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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-bromo-L-Tyr + H2O
2-bromophenol + pyruvate + NH3
-
-
-
r
2-bromophenol + pyruvate + NH3
2-bromo-L-Tyr + H2O
-
-
-
r
2-chloro-L-Tyr + H2O
2-chlorophenol + pyruvate + NH3
2-chlorophenol + pyruvate + NH3
2-chloro-L-Tyr + H2O
-
-
-
r
2-fluoro-L-Tyr + H2O
2-fluorophenol + pyruvate + NH3
2-fluorophenol + pyruvate + NH3
2-fluoro-L-Tyr + H2O
-
-
-
r
2-fluorotyrosine + H2O
2-fluorophenol + pyruvate + NH3
-
-
-
?
2-methoxy-L-Tyr + H2O
2-methoxyphenol + pyruvate + NH3
-
-
-
r
2-methoxyphenol + pyruvate + NH3
2-methoxy-L-Tyr + H2O
-
-
-
r
2-methyl-L-Tyr + H2O
2-methylphenol + pyruvate + NH3
-
-
-
r
2-methylphenol + pyruvate + NH3
2-methyl-L-Tyr + H2O
-
-
-
r
3,4-dihydroxyphenyl-L-Ala + H2O
pyrocatechol + NH3 + pyruvate
3,4-dihydroxyphenyl-L-alanine
?
Symbiobacterium sp.
-
-
-
?
3,4-dihydroxyphenyl-L-alanine + H2O
pyrocatechol + NH3 + pyruvate
-
-
-
-
?
3,5-difluorotyrosine + H2O
3,5-difluorophenol + pyruvate + NH3
-
-
-
?
3-bromo-L-Tyr + H2O
3-bromophenol + pyruvate + NH3
-
-
-
r
3-bromo-L-tyrosine + H2O
3-bromophenol + pyruvate + NH3
-
-
-
-
?
3-bromophenol + pyruvate + NH3
3-bromo-L-Tyr + H2O
-
-
-
r
3-chloro-L-Tyr + H2O
3-chlorophenol + pyruvate + NH3
-
-
-
r
3-chloro-L-tyrosine + H2O
3-chlorophenol + pyruvate + NH3
-
-
-
-
?
3-chloro-L-tyrosine + H2O
?
-
substrate of mutant M379V, not of the wild-type enzyme
-
-
?
3-chlorophenol + pyruvate + NH3
3-chloro-L-Tyr + H2O
-
-
-
r
3-chlorotyrosine + H2O
3-chlorophenol + pyruvate + NH3
-
-
-
?
3-fluoro-L-Tyr + H2O
3-fluorophenol + pyruvate + NH3
3-fluoro-L-tyrosine
3-fluorophenol + pyruvate + NH3
-
-
-
?
3-fluoro-L-tyrosine + H2O
3-fluoro-phenol + pyruvate + NH3
-
-
?
3-fluoro-L-tyrosine + H2O
3-fluorophenol + pyruvate + NH3
3-fluoro-L-tyrosine + H2O
?
-
substrate of mutant M379V, not of the wild-type enzyme
-
-
?
3-fluorophenol + pyruvate + NH3
3-fluoro-L-Tyr + H2O
-
-
-
r
3-fluorotyrosine + H2O
3-fluorophenol + pyruvate + NH3
-
-
-
?
3-iodo-L-tyrosine + H2O
3-iodophenol + pyruvate + NH3
-
-
-
-
?
3-methoxy-L-tyrosine + H2O
?
-
substrate of mutant M379V, not of the wild-type enzyme
-
-
?
3-methyl-L-Tyr + H2O
3-methylphenol + pyruvate + NH3
-
-
-
r
3-methyl-L-tyrosine + H2O
?
-
substrate of mutant M379V, not of the wild-type enzyme
-
-
?
3-methylphenol + pyruvate + NH3
3-methyl-L-Tyr + H2O
-
-
-
r
allothreonine + ?
Gly + ?
-
-
-
?
beta-chloro-L-alanine + H2O
?
beta-chloro-L-alanine + H2O
Cl- + pyruvate + NH3
-
-
-
r
catechol + pyruvate
L-DOPA + H2O
catechol + pyruvate + NH3
3,4-dihydroxyphenyl-L-alanine
catechol + pyruvate + NH3
L-dihydroxyphenylalanine
catechol + pyruvic acid
L-dopa + H2O
-
-
-
-
?
D-serine + H2O
?
Symbiobacterium sp.
-
at 11% the rate of L-tyrosine
-
?
D-tyrosine + H2O
phenol + pyruvate + NH3
L-3-4 dihydroxyphenylalanine + H2O
catechol + pyruvate + NH3
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-Asp + H2O
formate + pyruvate + NH3
L-asparagine + H2O
?
-
-
-
-
?
L-Cys + H2O
? + pyruvate + NH3
L-cysteine + H2O
thiophenol + pyruvate + NH3
12% of the activity with L-tyrosine
-
-
r
L-cystine + H2O
? + pyruvate + NH3
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-methionine + H2O
?
-
-
-
-
?
L-Phe + pyridoxal phosphate
pyridoxamine phosphate + keto acid
-
-
-
-
ir
L-phenylalanine + H2O
?
-
low activity
-
-
?
L-phenylalanine + H2O
? + pyruvate + NH3
7% of the activity with L-tyrosine
-
-
r
L-Ser + phenol
L-Tyr + H2O
L-Ser + pyridoxal phosphate
pyridoxamine phosphate + keto acid
-
-
-
-
ir
L-Ser + pyrocatechol
3,4-dihydroxyphenyl-L-Ala + H2O
L-serine + H2O
?
Symbiobacterium sp.
-
-
-
?
L-serine + H2O
pyruvate + NH3
9% of the activity with L-tyrosine
-
-
r
L-tryptophan + H2O
indole + pyruvate + NH3
L-Tyr + H2O
phenol + pyruvate + NH3
-
-
-
-
?
L-tyrosine + H2O
3,4-dihydroxyphenyl-L-alanine
L-tyrosine + H2O
phenol + pyruvate + NH3
L-valine + H2O
?
-
-
-
-
?
L-valine + H2O
? + pyruvate + NH3
6% of the activity with L-tyrosine
-
-
r
O-benzyl-L-Cys + H2O
?
-
-
-
?
O-benzyl-L-Ser + H2O
?
-
-
-
?
