L-Tyr + H2O
2-fluorophenol + pyruvate + NH3
show the reaction diagram
-
-
-
r
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-Ala + H2O
pyrocatechol + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
3,4-dihydroxyphenyl-L-Ala + H2O
pyrocatechol + NH3 + pyruvate
show the reaction diagram
Pantoea agglomerans, Pantoea agglomerans ATCC21434
-
i.e. L-dopa
-
?
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-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
3-chloro-L-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
3-chloro-L-Ala + H2O
?
show the reaction diagram
Escherichia coli SV370
-
-
-
-
?
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-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-Tyr + H2O
3-fluorophenol + pyruvate + NH3
show the reaction diagram
-
-
-
r
3-fluoro-L-Tyr + H2O
3-fluorophenol + pyruvate + NH3
show the reaction diagram
Pantoea agglomerans ATCC21434
-
-
-
-
?
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
P31013
-
-
?
3-fluoro-L-tyrosine + H2O
3-fluorophenol + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
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-methyl-L-Tyr + H2O
3-methylphenol + pyruvate + NH3
show the reaction diagram
-
-
-
r
3-methylphenol + pyruvate + NH3
3-methyl-L-Tyr + H2O
show the reaction diagram
-
-
-
r
Ala + H2O
?
show the reaction diagram
-
L-Ala, D-Ala
-
-
?
allothreonine + ?
Gly + ?
show the reaction diagram
-
-
-
-
beta-chloro-L-alanine
?
show the reaction diagram
P31013
-
-
?
beta-chloro-L-alanine
?
show the reaction diagram
-
-
-
?
beta-chloro-L-alanine + H2O
?
show the reaction diagram
-
-
-
r
beta-chloro-L-alanine + H2O
?
show the reaction diagram
Symbiobacterium sp., Symbiobacterium sp. SC-1
-
500% of activity compared to L-tyrosine
-
?
catechol + pyruvate + NH3
L-dihydroxyphenylalanine
show the reaction diagram
-
-
-
-
-
catechol + pyruvate + NH3
L-dihydroxyphenylalanine
show the reaction diagram
-
-
-
?
catechol + pyruvate + NH3
3,4-dihydroxyphenyl-L-alanine
show the reaction diagram
-
-
-
-
r
catechol + pyruvate + NH3
3,4-dihydroxyphenyl-L-alanine
show the reaction diagram
Citrobacter freundii, Citrobacter freundii NRRL B-2643
-
TPL is well-correlated to cytoplasmic 3,4-dihydroxyphenyl-L-alanine levels
-
-
r
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
Symbiobacterium sp., Symbiobacterium sp. SC-1
-
at 7% the rate of L-tyrosine
-
?
L-2-aminoadipate + H2O
?
show the reaction diagram
Escherichia coli, Escherichia coli SV370
-
no activity with wild-type enzyme, activity with mutant enzyme R100T/V283R
-
-
?
L-Ala + pyridoxal phosphate
pyridoxamine phosphate + keto acid
show the reaction diagram
-
-
-
-
ir
L-Asp + H2O
formate + pyruvate + NH3
show the reaction diagram
Escherichia coli, Escherichia coli SV370
-
no activity with wild-type enzyme, activity with mutant enzyme R100T/V283R
-
?
L-Cys + H2O
? + pyruvate + NH3
show the reaction diagram
-
-
-
?
L-Cys + H2O
? + pyruvate + NH3
show the reaction diagram
-
-
-
?
L-Cys + H2O
? + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-Cys + H2O
? + pyruvate + NH3
show the reaction diagram
Pantoea agglomerans ATCC21434
-
-
-
?
L-cysteine + H2O
?
show the reaction diagram
Symbiobacterium sp., Symbiobacterium sp. SC-1
-
-
-
?
L-cystine + H2O
? + pyruvate + NH3
show the reaction diagram
Pantoea agglomerans, Pantoea agglomerans ATCC21434
-
-
-
?
L-Glu + H2O
?
show the reaction diagram
Escherichia coli, Escherichia coli SV370
-
no activity with wild-type enzyme, activity with mutant enzyme R100T/V283R
-
-
?
L-m-Tyr + pyridoxal phosphate
pyridoxamine phosphate + keto acid
show the reaction diagram
-
-
-
-
ir
L-Met + H2O
?
show the reaction diagram
-
-
-
-
?
