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
Sundaraju, B.; Antson, A.A.; Phillips, R.S.; Demidkina, T.V.; Barbolina, M.V.; Gollnick, P.; Dodson, G.G.; Wilson, K.S.; Biochemistry 36, 6502-6510 (1997) 
Data extracted from this reference:
Crystallization (Commentary)
EC Number
Crystallization (Commentary)
Organism
4.1.99.2
tyrosine phenol-lyase complexed with 3-(4'-hydroxyphenyl)propionic acid
Citrobacter freundii
Engineering
EC Number
Protein Variants
Commentary
Organism
4.1.99.2
R381A
beta-elimination activity has been reduced by 0.0001fold compared to wild type enzyme
Citrobacter freundii
4.1.99.2
R381I
no detectable beta-elimination activity with L-Tyr as substrate
Citrobacter freundii
4.1.99.2
R381V
no detectable beta-elimination activity with L-Tyr as substrate
Citrobacter freundii
Organism
EC Number
Organism
UniProt
Commentary
Textmining
4.1.99.2
Citrobacter freundii
P31013
wild type enzyme and mutant enzymes R381A, R381V and R381I
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
4.1.99.2
O-benzoyl-L-Ser + H2O
-
33470
Citrobacter freundii
?
-
-
-
?
4.1.99.2
O-benzyl-L-Cys + H2O
-
33470
Citrobacter freundii
?
-
-
-
?
4.1.99.2
O-benzyl-L-Ser + H2O
-
33470
Citrobacter freundii
?
-
-
-
?
4.1.99.2
S-benzyl-L-Cys + H2O
-
33470
Citrobacter freundii
? + pyruvate + NH3
-
-
-
?
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.1.99.2
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
Citrobacter freundii
4.1.99.2
0.5
-
S-benzyl-L-Cys
wild-type enzyme
Citrobacter freundii
4.1.99.2
0.9
-
S-methyl-L-Cys
wild-type enzyme
Citrobacter freundii
4.1.99.2
1.7
-
S-ethyl-L-Cys
wild-type enzyme
Citrobacter freundii
4.1.99.2
2.2
-
L-Tyr
wild-type enzyme
Citrobacter freundii
4.1.99.2
3
-
3-chloro-L-Ala
wild-type enzyme
Citrobacter freundii
4.1.99.2
3.9
-
O-benzyl-L-Cys
wild-type enzyme
Citrobacter freundii
4.1.99.2
5.1
-
S-(o-nitrophenyl)-L-Cys
wild-type enzyme
Citrobacter freundii
4.1.99.2
8.3
-
O-benzoyl-L-Ser
wild-type enzyme
Citrobacter freundii
4.1.99.2
9.7
-
S-(o-nitrophenyl)-L-Cys
wild-type enzyme
Citrobacter freundii
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
4.1.99.2
tyrosine phenol-lyase complexed with 3-(4'-hydroxyphenyl)propionic acid
Citrobacter freundii
Engineering (protein specific)
EC Number
Protein Variants
Commentary
Organism
4.1.99.2
R381A
beta-elimination activity has been reduced by 0.0001fold compared to wild type enzyme
Citrobacter freundii
4.1.99.2
R381I
no detectable beta-elimination activity with L-Tyr as substrate
Citrobacter freundii
4.1.99.2
R381V
no detectable beta-elimination activity with L-Tyr as substrate
Citrobacter freundii
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
4.1.99.2
O-benzoyl-L-Ser + H2O
-
33470
Citrobacter freundii
?
-
-
-
?
4.1.99.2
O-benzyl-L-Cys + H2O
-
33470
Citrobacter freundii
?
-
-
-
?
4.1.99.2
O-benzyl-L-Ser + H2O
-
33470
Citrobacter freundii
?
-
-
-
?
4.1.99.2
S-benzyl-L-Cys + H2O
-
33470
Citrobacter freundii
? + pyruvate + NH3
-
-
-
?
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.1.99.2
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
Citrobacter freundii
4.1.99.2
0.5
-
S-benzyl-L-Cys
wild-type enzyme
Citrobacter freundii
4.1.99.2
0.9
-
S-methyl-L-Cys
wild-type enzyme
Citrobacter freundii
4.1.99.2
1.7
-
S-ethyl-L-Cys
wild-type enzyme
Citrobacter freundii
4.1.99.2
2.2
-
L-Tyr
wild-type enzyme
Citrobacter freundii
4.1.99.2
3
-
3-chloro-L-Ala
wild-type enzyme
Citrobacter freundii
4.1.99.2
3.9
-
O-benzyl-L-Cys
wild-type enzyme
Citrobacter freundii
4.1.99.2
5.1
-
S-(o-nitrophenyl)-L-Cys
wild-type enzyme
Citrobacter freundii
4.1.99.2
8.3
-
O-benzoyl-L-Ser
wild-type enzyme
Citrobacter freundii
4.1.99.2
9.7
-
S-(o-nitrophenyl)-L-Cys
wild-type enzyme
Citrobacter freundii