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
phenol + pyruvate + NH3
Tyr + H2O
pyrocatechol + pyruvate + NH3
3,4-dihydroxyphenyl-L-Ala + H2O
pyrocatechol + pyruvate + NH4+
L-DOPA + H2O
resorcinol + pyruvate + NH3
2,4-dihydroxyphenyl-L-Ala
-
-
-
?
S-(2-nitrophenyl)-L-cysteine
?
-
-
-
-
?
S-(2-nitrophenyl)-L-cysteine + H2O
2-nitrobenzenethiolate + pyruvate + NH3
S-(o-nitrophenyl)-L-Cys + H2O
?
-
-
-
-
?
S-(o-nitrophenyl)-L-Cys + H2O
? + pyruvate + NH3
-
-
-
-
?
S-(o-nitrophenyl)-L-cysteine
?
S-(o-nitrophenyl)-L-cysteine + H2O
?
S-benzoyl-L-Cys + H2O
?
-
-
-
-
?
S-benzyl-L-Cys + H2O
? + pyruvate + NH3
S-benzyl-L-cysteine
? + pyruvate + NH3
-
-
-
-
?
S-benzyl-L-cysteine + H2O
thiophenol + pyruvate + NH3
-
-
-
r
S-ethyl-L-cysteine
? + pyruvate + NH3
-
-
-
-
?
S-ethyl-L-cysteine + H2O
?
-
-
-
?
S-ethyl-L-cysteine + H2O
ethanethiol + pyruvate + NH3
-
-
-
r
S-methyl-L-Cys + H2O
? + pyruvate + NH3
S-methyl-L-cysteine
? + pyruvate + NH3
-
-
-
-
?
S-methyl-L-cysteine + H2O
?
Symbiobacterium sp.
-
385% of activity compared to L-tyrosine
-
?
S-methyl-L-cysteine + H2O
methanethiol + pyruvate + NH3
-
-
-
r
S-methyl-L-cysteine + H2O
methanthiol + pyruvate + NH3
13% of the activity with L-tyrosine
-
-
r
S-o-nitrophenyl-L-cysteine + H2O
?
-
-
-
-
?
Ser + H2O
? + pyruvate + NH3
Thr + ?
2-oxobutanoate + ?
Tyr + H2O
phenol + pyruvate + NH3
additional information
?
-
2-chloro-L-Tyr + H2O
2-chlorophenol + pyruvate + NH3
-
-
-
r
2-chloro-L-Tyr + H2O
2-chlorophenol + pyruvate + NH3
-
-
-
-
?
2-fluoro-L-Tyr + H2O
2-fluorophenol + pyruvate + NH3
-
-
-
r
2-fluoro-L-Tyr + H2O
2-fluorophenol + pyruvate + NH3
-
-
-
-
?
3,4-dihydroxyphenyl-L-Ala + H2O
pyrocatechol + NH3 + pyruvate
-
-
-
?
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-chloro-L-Ala + H2O
?
-
-
-
-
?
3-chloro-L-Ala + H2O
?
-
-
-
-
?
3-chloro-L-Ala + H2O
?
-
-
-
-
?
3-chloro-L-Ala + H2O
?
-
-
-
-
?
3-fluoro-L-Tyr + H2O
3-fluorophenol + pyruvate + NH3
-
-
-
r
3-fluoro-L-Tyr + H2O
3-fluorophenol + pyruvate + NH3
-
-
-
-
?
3-fluoro-L-Tyr + H2O
3-fluorophenol + pyruvate + NH3
-
-
-
-
?
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
Ala + H2O
?
-
L-Ala
-
-
?
Ala + H2O
?
-
D-Ala
-
-
?
beta-chloro-L-alanine
?
-
-
-
?
beta-chloro-L-alanine
?
-
-
?
beta-chloro-L-alanine + H2O
?
-
-
-
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
L-DOPA + H2O
-
-
-
r
catechol + pyruvate
L-DOPA + H2O
-
-
-
r
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
catechol + pyruvate + NH3
3,4-dihydroxyphenyl-L-alanine
-
-
-
-
r
catechol + pyruvate + NH3
L-dihydroxyphenylalanine
-
-
-
?
catechol + pyruvate + NH3
L-dihydroxyphenylalanine
-
-
-
-
?
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-Cys + H2O
? + pyruvate + NH3
-
-
-
?
L-Cys + H2O
? + pyruvate + NH3
-
-
-
?
L-Cys + H2O
? + pyruvate + NH3
-
-
-
?
L-Cys + H2O
? + pyruvate + NH3
-
-
-
-
?
L-cysteine + H2O
?
Symbiobacterium sp.
-
-
-
?
L-cysteine + H2O
?
-
-
-
?
L-cystine + H2O
? + pyruvate + NH3
-
-
-
?
L-cystine + H2O
? + pyruvate + NH3
-
-
-
?
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-Phe + H2O
?
-
-
-
-
?
L-Ser + phenol
L-Tyr + H2O
-
-
-
?
L-Ser + phenol
L-Tyr + H2O
-
-
-
?
L-Ser + phenol
L-Tyr + H2O
-
-
-
?
L-Ser + phenol
L-Tyr + H2O
-
-
-
?
L-Ser + phenol
L-Tyr + H2O
-
-
-
?
L-Ser + phenol
L-Tyr + H2O
-
-
-
?
L-Ser + phenol
L-Tyr + H2O
-
-
-
?
L-Ser + phenol
L-Tyr + H2O
Pseudomonas pelurida
-
-
-
?
L-Ser + phenol
L-Tyr + H2O
Pseudomonas trifolii
-
-
-
?
L-Ser + phenol
L-Tyr + H2O
-
-
-
?
L-Ser + phenol
L-Tyr + H2O
-
-
-
?
L-Ser + pyrocatechol
3,4-dihydroxyphenyl-L-Ala + H2O
-
-
-
?
L-Ser + pyrocatechol
3,4-dihydroxyphenyl-L-Ala + H2O
-
-
-
?
L-Ser + pyrocatechol
3,4-dihydroxyphenyl-L-Ala + H2O
-
-
-
?
L-Ser + pyrocatechol
3,4-dihydroxyphenyl-L-Ala + H2O
-
-
-
?
L-Ser + pyrocatechol
3,4-dihydroxyphenyl-L-Ala + H2O
-
-
-
?
L-Ser + pyrocatechol
3,4-dihydroxyphenyl-L-Ala + H2O
-
-
-
?
L-Ser + pyrocatechol
3,4-dihydroxyphenyl-L-Ala + H2O
-
-
i.e. L-dopa
?