L-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
L-Phe + H2O
?
show the reaction diagram
-
-
-
-
r
L-Phe + pyridoxal phosphate
pyridoxamine phosphate + keto acid
show the reaction diagram
-
-
-
-
ir
L-Ser + phenol
L-Tyr + H2O
show the reaction diagram
-
-
-
?
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
-
-
i.e. L-dopa
?
L-serine + H2O
?
show the reaction diagram
Symbiobacterium sp.
-
-
-
?
L-Tyr + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-tyrosine + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
-
-
-
r
L-tyrosine + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
-
-
-
r
L-tyrosine + H2O
phenol + pyruvate + NH3
show the reaction diagram
P31013
-
-
?
L-tyrosine + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
-
-
?
L-tyrosine + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-tyrosine + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
-
-
r
L-tyrosine + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
-
-
-
r
L-tyrosine + H2O
phenol + pyruvate + NH3
show the reaction diagram
Symbiobacterium sp.
-
-
-
?
L-tyrosine + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-tyrosine + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
-
-
-
r
L-tyrosine + H2O
phenol + pyruvate + NH3
show the reaction diagram
P31013
-
-
-
?
L-tyrosine + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
-
-
?
L-tyrosine + H2O
phenol + pyruvate + NH3
show the reaction diagram
Citrobacter freundii MTCC 2424
P31013
-
-
-
?
O-benzoyl-L-Ser + H2O
?
show the reaction diagram
P31013
-
-
-
?
O-benzoyl-L-Ser + H2O
?
show the reaction diagram
-
-
-
-
?
O-benzyl-L-Ser + H2O
?
show the reaction diagram
P31013
-
-
-
?
phenol + pyruvate + NH3
Tyr + H2O
show the reaction diagram
-
-
-
-
phenol + pyruvate + NH3
Tyr + H2O
show the reaction diagram
-
-
-
r
pyrocatechol + pyruvate + NH3
3,4-dihydroxyphenyl-L-Ala + H2O
show the reaction diagram
-
-
-
?
pyrocatechol + pyruvate + NH3
3,4-dihydroxyphenyl-L-Ala + 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
P31013
-
-
?
S-(o-nitrophenyl)-L-cysteine
?
show the reaction diagram
-
-
-
?
S-(o-nitrophenyl)-L-cysteine
?
show the reaction diagram
-
-
-
?
S-(o-nitrophenyl)-L-cysteine + H2O
?
show the reaction diagram
-
-
-
-
?
S-(o-nitrophenyl)-L-cysteine + H2O
?
show the reaction diagram
-
-
-
r
S-(o-nitrophenyl)-L-cysteine + H2O
?
show the reaction diagram
Symbiobacterium sp., Symbiobacterium sp. SC-1
-
250% of activity compared to L-tyrosine
-
?
S-benzyl-L-Cys + H2O
? + pyruvate + NH3
show the reaction diagram
P31013
-
-
-
-
S-benzyl-L-Cys + H2O
? + pyruvate + NH3
show the reaction diagram
-
-
-
?
S-benzyl-L-Cys + H2O
? + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
S-benzyl-L-cysteine
?
show the reaction diagram
P31013
-
-
?
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
P31013
-
-
?
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-Cys + H2O
? + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
S-methyl-L-Cys + H2O
? + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
S-methyl-L-Cys + H2O
? + pyruvate + NH3
show the reaction diagram
-
-
-
?
S-methyl-L-Cys + H2O
? + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
S-methyl-L-cysteine
?
show the reaction diagram
P31013
-
-
?
S-methyl-L-cysteine
?
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
-
-
-
-
?
Ser + H2O
? + pyruvate + NH3
show the reaction diagram
-
-
-
?
Ser + H2O
? + pyruvate + NH3
show the reaction diagram
-
L-Ser
-
-
?
Ser + H2O
? + pyruvate + NH3
show the reaction diagram
-
L-Ser
-
-
-
Ser + H2O
? + pyruvate + NH3
show the reaction diagram
-
L-Ser
-
-
?
Ser + H2O
? + pyruvate + NH3
show the reaction diagram
-
D-Ser
-
-
?
Thr + ?
2-oxobutanoate + ?
show the reaction diagram
-
alpha,beta-elimination, D-Thr, L-Thr
-
?
Tyr + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
-
-
-
-
Tyr + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
Tyr + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
-
-
?
Tyr + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
Tyr + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
Tyr + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
-
-
-
-
Tyr + H2O
phenol + pyruvate + NH3
show the reaction diagram
Aeromonas phenologenes
-
-
-
-
?
Tyr + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
L-Tyr
-
?
Tyr + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
L-Tyr
-
-
?
Tyr + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
L-Tyr
-
-
-
Tyr + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
L-Tyr
-
-
r
Tyr + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
L-Tyr
-
-
?
Tyr + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
D-Tyr
-
-
-
Tyr + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
D-Tyr
-
-
?
Tyr + H2O
phenol + pyruvate + NH3
show the reaction diagram
Escherichia coli SV370
-
-
-
-
-
Tyr + H2O
phenol + pyruvate + NH3
show the reaction diagram
Pantoea agglomerans ATCC21434
-
-
-
-
?
L-tyrosine + H2O
3,4-dihydroxyphenyl-L-alanine
show the reaction diagram
Pantoea agglomerans, Pantoea agglomerans NRRL B-3466
-
TPL is well-correlated to cytoplasmic 3,4-dihydroxyphenyl-L-alanine levels
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
catalyzes racemization of L-Ala
-
-
-
additional information
?
-
-
catalyzes racemization of L-Ala
-
-
-
additional information
?
-
-
inducible enzyme
-
-
-
additional information
?
-
-
adaptive enzyme responsible for cells' growth on media with L-Tyr as the sole source of carbon
-
-
-
additional information
?
-
-
mechanism of alpha-proton isotope exchange in amino acids catalysed by tyrosine phenol-lyase
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-tyrosine + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
-
-
-
r
L-tyrosine + H2O
phenol + pyruvate + NH3
show the reaction diagram
-
-
-
-
r
L-tyrosine + H2O
phenol + pyruvate + NH3
show the reaction diagram
Citrobacter freundii, Citrobacter freundii MTCC 2424
P31013
-
-
-
?
additional information
?
-
-
inducible enzyme
-
-
-
additional information
?
-
-
adaptive enzyme responsible for cells' growth on media with L-Tyr as the sole source of carbon
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
required
pyridoxal 5'-phosphate
-
cofactor
pyridoxal 5'-phosphate
Aeromonas phenologenes
-
cofactor; Km: 0.032 mM
pyridoxal 5'-phosphate
-
2 pyridoxal 5'-phosphate binding sites per mol of enzyme; cofactor
pyridoxal 5'-phosphate
-
contains 2 mol of pyridoxal phosphate per mol of enzyme; Km: 0.00152 mM
pyridoxal 5'-phosphate
-
cofactor
pyridoxal 5'-phosphate
Symbiobacterium sp.
-
1 mol per mol of subunit
pyridoxal 5'-phosphate
-
the phosphate group changes from being monoanionic at low pH to dianionic at high pH
pyridoxal 5'-phosphate
-
dependent
pyridoxal 5'-phosphate
-
Km: 0.002 mM
pyridoxal 5'-phosphate
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K+
-
K+ or NH4+ required for maximal activity
K+
-
5-10 mM, accelerates activity
K+
-
activation
K+
-
catalytically important
NH4+
-
K+ or NH4+ required for maximal activity
NH4+
-
5-10 mM, accelerates activity
K+
-
activating
additional information
-
divalent cations (Mg2+, Ca2+, Ba2+, and Sr2+) do not activate TPL
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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-Ala
-
inhibits pyruvate formation from L-Tyr
L-Phe
-
competitive
L-Phe
-
inhibits pyruvate formation from L-Tyr
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
-
cleavage of Tyr
Phenol
-
cleavage of Tyr; mixed type inhibion
Phenol
-
100 mM and above
Phenol
-
In presence of 1 mM, only 23% of the original activity remained. The presence of phenol seriously affects its own production, through the inhibition of TPL
pyrocatechol
-
inhibits pyruvate formation from L-Tyr, mixed type
additional information
-
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
Vitreoscilla hemoglobin positive strains (vgb+ strains) have substantially higher TPL activity than the respective wild-type hosts or the strains bearing a comparable plasmid without vgb (the vgb- strains)
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
3,4-dihydroxyphenyl-L-alanine
-
wild type enzyme, in 0.1 M potassium phosphate buffer (pH 8.0) at 30C
4.6
-
3,4-dihydroxyphenyl-L-alanine
-
mutant enzyme T15A, at 30C
9.9
-
3,4-dihydroxyphenyl-L-alanine
Symbiobacterium sp.