L-Ser + pyrocatechol
3,4-dihydroxyphenyl-L-Ala + H2O
Pseudomonas pelurida
-
-
-
?
L-Ser + pyrocatechol
3,4-dihydroxyphenyl-L-Ala + H2O
Pseudomonas trifolii
-
-
-
?
L-Ser + pyrocatechol
3,4-dihydroxyphenyl-L-Ala + H2O
-
-
-
?
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
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
-
-
-
-
?
L-tyrosine + H2O
phenol + pyruvate + NH3
-
-
-
r
L-tyrosine + H2O
phenol + pyruvate + NH3
-
-
-
-
r
L-tyrosine + H2O
phenol + pyruvate + NH3
-
-
?
L-tyrosine + H2O
phenol + pyruvate + NH3
-
-
-
?
L-tyrosine + H2O
phenol + pyruvate + NH3
-
-
-
-
?
L-tyrosine + H2O
phenol + pyruvate + NH3
-
-
-
r
L-tyrosine + H2O
phenol + pyruvate + NH3
-
-
-
-
r
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
-
-
-
r
L-tyrosine + H2O
phenol + pyruvate + NH3
-
alpha-beta elimination
-
-
r
L-tyrosine + H2O
phenol + pyruvate + NH3
-
-
-
?
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
-
-
-
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
-
-
-
-
r
L-tyrosine + H2O
phenol + pyruvate + NH3
-
-
-
-
r
L-tyrosine + H2O
phenol + pyruvate + NH3
Symbiobacterium sp.
-
-
-
?
L-tyrosine + H2O
phenol + pyruvate + NH3
-
-
-
?
L-tyrosine + H2O
phenol + pyruvate + NH3
-
-
-
-
?
L-tyrosine + H2O
phenol + pyruvate + NH3
-
-
-
-
r
O-benzoyl-L-Ser + H2O
?
-
-
-
-
?
O-benzoyl-L-Ser + H2O
?
-
-
-
?
phenol + pyruvate + NH3
Tyr + H2O
-
-
-
?
phenol + pyruvate + NH3
Tyr + H2O
-
-
-
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
-
-
-
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
?
-
-
-
?
S-(o-nitrophenyl)-L-cysteine
?
-
-
-
?
S-(o-nitrophenyl)-L-cysteine
?
-
-
?
S-(o-nitrophenyl)-L-cysteine + H2O
?
-
-
-
r
S-(o-nitrophenyl)-L-cysteine + H2O
?
-
-
-
?
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
-
?
S-benzyl-L-Cys + H2O
? + pyruvate + NH3
-
-
-
?
S-benzyl-L-Cys + H2O
? + pyruvate + NH3
-
-
-
-
?
S-benzyl-L-Cys + H2O
? + pyruvate + NH3
-
-
-
?
S-benzyl-L-cysteine
?
-
-
-
?
S-benzyl-L-cysteine
?
-
-
?
S-ethyl-L-Cys + H2O
?
-
-
-
-
?
S-ethyl-L-Cys + H2O
?
-
-
-
?
S-ethyl-L-cysteine
?
-
-
-
?
S-ethyl-L-cysteine
?
-
-
?
S-methyl-L-Cys + H2O
? + pyruvate + NH3
-
-
-
-
?
S-methyl-L-Cys + H2O
? + pyruvate + NH3
-
-
-
?
S-methyl-L-Cys + H2O
? + pyruvate + NH3
-
-
-
?
S-methyl-L-Cys + H2O
? + pyruvate + NH3
-
-
-
-
?
S-methyl-L-Cys + H2O
? + pyruvate + NH3
-
-
-
-
?
S-methyl-L-cysteine
?
-
-
-
?
S-methyl-L-cysteine
?
-
-
-
?
S-methyl-L-cysteine
?
-
-
?
Ser + H2O
? + pyruvate + NH3
-
L-Ser
-
-
?
Ser + H2O
? + pyruvate + NH3
-
-
-
-
?
Ser + H2O
? + pyruvate + NH3
-
-
-
?
Ser + H2O
? + pyruvate + NH3
-
L-Ser
-
-
?
Ser + H2O
? + pyruvate + NH3
-
D-Ser
-
-
?
Ser + H2O
? + pyruvate + NH3
-
L-Ser
-
-
?
Thr + ?
2-oxobutanoate + ?
-
alpha,beta-elimination
-
?
Thr + ?
2-oxobutanoate + ?
-
D-Thr
-
?
Thr + ?
2-oxobutanoate + ?
-
L-Thr
-
?
Tyr + H2O
phenol + pyruvate + NH3
Aeromonas phenologenes
-
-
-
-
?
Tyr + H2O
phenol + pyruvate + NH3
-
-
-
-
?
Tyr + H2O
phenol + pyruvate + NH3
-
L-Tyr
-
?
Tyr + H2O
phenol + pyruvate + NH3
-
L-Tyr
-
-
?
Tyr + H2O
phenol + pyruvate + NH3
-
-
-
-
?
Tyr + H2O
phenol + pyruvate + NH3
-
L-Tyr
-
-
?
Tyr + H2O
phenol + pyruvate + NH3
-
L-Tyr
-
-
r
Tyr + H2O
phenol + pyruvate + NH3
-
D-Tyr
-
-
?
Tyr + H2O
phenol + pyruvate + NH3
-
-
-
-
?
Tyr + H2O
phenol + pyruvate + NH3
-
-
-
-
?
Tyr + H2O
phenol + pyruvate + NH3
-
-
-
-
?
Tyr + H2O
phenol + pyruvate + NH3
-
-
-
?
Tyr + H2O
phenol + pyruvate + NH3
-
-
-
-
?
Tyr + H2O
phenol + pyruvate + NH3
-
L-Tyr
-
?
Tyr + H2O
phenol + pyruvate + NH3
-
-
-
-
?
Tyr + H2O
phenol + pyruvate + NH3
-
L-Tyr
-
-
?
Tyr + H2O
phenol + pyruvate + NH3
-
D-Tyr
-
-
?
additional information
?
-
-
catalyzes racemization of L-Ala
-
-
?
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
?
-
-
-
-
-
?
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
?
-
-
inducible enzyme
-
-
?
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
?
-
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
?
-
-
inducible enzyme
-
-
?
additional information
?
-
-
-
-
-
?