-
pH 7.2, 60C
1.4
-
3-bromo-L-Tyr
-
-
1.7
-
3-chloro-L-Ala
-
wild-type enzyme
2
-
3-chloro-L-Ala
-
mutant enzyme Y71F
2
-
3-chloro-L-Ala
-
wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25C
3.2
-
3-chloro-L-Ala
-
mutant enzyme Y71F
10.2
-
3-chloro-L-Ala
-
-
11.4
-
3-chloro-L-Ala
-
mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25C
13.3
-
3-chloro-L-Ala
-
mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25C
46
-
3-chloro-L-Ala
-
mutant enzyme R100T/V283R
3
-
3-Chloro-L-Tyr
-
-
0.1
-
3-fluoro-L-Tyr
-
wild-type enzyme
0.1
-
3-fluoro-L-Tyr
-
wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25C
0.4
-
3-fluoro-L-Tyr
-
-
1.2
-
3-fluoro-L-Tyr
-
mutant enzyme H343A
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
-
wild-type enzyme, alpha,beta-elimination
32
-
D-Ala
-
racemization
11
-
L-Ala
-
wild-type enzyme
103
-
L-Ala
-
mutant enzyme H343A
0.21
-
L-Asp
-
mutant enzyme R100T/V283R
54
-
L-Asp
-
mutant enzyme R100T/V283R
5.3
-
L-Glu
-
mutant enzyme R100T/V283R
0.94
-
L-m-Tyr
-
transamination
0.0915
-
L-Met
-
-
11
-
L-Ser
-
mutant enzyme H343A
18
-
L-Ser
-
wild-type enzyme
0.2
-
L-Tyr
-
wild-type enzyme
0.2
-
L-Tyr
-
wild-type enzyme
0.2
-
L-Tyr
-
wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25C
0.23
-
L-Tyr
Aeromonas phenologenes
-
-
0.32
-
L-Tyr
-
mutant enzyme R100T/V283R
2.2
-
L-Tyr
-
mutant enzyme H343A
0.19
-
L-tyrosine
Symbiobacterium sp.
-
pH 7.2, 60C
0.22
-
L-tyrosine
-
mutant enzyme T15A, in 0.1 M potassium phosphate buffer (pH 8.0) at 30C
0.24
-
L-tyrosine
-
wild type enzyme, in 0.1 M potassium phosphate buffer (pH 8.0) at 30C
0.8
-
O-benzoyl-L-Ser
-
mutant enzyme Y71F
2.9
-
O-benzoyl-L-Ser
-
mutant enzyme Y71F
4.15
-
Phe
-
beta-elimination
110
-
pyruvate
-
-
0.1
-
S-(o-nitrophenyl)-L-Cys
-
wild-type enzyme
0.1
-
S-(o-nitrophenyl)-L-Cys
-
wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25C
0.16
-
S-(o-nitrophenyl)-L-Cys
-
mutant enzyme Y71F
0.5
-
S-(o-nitrophenyl)-L-Cys
-
mutant enzyme H343A
1.32
-
S-(o-nitrophenyl)-L-Cys
-
mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25C
1.86
-
S-(o-nitrophenyl)-L-Cys
-
mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25C
0.27
-
S-(o-nitrophenyl)-L-cysteine
-
pH 8.0, 25C
0.36
-
S-(o-nitrophenyl)-L-cysteine
Symbiobacterium sp.
-
pH 7.2, 60C
0.05
-
S-benzyl-L-Cys
-
mutant enzyme Y71F
0.2
-
S-benzyl-L-Cys
-
wild-type enzyme
0.2
-
S-benzyl-L-Cys
-
wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25C
1.2
-
S-benzyl-L-Cys
-
mutant enzyme H343A
5.1
-
S-benzyl-L-Cys
-
mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25C
7
-
S-benzyl-L-Cys
-
mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25C
0.3
-
S-ethyl-L-Cys
-
mutant enzyme Y71F
1.2
-
S-ethyl-L-Cys
-
mutant enzyme H343A
6.6
-
S-ethyl-L-Cys
-
wild-type enzyme
0.52
-
S-Methyl-L-Cys
-
mutant enzyme Y71F
1.67
-
S-Methyl-L-Cys
-
-
3.4
-
S-Methyl-L-Cys
-
wild-type enzyme
3.4
-
S-Methyl-L-Cys
-
wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25C
4.17
-
S-Methyl-L-Cys
-
-
12.99
-
S-Methyl-L-Cys
-
mutant enzyme H343A
13.4
-
S-Methyl-L-Cys
-
mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25C
50
-
S-Methyl-L-Cys
-
mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25C
56.4
-
S-Methyl-L-Cys
-
wild-type enzyme
3.2
-
S-methyl-L-cysteine
-
pH 8.0, 25C
5.5
-
S-methyl-L-cysteine
Symbiobacterium sp.