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0.31 - 0.68
3,4-dihydroxyphenyl-L-alanine
0.0065 - 3
3-chloro-L-Ala
0.18 - 1.4
3-fluoro-L-Tyr
0.012 - 1.4
3-fluoro-L-tyrosine
0.00153
Ala
-
beta-elimination
0.15 - 6
beta-chloro-L-alanine
0.03
L-Ala
-
wild-type enzyme
0.54
L-Dopa
recombinant enzyme, pH 8.5, 20°C
0.00268
L-m-Tyr
-
transamination
0.000034 - 3.5
L-tyrosine
0.15 - 8.3
O-benzoyl-L-Ser
3.9
O-benzyl-L-Cys
wild-type enzyme
0.0008
Phe
-
beta-elimination
0.44
phenol
recombinant enzyme, L-tyrosine formation is measured from phenol, pyruvate, and ammonium, pH 8.5, 20°C
2.68
pyrocatechol
recombinant enzyme, L-DOPA formation is measured from dicatechol, pyruvate, and ammonium, pH 8.5, 20°C
0.26 - 9.7
S-(2-nitrophenyl)-L-cysteine
0.024 - 9.7
S-(o-nitrophenyl)-L-Cys
0.0091 - 7.4
S-(o-nitrophenyl)-L-cysteine
0.02
S-benzoyl-L-Cys
-
mutant enzyme H343A
0.0012 - 0.52
S-benzyl-L-Cys
0.015 - 0.63
S-Benzyl-L-cysteine
0.000217 - 3.88
S-ethyl-L-Cys
0.083 - 5.4
S-ethyl-L-cysteine
0.000383 - 0.9
S-methyl-L-Cys
0.044 - 1.13
S-methyl-L-cysteine
0.2
Tyr
-
beta-elimination
additional information
additional information
-
0.31
3,4-dihydroxyphenyl-L-alanine
-
wild type enzyme, in 0.1 M potassium phosphate buffer (pH 8.0) at 30°C
0.68
3,4-dihydroxyphenyl-L-alanine
-
mutant enzyme T15A, at 30°C
0.0065
3-chloro-L-Ala
-
mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C
0.02
3-chloro-L-Ala
-
mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C
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 25°C
1.13
3-chloro-L-Ala
-
mutant enzyme R100T/V283R
3
3-chloro-L-Ala
-
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 25°C
0.012
3-fluoro-L-tyrosine
recombinant mutant S51A, pH 8.0, 30°C
1.4
3-fluoro-L-tyrosine
recombinant wild-type enzyme, pH 8.0, 30°C
0.15
beta-chloro-L-alanine
recombinant mutant S51A, pH 8.0, 30°C
6
beta-chloro-L-alanine
recombinant wild-type enzyme, pH 8.0, 30°C
0.004
D-Ala
-
mutant enzyme H343A
0.008
D-Ala
-
racemization
0.01
D-Ala
-
wild-type enzyme
0.748
L-Phe
-
-
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
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 25°C
0.000034
L-tyrosine
pH 8.0, 25°C, recombinant mutant F448H
0.00013
L-tyrosine
pH 8.0, 25°C, mutant enzyme K256H
0.00016
L-tyrosine
pH 8.0, 25°C, recombinant mutant F449A
0.00026
L-tyrosine
pH 8.0, 25°C, recombinant mutant F448A
0.001
L-tyrosine
pH 8.0, 25°C, mutant enzyme K256A
0.005
L-tyrosine
pH 8.0, 25°C, recombinant mutant F448L
0.03
L-tyrosine
recombinant mutant S51A, pH 8.0, 30°C
0.12
L-tyrosine
pH 8.0, 25°C, mutant enzyme K256R
1.2
L-tyrosine
-
mutant enzyme T15A, in 0.1 M potassium phosphate buffer (pH 8.0) at 30°C
1.72
L-tyrosine
recombinant enzyme, pH 8.5, 20°C
1.8
L-tyrosine
-
wild type enzyme, in 0.1 M potassium phosphate buffer (pH 8.0) at 30°C
3.5
L-tyrosine
pH 8.0, 25°C, recombinant wild-type enzyme
3.5
L-tyrosine
recombinant wild-type enzyme, pH 8.0, 30°C
0.15
O-benzoyl-L-Ser
-
mutant enzyme Y71F
8.3
O-benzoyl-L-Ser
-
wild-type enzyme
8.3
O-benzoyl-L-Ser
wild-type enzyme
0.26
S-(2-nitrophenyl)-L-cysteine
pH 8.0, 25°C, recombinant mutant F448L
0.36
S-(2-nitrophenyl)-L-cysteine
pH 8.0, 25°C, recombinant mutant F449A
0.6
S-(2-nitrophenyl)-L-cysteine
pH 8.0, 25°C, recombinant mutant F448H
2.5
S-(2-nitrophenyl)-L-cysteine
pH 8.0, 25°C, recombinant mutant F448A
8.7
S-(2-nitrophenyl)-L-cysteine
recombinant mutant S51A, pH 8.0, 30°C
9.65
S-(2-nitrophenyl)-L-cysteine
recombinant wild-type enzyme, pH 8.0, 30°C
9.7
S-(2-nitrophenyl)-L-cysteine
pH 8.0, 25°C, recombinant wild-type enzyme
0.024
S-(o-nitrophenyl)-L-Cys
-
mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C
0.041
S-(o-nitrophenyl)-L-Cys
-
mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C
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
wild-type enzyme
5.1
S-(o-nitrophenyl)-L-Cys
-
wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C
9.7
S-(o-nitrophenyl)-L-Cys
wild-type enzyme
0.0091
S-(o-nitrophenyl)-L-cysteine
pH 8.0, 25°C, mutant enzyme K256A
0.027
S-(o-nitrophenyl)-L-cysteine
pH 8.0, 25°C, mutant enzyme K256H
0.17
S-(o-nitrophenyl)-L-cysteine
pH 8.0, 25°C, mutant enzyme K256R
7.4
S-(o-nitrophenyl)-L-cysteine
pH 8.0, 25°C, mutant enzyme E69D/K256R
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 25°C
0.02
S-benzyl-L-Cys
-
mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C
0.5
S-benzyl-L-Cys
wild-type enzyme
0.5
S-benzyl-L-Cys
-
wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C
0.52
S-benzyl-L-Cys
-
wild-type enzyme
0.015
S-Benzyl-L-cysteine
recombinant mutant S51A, pH 8.0, 30°C
0.63
S-Benzyl-L-cysteine
recombinant wild-type enzyme, pH 8.0, 30°C
0.000217
S-ethyl-L-Cys
-
mutant enzyme Y71F
0.0025
S-ethyl-L-Cys
pH 8.0, 25°C, mutant enzyme K256A
0.0088
S-ethyl-L-Cys
pH 8.0, 25°C, mutant enzyme K256H
0.02
S-ethyl-L-Cys
pH 8.0, 25°C, mutant enzyme K256R
0.37
S-ethyl-L-Cys
pH 8.0, 25°C, mutant enzyme E69D/K256R
1.4
S-ethyl-L-Cys
-
mutant enzyme H343A
1.7
S-ethyl-L-Cys
wild-type enzyme
3.88
S-ethyl-L-Cys
-
wild-type enzyme
0.083
S-ethyl-L-cysteine
recombinant mutant S51A, pH 8.0, 30°C
0.12
S-ethyl-L-cysteine
pH 8.0, 25°C, recombinant mutant F449A
0.23
S-ethyl-L-cysteine
pH 8.0, 25°C, recombinant mutant F448L
0.27
S-ethyl-L-cysteine
pH 8.0, 25°C, recombinant mutant F448H
0.51
S-ethyl-L-cysteine
pH 8.0, 25°C, recombinant mutant F448A
3.9
S-ethyl-L-cysteine
pH 8.0, 25°C, recombinant wild-type enzyme
5.4
S-ethyl-L-cysteine
recombinant wild-type enzyme, pH 8.0, 30°C
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 25°C
0.0052
S-methyl-L-Cys
-
mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C
0.15
S-methyl-L-Cys
-
mutant enzyme H343A
0.9
S-methyl-L-Cys
-
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 25°C
0.044
S-methyl-L-cysteine
recombinant mutant S51A, pH 8.0, 30°C
1.13
S-methyl-L-cysteine
recombinant wild-type enzyme, pH 8.0, 30°C
0.001
Ser
-
transamination
0.012
Ser
-
beta-elimination
additional information
additional information
-
pH-independent kinetic constants for substrates bearing small substituents
-
additional information
additional information
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
-
additional information
additional information
-
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
-
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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
F448A
site-directed mutagenesis, the mutant shows a 104fold reduced activity with L-tyrosine compared to wild-type, stopped-flow kinetics of enzyme mutant F448A. The mutant F448A TPL forms quinonoid intermediates from L-tyrosine and S-ethyl-L-cysteine with rate constants similar to those of wild-type TPL, and can form an aminoacrylate intermediate from S-ethyl-L-cysteine but not L-tyrosine, with a rate constant similar to that of wild-type TPL
F448L
site-directed mutagenesis, the mutant shows a 103fold reduced activity with L-tyrosine compared to wild-type
F448V
-
changed substrate specificity
F449A
site-directed mutagenesis, the mutant shows a 104fold reduced activity with L-tyrosine compared to wild-type
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
N185A
-
2% residual activtiy with L-tyrosine or 3-fluoro-L-tyrosine, N185 stabilizes reaction intermediate
S51A
site-directed mutagenesis, the mutation leads to a decrease of the kcat/Km parameter for reactions with L-tyrosine and 3-fluoro-L-tyrosine by three orders of magnitude, compared to the wild-type enzyme, phenotype, overview. Influence of replacement of Ser51 by Ala on the kinetic parameters of TPL reactions with inhibitory L-phenylalanine and L-methionine, kinetics and structures, overview
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
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
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
F448H
-
site-directed mutagenesis, the mutant enzyme lacks the beta-elimination activity with L-Tyr or 3-fluoro-L-tyrosine as substrates, instead, it accumulates quinonoid intermediate
F448H
site-directed mutagenesis, enzyme mutant crystal structure with bound 3-fluoro-L-tyrosine, tense and closed conformation of F448H TPL quinonoid complex with the ligand, overview
F448H
site-directed mutagenesis, enzyme mutant crystal structure with bound 3-fluoro-L-tyrosine, tense and closed conformation of F448H TPL quinonoid complex with the ligand, overview. Mutant F448H TPL has very low catalytic activity with L-tyrosine compared to wild-type
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
H343A
site-directed mutagenesis, the mutant shows altered kinetics compared to wild-type enzyme
M379V
-
changed substrate specificity
M379V
-
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
R381A
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
R381A
site-directed mutagenesis, the mutant shows very low remaining activity compared to wild-type
R381I
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
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
-
dramatic decrease in activity with L-tyrosine
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
site-directed mutagenesis, the mutant shows very low remaining activity compared to wild-type
T124D
-
no detectable activity with L-tyrosine, but significant activity with other substrates with good leaving groups
T124D
very little activity with L-tyrosine, significant activity with S-(o-nitrophenyl)-L-cysteine, S-alkyl-L-cysteine and beta-chloro-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
Y71F
-
site-directed mutagenesis, the mutant enzyme lacks the beta-elimination activity with L-Tyr or 3-fluoro-L-tyrosine as substrates, instead, it accumulates quinonoid intermediate
Y71F
site-directed mutagenesis, enzyme mutant crystal structure with bound 3-fluoro-L-tyrosine, open conformation of Y71F TPL quinonoid complex with the ligand, overview
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
-
increases the beta-elimination activity towards dicarboxylic amino acids, L-Asp, L-Glu and L-2-aminoadipate at least 10000-fold
-
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
L-dihydroxyphenylalanine (DOPA) is biosynthesized by a tyrosine-phenol lyase from catechol, pyruvate, and ammonia in recombinant Escherichia coli expressing the enzyme, and the biosynthesized amino acid is directly incorporated into proteins. Three biochemical experiments with mutant proteins containing DOPA confirm the genetic incorporation of biosynthesized DOPA, and reveal its potential for various biochemical applications
additional information
-
L-dihydroxyphenylalanine (DOPA) is biosynthesized by a tyrosine-phenol lyase from catechol, pyruvate, and ammonia in recombinant Escherichia coli expressing the enzyme, and the biosynthesized amino acid is directly incorporated into proteins. Three biochemical experiments with mutant proteins containing DOPA confirm the genetic incorporation of biosynthesized DOPA, and reveal its potential for various biochemical applications
-
additional information
-
sRNA-based knockdown of the two regulators and overexpression of the genes involved in the tyrosine biosynthetic pathway together with tyrosine phenol-lyase in Escherichia coli strains results in the production of phenol from glucose. The 18 engineered strains show significant differences in the production of tyrosine (i.e. the immediate precursor for phenol), TPL activity, and tolerance to phenol, overview. Engineered Escherichia coli strain BL21 produces phenol most efficiently by flask culture or fed-batch culture
additional information
the tyrosine phenol lyase (TPL) catalyzed synthesis of L-DOPA is regarded as one of the most economic routes for L-DOPA synthesis, usage in a fed-batch approach with sodium pyruvate, dicatechol and ammonium acetate. In addition, L-DOPA crystals are exogenously added to inhibit cell encapsulation by the precipitated product. The final L-DOPA concentration reaches higher than 120 g/l with dicatechol conversion more than 96% in a 15-l stirred tank, demonstrating the great potential of Fn-TPL for industrial production of L-DOPA. Optimization of reaction conditions and upscaling of the recombinant enzyme TPL from Fusobacterium nucleatum in enzyme-expressing Escherichia coli cells, detailed overview
additional information
-
the tyrosine phenol lyase (TPL) catalyzed synthesis of L-DOPA is regarded as one of the most economic routes for L-DOPA synthesis, usage in a fed-batch approach with sodium pyruvate, dicatechol and ammonium acetate. In addition, L-DOPA crystals are exogenously added to inhibit cell encapsulation by the precipitated product. The final L-DOPA concentration reaches higher than 120 g/l with dicatechol conversion more than 96% in a 15-l stirred tank, demonstrating the great potential of Fn-TPL for industrial production of L-DOPA. Optimization of reaction conditions and upscaling of the recombinant enzyme TPL from Fusobacterium nucleatum in enzyme-expressing Escherichia coli cells, detailed overview
-
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Kiick, D.M.; Phillips, R.S.