-
pH 7.2, 60C
34
-
Ser
-
beta-elimination
51
-
Ser
-
transamination
0.24
-
Tyr
-
beta-elimination
0.406
-
L-tyrosine
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
pH-independent kinetic constants for substrates bearing small substituents
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.31
-
3,4-dihydroxyphenyl-L-alanine
-
wild type enzyme, in 0.1 M potassium phosphate buffer (pH 8.0) at 30C
0.68
-
3,4-dihydroxyphenyl-L-alanine
-
mutant enzyme T15A, at 30C
0.0065
-
3-chloro-L-Ala
-
mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25C
0.02
-
3-chloro-L-Ala
-
mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25C
0.053
-
3-chloro-L-Ala
-
mutant enzyme Y71F
0.7
-
3-chloro-L-Ala
-
wild-type enzyme
0.7
-
3-chloro-L-Ala
-
wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25C
1.13
-
3-chloro-L-Ala
-
mutant enzyme R100T/V283R
3
-
3-chloro-L-Ala
P31013
wild-type enzyme
3
-
3-chloro-L-Ala
-
wild-type enzyme
0.18
-
3-fluoro-L-Tyr
-
mutant enzyme H343A
1.4
-
3-fluoro-L-Tyr
-
wild-type enzyme
1.4
-
3-fluoro-L-Tyr
-
wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25C
0.00153
-
Ala
-
beta-elimination
0.004
-
D-Ala
-
mutant enzyme H343A
0.008
-
D-Ala
-
racemization
0.01
-
D-Ala
-
wild-type enzyme
0.03
-
L-Ala
-
wild-type enzyme
0.00268
-
L-m-Tyr
-
transamination
0.07
-
L-Ser
-
mutant enzyme H343A
0.17
-
L-Ser
-
wild-type enzyme
0.11
-
L-Tyr
-
mutant enzyme R100T/V283R
0.42
-
L-Tyr
-
mutant enzyme H343A
2.2
-
L-Tyr
P31013
wild-type enzyme
3.5
-
L-Tyr
-
wild-type enzyme
3.5
-
L-Tyr
-
wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25C
3.7
-
L-Tyr
-
-
0.00013
-
L-tyrosine
-
pH 8.0, 25C, mutant enzyme K256H
0.001
-
L-tyrosine
-
pH 8.0, 25C, mutant enzyme K256A
0.12
-
L-tyrosine
-
pH 8.0, 25C, mutant enzyme K256R
1.2
-
L-tyrosine
-
mutant enzyme T15A, in 0.1 M potassium phosphate buffer (pH 8.0) at 30C
0.15
-
O-benzoyl-L-Ser
-
mutant enzyme Y71F
8.3
-
O-benzoyl-L-Ser
P31013
wild-type enzyme
8.3
-
O-benzoyl-L-Ser
-
wild-type enzyme
3.9
-
O-benzyl-L-Cys
P31013
wild-type enzyme
-
0.0008
-
Phe
-
beta-elimination
0.024
-
S-(o-nitrophenyl)-L-Cys
-
mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25C
0.041
-
S-(o-nitrophenyl)-L-Cys
-
mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25C
0.25
-
S-(o-nitrophenyl)-L-Cys
-
mutant enzyme Y71F
1.55
-
S-(o-nitrophenyl)-L-Cys
-
mutant enzyme H343A
5.1
-
S-(o-nitrophenyl)-L-Cys
-
wild-type enzyme
5.1
-
S-(o-nitrophenyl)-L-Cys
P31013
wild-type enzyme
5.1
-
S-(o-nitrophenyl)-L-Cys
-
wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25C
9.7
-
S-(o-nitrophenyl)-L-Cys
P31013
wild-type enzyme
0.0091
-
S-(o-nitrophenyl)-L-cysteine
-
pH 8.0, 25C, mutant enzyme K256A
0.027
-
S-(o-nitrophenyl)-L-cysteine
-
pH 8.0, 25C, mutant enzyme K256H
0.17
-
S-(o-nitrophenyl)-L-cysteine
-
pH 8.0, 25C, mutant enzyme K256R
7.4
-
S-(o-nitrophenyl)-L-cysteine
-
pH 8.0, 25C, mutant enzyme E69D/K256R
0.02
-
S-benzoyl-L-Cys
-
mutant enzyme H343A
0.0012
-
S-benzyl-L-Cys
-
mutant enzyme Y71F
0.0067
-
S-benzyl-L-Cys
-
mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25C
0.02
-
S-benzyl-L-Cys
-
mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25C
0.5
-
S-benzyl-L-Cys
P31013
wild-type enzyme
0.5
-
S-benzyl-L-Cys
-
wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25C
0.52
-
S-benzyl-L-Cys
-
wild-type enzyme
0.000217
-
S-ethyl-L-Cys
-
mutant enzyme Y71F
0.0025
-
S-ethyl-L-Cys
-
pH 8.0, 25C, mutant enzyme K256A
0.0088
-
S-ethyl-L-Cys
-
pH 8.0, 25C, mutant enzyme K256H
0.02
-
S-ethyl-L-Cys