Mechanistic deductions from kinetic isotope effects and pH studies of pyridoxal phosphate dependent carbon-carbon lyases: Erwinia herbicola and Citrobacter freundii tyrosine phenol-lyase
Biochemistry
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7333-7338
1988
Citrobacter freundii, Pantoea agglomerans
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1988
Citrobacter freundii
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Citrobacter intermedius
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Stereochemistry and mechanism of reactions catalyzed by tyrosine phenol-lyase from Escherichia intermedia
Z. Naturforsch. C
42
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1987
Citrobacter intermedius
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Location of tyrosine phenol-lyase in some Gram-negative bacteria
FEMS Microbiol. Lett.
30
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1985
Citrobacter intermedius, Escherichia coli, Morganella morganii
-
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Properties of stearylamine liposomes containing tyrosine phenol-lyase
Biochim. Biophys. Acta
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177-186
1981
Pantoea agglomerans
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Nagasawa, T.; Utagawa, T.; Goto, J.; Kim, C.J.; Tani Y.; Kumagai, H.; Yamada, H.
Syntheses of L-tyrosine-related amino acids by tyrosine phenol-lyase of Citrobacter intermedius
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Citrobacter intermedius
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Catalytic properties of extracts from tyrosine phenol lyase producing cells of Escherichia intermedia: multienzyme complex instead of the single multisubstrate enzyme
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1981
Citrobacter intermedius
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McKenzie, D.; Robb, D.A.
The periplasmic location of tyrosine phenol-lyase in Erwinia herbicola
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9
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Pantoea agglomerans
-
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Reactions of partially purified tyrosine phenol lyase with threonine and other amino acids
Enzyme Microb. Technol.
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Citrobacter intermedius
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Muro, T.; Nakatani, H.; Hiromi, K.; Kumagai, H.; Yamada, H.
Elementary processes in the interaction of tyrosine phenol lyase with inhibitors and substrate
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Citrobacter intermedius
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Partial purification and some properties of tyrosine phenol-lyase from Aeromonas phenologenes ATCC 29063
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1977
Aeromonas phenologenes
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Yamada, H.; Kumagai, H.
Synthesis of L-tyrosine-related amino acids by beta-tyrosinase
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Citrobacter intermedius, Pantoea agglomerans
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Elimination, replacement and isomerization reactions by intact cells containing tyrosine phenol lyase
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Pantoea agglomerans, Pantoea agglomerans ATCC 21434
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Bacillus cereus, Citrobacter freundii, Citrobacter intermedius, Escherichia coli, Klebsiella aerogenes, Morganella morganii, Pantoea agglomerans, Pseudomonas pelurida, Pseudomonas trifolii, Salmonella enterica subsp. enterica serovar Typhimurium, Xanthomonas campestris
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Purification, crystallization and properties of tyrosine phenol lyase from Erwinia herbicola
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Pantoea agglomerans
-
brenda
Yamada, H.; Kumagai, H.; Kashima, N.; Torii, H.; Enei, H.; Okumura, S.
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1972
Citrobacter intermedius
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Citrobacter intermedius
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Citrobacter intermedius
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Symbiobacterium sp., Symbiobacterium sp. SMH1
-
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1996
Pantoea agglomerans
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Site-directed mutagenesis of His343-->Ala in Citrobacter freundii tyrosine phenol-lyase. Effects on the kinetic mechanism and rate-determining step
Eur. J. Biochem.
229
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1995
Citrobacter freundii
brenda
Foor, F.; Morin, N.; Bostian, K.A.
Production of L-dihydroxyphenylalanine in Escherichia coli with the tyrosine phenol-lyase gene cloned from Erwinia herbicola
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59
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1993
Pantoea agglomerans
brenda
Hirahara, T.; Horinouchi, S.; Beppu, T.
Cloning, nucleotide sequence, and overexpression in Escherichia coli of the beta-tyrosinase gene from an obligately symbiotic thermophile, Symbiobacterium thermophilum
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39
341-346
1993
Symbiobacterium thermophilum
brenda
Suzuki, S.; Hirahara, T.; Shim, J.K.; Horinouchi, S.; Beppu, T.
Purification and properties of thermostable beta-tyrosinase from an obligate symbiotic thermophile, Symbiobacterium thermophilum
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56
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1992
Symbiobacterium thermophilum
-
brenda
Anderson, W.A.; Moo-Young, M.; Legge, R.L.
Development of a multienzyme reactor for dopamine synthesis: I. Enzymology and kinetics
Biotechnol. Bioeng.
39
781-789
1992
Pantoea agglomerans
brenda
Faleev, N.G.; Spirina, S.N.; Ivoilov, V.S.; Demidkina, T.V.; Phillips, R.S.
The catalytic mechanism of tyrosine phenol-lyase from Erwinia herbicola: the effect of substrate structure on pH-dependence of kinetic parameters in the reactions with ring-substituted tyrosines
Z. Naturforsch. C
51
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1996
Pantoea agglomerans
brenda
Lee, S.G.; Hong, S.P.; Choi, Y.H.; Chung, Y.J.; Sung, M.H.