-
pH 8.0, 25C, mutant enzyme K256R
0.37
-
S-ethyl-L-Cys
-
pH 8.0, 25C, mutant enzyme E69D/K256R
1.4
-
S-ethyl-L-Cys
-
mutant enzyme H343A
1.7
-
S-ethyl-L-Cys
P31013
wild-type enzyme
3.88
-
S-ethyl-L-Cys
-
wild-type enzyme
0.000383
-
S-Methyl-L-Cys
-
mutant enzyme Y71F
0.0016
-
S-Methyl-L-Cys
-
mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25C
0.0052
-
S-Methyl-L-Cys
-
mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25C
0.15
-
S-Methyl-L-Cys
-
mutant enzyme H343A
0.9
-
S-Methyl-L-Cys
P31013
wild-type enzyme
0.9
-
S-Methyl-L-Cys
-
wild-type enzyme
0.9
-
S-Methyl-L-Cys
-
wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25C
0.001
-
Ser
-
transamination
0.012
-
Ser
-
beta-elimination
0.2
-
Tyr
-
beta-elimination
1.8
-
L-tyrosine
-
wild type enzyme, in 0.1 M potassium phosphate buffer (pH 8.0) at 30C
additional information
-
additional information
-
pH-independent kinetic constants for substrates bearing small substituents
-
additional information
-
additional information
P31013
the turnover-numbers of the mutant enzyme R381I, R381V and R381A for the substrates S-(o-nitrophenyl)-L-Cys, 3-chloro-L-Ala, O-benzoyl-L-Ser and S-methyl-L-Cys are comparable to those of the wild-type enzyme
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5.44
-
1-amino-2-(4-hydroxyphenyl)-ethyl phosphinic acid
-
-
100
-
1-amino-2-(4-hydroxyphenyl)-ethyl phosphonic acid
-
-
0.135
-
2-aza-L-tyrosine
-
25C, pH 7.8
3.4
-
2-aza-L-tyrosine
-
25C, pH 7.8
3
-
L-Asp
-
mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25C
3.5
-
L-Asp
-
wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25C, using L-Tyr as a substrate; wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25C, using S-(o-nitrophenyl)-L-Cys as a substrate
3.6
-
L-Asp
-
mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25C
5
-
L-Glu
-
wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25C, using L-Tyr as a substrate; wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25C, using S-(o-nitrophenyl)-L-Cys as a substrate
66
-
L-Glu
-
mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25C
100
-
L-Glu
-
mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25C
1.33
-
L-homoserine
-
wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25C, using L-Tyr as a substrate; wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25C, using S-(o-nitrophenyl)-L-Cys as a substrate
69
-
L-homoserine
-
mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25C
82
-
L-homoserine
-
mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25C
0.73
-
L-Met
-
wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25C, using L-Tyr as a substrate; wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25C, using S-(o-nitrophenyl)-L-Cys as a substrate
4.2
-
L-Met
-
mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25C
11
-
L-Met
-
mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25C
1.7
-
L-Phe
-
wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25C, using L-Tyr as a substrate; wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25C, using S-(o-nitrophenyl)-L-Cys as a substrate
17
-
L-Phe
-
mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25C
22
-
L-Phe
-
mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25C
1.7
-
L-phenylalanine
-
-
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]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
2.8
-
Aeromonas phenologenes
-
-
10
-
-
pH 7.8, 30C
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
8
Symbiobacterium sp.
-
-
8
9
-
phenol as substrate
8
-
Symbiobacterium sp.
-
-
8.5
9
-
synthesis of L-Tyr from pyruvate, ammonia and phenol
8.5
-
Aeromonas phenologenes
-
-
8.5
-
P31013
activity assay
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
P31013
activity assay
30
-
-
assay at
40
-
-
native enzyme, using 3,4-dihydroxyphenyl-L-alanine as a substrate
45
-
-
mutant enzyme T15A, using 3,4-dihydroxyphenyl-L-alanine as a substrate
55
60
Symbiobacterium sp.
-
-
55
-
-
native enzyme, using L-tyrosine as a substrate
60
-
-
mutant enzyme T15A, using L-tyrosine as a substrate
80
-
Symbiobacterium sp.
-
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.9
-
Symbiobacterium sp.
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
wild-type S12 and its mutant strains S12TPL3 (optimized for phenol production)
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
52000
-
-
SDS-PAGE
159000
-
-
calculation from diffusion and sedimentation data
200000
-
-
gel filtration
202000
-
Symbiobacterium sp.
-
gel filtration
380000
-
Aeromonas phenologenes
-
gel filtration, nnon-denaturing PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 52269, calculation from nucleotide sequence
?
Symbiobacterium sp.
-
x * 52196, calculation from nucleotide sequence
?
-
x * 52196, calculation from nucleotide sequence
-
homotetramer
-
4 * 51400
homotetramer
-
composed of two catalytic dimers
tetramer
-
4 * 48000, SDS-PAGE
tetramer
Symbiobacterium sp.
-
4 * 52200, deduced from amino acid sequence
tetramer
-
x-ray crystallography
tetramer
-
4 * 52200, deduced from amino acid sequence
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
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
P31013
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
decrease of the enzymatic activity at pH 6.0
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
40
-
Aeromonas phenologenes
-
-
40
-
-
stable up to
50
-
Aeromonas phenologenes
-
-
50
-
-
rapid inactivation above
60
-
Aeromonas phenologenes
-
10 min, about 45% loss of activity
70
-
Aeromonas phenologenes
-
10 min, complete loss of activity
70
-
Symbiobacterium sp.
-
30 min, stable up to
80
-
-
20 min, stable up to
80
-
Symbiobacterium sp.
-
30 min, 70% loss of activity
85
-
-
20 min, about 25% loss of activity
90
-
-
20 min, about 90% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
not stable to freezing and thawing
Aeromonas phenologenes
-
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
-
the enzyme maintains its original activity at phenol concentrations below 75 mM
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2C, 0.02 M phosphate buffer + mercaptoethanol, pH 7.0, 1 week, 50% loss of activity
Aeromonas phenologenes
-
4C, 3 days, negligible activity after 3 days
-
stable against 0.2% sodium dodecylsulfate
Symbiobacterium sp.
-
40C, in the presence of 75 mM phenol at pH 8.5, 18h, no loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
partial
Aeromonas phenologenes
-
ammonium sulfate precipitation
-
mutant enzyme His343Ala
-
Resource Q ion exchange chromatography and Phenyl Superose Phenyl Superose column chromatography
-
-
Symbiobacterium sp.
-
mutant enzyme A13V
-
partial purification by methanol treatment
-
wild-type protein and mutants T451A/A13V/E83K and T129I/A13V purified to homogeneity with purification yields of over 40%
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli SVS370 cells
-
expressed in Escherichia coli XL-1 Blue cells
-
the plasmid pTZTPL is constructed for expression of the protein in Escherichia coli SVS370 cells
-
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
-
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.
-
expression in Escherichia coli
Symbiobacterium sp.