Thermostable tyrosine phenol-lyase of Symbiobacterium sp. SC-1: gene cloning, sequence determination, and overproduction in Escherichia coli
Protein Expr. Purif.
11
263-270
1997
Symbiobacterium sp., Symbiobacterium sp. SC-1
brenda
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Binding of phenol and analogues to alanine complexes of tyrosine phenol-lyase from Citrobacter freundii: implications for the mechanisms of alpha,beta-elimination and alanine racemization
Biochemistry
32
11591-11599
1993
Citrobacter freundii
brenda
Sundaraju, B.; Antson, A.A.; Phillips, R.S.; Demidkina, T.V.; Barbolina, M.V.; Gollnick, P.; Dodson, G.G.; Wilson, K.S.
The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4 -hydroxyphenyl)propionic acid, together with site-directed mutagenesis and kinetic analysis, demonstrates that arginine 381 is required for substrate specificity
Biochemistry
36
6502-6510
1997
Citrobacter freundii (P31013), Citrobacter freundii
brenda
Chen, H.Y.; Demidkina, T.V.; Phillips, R.S.
Site-directed mutagenesis of tyrosine-71 to phenylalanine in Citrobacter freundii tyrosine phenol-lyase: evidence for dual roles of tyrosine-71 as a general acid catalyst in the reaction mechanism and in cofactor binding
Biochemistry
34
12276-12283
1995
Citrobacter freundii
brenda
Mouratou, B.; Kasper, P.; Gehring, H.; Christen, P.
Conversion of tyrosine phenol-lyase to dicarboxylic amino acid beta-lyase, an enzyme not found in nature
J. Biol. Chem.
274
1320-1325
1999
Escherichia coli, Escherichia coli SV370
brenda
Demidkina, T.V.; Barbolina, M.V.; Faleev, N.G.; Sundararaju, B.; Gollnick, P.D.; Phillips, R.S.
Threonine-124 and phenylalanine-448 in Citrobacter freundii tyrosine phenol-lyase are necessary for activity with L-tyrosine
Biochem. J.
363
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2002
Citrobacter freundii (P31013), Citrobacter freundii
brenda
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Inhibition of tyrosine phenol-lyase from Citrobacter freundii by 2-azatyrosine and 3-azatyrosine
Biochemistry
40
14862-14868
2001
Citrobacter freundii
brenda
Phillips, R.S.; Demidkina, T.V.; Faleev, N.G.
Structure and mechanism of tryptophan indole-lyase and tyrosine phenol-lyase
Biochim. Biophys. Acta
1647
167-172
2003
Citrobacter freundii
brenda
Faleev, N.G.; Axenova, O.V.; Demidkina, T.V.; Phillips, R.S.
The role of acidic dissociation of substrate's phenol group in the mechanism of tyrosine phenol-lyase
Biochim. Biophys. Acta
1647
260-265
2003
Citrobacter intermedius
brenda
Bazhulina, N.P.; Morozov, Y.V.; Papisova, A.I.; Demidkina, T.V.
Pyridoxal 5'-phoshate schiff base in Citrobacter freundii tyrosinephenol-lyase. Ionic and tautomeric equilibria
Eur. J. Biochem.
267
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2000
Citrobacter freundii
brenda
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Interaction of tyrosine phenol-lyase with phosphoroorganic analogues of substrate amino acids
Eur. J. Biochem.
267
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2000
Citrobacter intermedius
brenda
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Characterization of thermostable tyrosine phenol-lyase from an obligatory symbiotic thermophile, Symbiobacterium sp. SC-1
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32
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1999
Symbiobacterium sp., Symbiobacterium sp. SC-1
-
brenda
Phillips, R.S.; Demidkina, T.V.; Zakomirdina, L.N.; Bruno, S.; Ronda, L.; Mozzarelli, A.
Crystals of tryptophan indole-lyase and tyrosine phenol-lyase form stable quinonoid complexes
J. Biol. Chem.
277
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2002
Citrobacter freundii
brenda
Barbolina, M.V.; Phillips, R.S.; Gollnick, P.D.; Faleev, N.G.; Demidkina, T.V.
Citrobacter freundii tyrosine phenol-lyase: the role of asparagine 185 in modulating enzyme function through stabilization of a quinonoid intermediate
Protein Eng.
13
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2000
Citrobacter freundii
brenda
Pioselli, B.; Bettati, S.; Demidkina, T.V.; Zakomirdina, L.N.; Phillips, R.S.; Mozzarelli, A.
Tyrosine phenol-lyase and tryptophan indole-lyase encapsulated in wet nanoporous silica gels: Selective stabilization of tertiary conformations
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2004
Citrobacter freundii
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Yamada, H.
Screening of novel enzymes for the production of useful compounds, in: New Frontiers in Screening for Microbial Biocatalysis
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13-17
1998
Pantoea agglomerans
-
brenda
Phillips, R.S.; Chen, H.Y.; Shim, D.; Lima, S.; Tavakoli, K.; Sundararaju, B.
Role of lysine-256 in Citrobacter freundii tyrosine phenol-lyase in monovalent cation activation
Biochemistry
43
14412-14419
2004
Citrobacter freundii (P31013), Citrobacter freundii
brenda
Schnackerz, K.D.; Keller, J.; Phillips, R.S.; Toney, M.D.
Ionization state of pyridoxal 5'-phosphate in d-serine dehydratase, dialkylglycine decarboxylase and tyrosine phenol-lyase and the influence of monovalent cations as inferred by (31)P NMR spectroscopy
Biochim. Biophys. Acta
1764
230-238
2006
Citrobacter freundii
brenda
Faleev, N.G.; Demidkina, T.V.; Tsvetikova, M.A.; Phillips, R.S.; Yamskov, I.A.
The mechanism of alpha-proton isotope exchange in amino acids catalysed by tyrosine phenol-lyase. What is the role of quinonoid intermediates?
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271
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2004
Citrobacter freundii
brenda
Koralewska, A.; Augustyniak, W.; Temeriusz, A.; Kanska, M.
Effects of cyclodextrin derivatives on the catalytic activity of tyrosine phenol-lyase
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49
193-197
2004
Citrobacter freundii
-
brenda
Kim, J.H.; Song, J.J.; Kim, B.G.; Sung, M.H.; Lee, S.C.
Enhanced stability of tyrosine phenol-lyase from Symbiobacterium toebii by DNA shuffling
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14
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2004
Symbiobacterium toebii
-
brenda
Milic, D.; Matkovic-Calogovic, D.; Demidkina, T.V.; Kulikova, V.V.; Sinitzina, N.I.; Antson, A.A.
Structures of apo- and holo-tyrosine phenol-lyase reveal a catalytically critical closed conformation and suggest a mechanism for activation by K+ ions
Biochemistry
45
7544-7552
2006
Citrobacter freundii (P31013), Citrobacter freundii
brenda
Phillips, R.S.; Chen, H.Y.; Faleev, N.G.
Aminoacrylate intermediates in the reaction of Citrobacter freundii tyrosine phenol-lyase
Biochemistry
45
9575-9583
2006
Citrobacter freundii
brenda
Demidkina, T.V.; Faleev, N.G.; Papisova, A.I.; Bazhulina, N.P.; Kulikova, V.V.; Gollnick, P.D.; Phillips, R.S.
Aspartic acid 214 in Citrobacter freundii tyrosine phenol-lyase ensures sufficient C--H-acidity of the external aldimine intermediate and proper orientation of the cofactor at the active site
Biochim. Biophys. Acta
1764
1268-1276
2006
Citrobacter freundii
brenda
Lee, S.G.; Hong, S.P.; Kim, D.Y.; Song, J.J.; Ro, H.S.; Sung, M.H.
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2006
Citrobacter freundii
brenda
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Development of bioreactor system for L-tyrosine synthesis using thermostable tyrosine phenol-lyase
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17
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2007
Symbiobacterium toebii
brenda
Chandel, M.; Azmi, W.
Optimization of process parameters for the production of tyrosine phenol lyase by Citrobacter freundii MTCC 2424
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2008
Pseudomonas putida
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283
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Citrobacter freundii (P31013), Citrobacter freundii
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Hyperproduction of 3,4-dihydroxyphenyl-L-alanine (L-Dopa) using Erwinia herbicola cells carrying a mutant transcriptional regulator TyrR
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2009
Pantoea agglomerans
brenda
Kurt, A.G.; Aytan, E.; Ozer, U.; Ates, B.; Geckil, H.
Production of L-DOPA and dopamine in recombinant bacteria bearing the Vitreoscilla hemoglobin gene
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2009
Citrobacter freundii, Pantoea agglomerans, Pantoea agglomerans NRRL B-3466, Citrobacter freundii NRRL B-2643
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276
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2009
Symbiobacterium toebii
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Cutting long syntheses short: Access to non-natural tyrosine derivatives employing an engineered tyrosine phenol lyase
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352
731-736
2010
Citrobacter freundii
-
brenda
Koulikova, V.; Zakomirdina, L.; Gogoleva, O.; Tsvetikova, M.; Morozova, E.; Komissarov, V.; Tkachev, Y.; Timofeev, V.; Demidkina, T.; Faleev, N.
Stereospecificity of isotopic exchange of C-alpha-protons of glycine catalyzed by three PLP-dependent lyases: the unusual case of tyrosine phenol-lyase
Amino Acids
41
1247-1256
2010
Citrobacter freundii
brenda
Azmi, W.; Kumar, A.; Dev, V.
Paraffin as oxygen vector modulates tyrosine phenol lyase production by Citrobacter freundii MTCC 2424
Acta Microbiol. Immunol. Hung.
60
145-154
2013
Citrobacter freundii, Citrobacter freundii MTCC 2424
brenda
Chandel, M.; Azmi, W.
Purification and characterization of tyrosine phenol lyase from Citrobacter freundii
Appl. Biochem. Biotechnol.
171
2040-2052
2013
Citrobacter freundii
brenda
Kim, B.; Park, H.; Na, D.; Lee, S.Y.
Metabolic engineering of Escherichia coli for the production of phenol from glucose
Biotechnol. J.
9
621-629
2014
Escherichia coli
brenda
Milic, D.; Demidkina, T.V.; Faleev, N.G.; Phillips, R.S.; Matkovic-Calogovic, D.; Antson, A.A.
Crystallographic snapshots of tyrosine phenol-lyase show that substrate strain plays a role in C-C bond cleavage
J. Am. Chem. Soc.
133
16468-16476
2011
Citrobacter freundii
brenda
Phillips, R.; Vita, A.; Spivey, J.; Rudloff, A.; Driscoll, M.; Hay, S.
Ground-state destabilization by Phe-448 and Phe-449 contributes to tyrosine phenol-lyase catalysis
ACS Catal.
6
6770-6779
2016
Citrobacter freundii (P31013)
-
brenda
Do, Q.; Nguyen, G.T.; Phillips, R.S.
Inhibition of tyrosine phenol-lyase by tyrosine homologues
Amino Acids
48
2243-2251
2016
Citrobacter freundii (P31013)
brenda
Miao, L.; Li, Q.; Diao, A.; Zhang, X.; Ma, Y.
Construction of a novel phenol synthetic pathway in Escherichia coli through 4-hydroxybenzoate decarboxylation
Appl. Microbiol. Biotechnol.
99
5163-5173
2015
Citrobacter freundii (P31013)
brenda
Phillips, R.S.; Demidkina, T.V.; Faleev, N.G.
The role of substrate strain in the mechanism of the carbon-carbon lyases
Bioorg. Chem.
57
198-205
2014
Citrobacter freundii (P31013)
brenda
Tang, X.L.; Liu, X.; Suo, H.; Wang, Z.C.; Zheng, R.C.; Zheng, Y.G.
Process development for efficient biosynthesis of L-DOPA with recombinant Escherichia coli harboring tyrosine phenol lyase from Fusobacterium nucleatum
Bioprocess Biosyst. Eng.
41
1347-1354
2018
Fusobacterium nucleatum subsp. nucleatum (Q8RHM6), Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131 (Q8RHM6)
brenda
Kim, S.; Sung, B.H.; Kim, S.C.; Lee, H.S.
Genetic incorporation of l-dihydroxyphenylalanine (DOPA) biosynthesized by a tyrosine phenol-lyase
Chem. Commun. (Camb.)
54
3002-3005
2018
Citrobacter freundii (P31013), Citrobacter freundii ATCC 8090 (P31013)
brenda
Zheng, R.C.; Tang, X.L.; Suo, H.; Feng, L.L.; Liu, X.; Yang, J.; Zheng, Y.G.
Biochemical characterization of a novel tyrosine phenol-lyase from Fusobacterium nucleatum for highly efficient biosynthesis of L-DOPA
Enzyme Microb. Technol.
112
88-93
2018
Fusobacterium nucleatum subsp. nucleatum (Q8RHM6), Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131 (Q8RHM6)
brenda