-
expression in Escherichia coli
-
expressed in Escherichia coli strain BL21
-
plasmid pHCE IIB-TPL ligated at 4C for 24 h with a T4 DNA ligase, products electrotransformed into Escherichia coli JM83
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-tyrosine addition only has a positive effect in terms of TPL induction for cell cultures harvested after 12 h
-
L-tyrosine addition only has a positive effect in terms of TPL induction for cell cultures harvested after 12 h
Citrobacter freundii NRRL B-2643
-
-
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
-
L-tyrosine addition only has a positive effect in terms of TPL induction for cell cultures harvested after 12 h
-
L-tyrosine addition only has a positive effect in terms of TPL induction for cell cultures harvested after 12 h
Pantoea agglomerans NRRL B-3466
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
F448H
-
very little activity with L-tyrosine, significant activity with S-(o-nitrophenyl)-L-cysteine, S-alkyl-L-cysteine and beta-chloro-L-alanine
F448H
-
very low activity with L-tyrosine, reduced activity with other substrates
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
N185A
-
2% residual activtiy with L-tyrosine or 3-fluoro-L-tyrosine, N185 stabilizes reaction intermediate
R381A
P31013
beta-elimination activity has been reduced by 0.0001fold compared to wild type enzyme
R381A
-
dramatic decrease in activity with L-tyrosine, but little effect on activity with other substrates
R381I
P31013
no detectable beta-elimination activity with L-Tyr as substrate
R381I
-
dramatic decrease in activity with L-tyrosine, but little effect on activity with other substrates
R381V
P31013
no detectable beta-elimination activity with L-Tyr as substrate
R381V
-
dramatic decrease in activity with L-tyrosine, but little effect on activity with other substrates
T124A
-
very little activity with L-tyrosine, significant activity with S-(o-nitrophenyl)-L-cysteine, S-alkyl-L-cysteine and beta-chloro-L-alanine
T124A
-
dramatic decrease in activity with L-tyrosine
T124D
-
very little activity with L-tyrosine, significant activity with S-(o-nitrophenyl)-L-cysteine, S-alkyl-L-cysteine and beta-chloro-L-alanine
T124D
-
no detectable activity with L-tyrosine, but significant activity with other substrates with good leaving groups
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
Y71F
-
no activity for beta-elimination of L-Tyr. Can react with S-alkylcysteines, but these substrates exhibit a 1000-10000fold reduced turnover number compared to wild-type. For substrates with good leaving groups S-(o-nitrophenyl)-L-Cys, 3-chloro-L-Ala and O-benzoyl-L-Ser the mutant enzyme exhibits turnover numbers 1.85-7% those of the wild-type enzyme. Tyr 71 plays a dual role, both in cofactor binding in the absence of substrate and also as a general acid catalyst in the elimination of leaving groups from quinoid intermediates
Y71F
-
no detectable activity with L-tyrosine, but significant activity with other substrates with good leaving groups
Y71F
-
no enzymic activity, crystallization data
R100T/V283R
-
increases the beta-elimination activity towards dicarboxylic amino acids, L-Asp, L-Glu and L-2-aminoadipate at least 10000-fold
R100T/V283R
Escherichia coli SV370
-
increases the beta-elimination activity towards dicarboxylic amino acids, L-Asp, L-Glu and L-2-aminoadipate at least 10000-fold
-
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
biotechnology
-
encapsulation of enzyme in wet nanoporous silica gels to selectively stabilize tertiary and quarternary protein conformations and to develop bioreactors and biosensors
biotechnology
P31013
tyrosine phenol lyase modifies and synthesizes natural and non-natural amino acids, synthesizes precursor of a large number of relevant compounds and plays an important role in phenolic waste treatment
biotechnology
Citrobacter freundii MTCC 2424
-
tyrosine phenol lyase modifies and synthesizes natural and non-natural amino acids, synthesizes precursor of a large number of relevant compounds and plays an important role in phenolic waste treatment
-
synthesis
-
development of a multienzyme reactor with ec 4.1.99.2 and ec 4.1.1.25 for dopamine synthesis
synthesis
-
production of L-dopa, which is applied for the treatment of Parkinsonism
degradation
Symbiobacterium sp.
-
removal and bioconversion of phenol in wastewater by a thermostable beta-tyrosinase
degradation
Symbiobacterium sp. SMH1
-
removal and bioconversion of phenol in wastewater by a thermostable beta-tyrosinase
-