Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-oxindolyl-L-alanine + H2O
?
-
-
-
?
4-methyl-Trp + H2O
?
-
52% of the activity with L-Trp
-
-
?
5-hydroxyindole + L-Cys
5-hydroxy-L-Trp + ?
-
-
-
-
?
5-hydroxyindole + S-methyl-L-Cys
5-hydroxy-L-Trp + ?
-
-
-
-
?
5-methylindole + L-Cys
5-methyl-L-Trp + ?
-
-
-
-
?
5-methylindole + S-methyl-L-Cys
5-methyl-L-Trp + ?
-
-
-
-
?
6-methyl-Trp + H2O
?
-
44% of the activity with L-Trp
-
-
?
alpha,beta-diaminopropionic acid
?
-
-
-
-
?
beta-(benzimidazol-1-yl)-L-alanine + H2O
?
beta-chloro-L-Ala + H2O
?
beta-chloroalanine + H2O
?
beta-chloroalanine + H2O
pyruvate + NH4+ + Cl-
-
-
-
-
?
cysteine sulfinic acid + H2O
?
-
-
-
-
?
D-serine
pyruvate + NH3
-
with high diammonium hydrogen phosphate concentration, e.g. 1.2 M
-
-
?
D-serine + indole
L-tryptophan + H2O
D-Trp + H2O
indole + pyruvate + NH4+
indole + L-Ser
L-Trp + ?
-
-
-
?
indole + pyruvate + NH4+
L-Trp + H2O
indole + S-methyl-L-Cys
L-Trp + ?
L-Ser + H2O
pyruvate + H2O
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
-
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH3
-
effects of temperature and hydrostatic pressure on the equilibria and rate constants for quinoid intermediate formation from L-Trp and L-Met with H463 mutant enzyme
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
L-Trp + H2O
pyruvate + NH3 + indole
L-tryptophan + H2O
indole + pyruvate + NH3
O-benzylserine + H2O
?
-
-
-
-
?
O-methylserine + H2O
?
-
-
-
-
?
oxindolyl-L-alanine + H2O
?
OIA, transition state analogue, the reaction of enzyme TIL mutant Y72F with OIA is accompanied by the appearance of intense absorption at 509 nm which may be explained by the formation of a quinonoid intermediate, transformation of the external aldimine into the quinonoid intermediate implies the transfer of alpha-proton to the base-acceptor in the active site. Oxindolyl-L-alanine also inhibits the enzyme
-
-
?
S-(2-nitrophenyl)-L-cysteine + H2O
2-nitrobenzenethiolate + pyruvate + NH3
S-(2-nitrophenyl)-L-cysteine + H2O
?
-
-
-
-
r
S-(o-nitrophenyl)-L-cysteine
?
-
-
-
?
S-benzyl-L-Cys + H2O
phenylmethanethiol + pyruvate + NH4+
S-benzyl-L-cysteine + H2O
phenylmethanethiol + pyruvate + NH3
S-benzylcysteine + H2O
pyruvate + NH4+ + phenylmethanethiol
-
-
-
-
?
S-ethyl-L-Cys + H2O
ethanethiol + pyruvate + NH4+
S-ethyl-L-cysteine + H2O
?
S-ethyl-L-cysteine + H2O
ethanethiol + pyruvate + NH3
S-ethyl-L-cysteine + H2O
ethanethiol + pyruvate + NH4+
S-ethyl-L-cysteine + H2O
pyruvate + NH4+ + ethanethiol
-
-
-
-
?
S-ethylcysteine + H2O
?
-
-
-
-
?
S-methyl-L-Cys + H2O
methanethiol + pyruvate + NH4+
S-methyl-L-Cys + H2O
pyruvate + NH4+ + methanethiol
-
-
-
-
?
S-methyl-L-Cys + indole
Trp + ?
S-methyl-L-cysteine
?
-
-
-
?
S-methyl-L-cysteine + H2O
?
S-methyl-L-cysteine + H2O
methanethiol + pyruvate + NH3
S-methyl-L-cysteine + H2O
methanethiol + pyruvate + NH4+
S-o-nitrophenyl-L-Cys + H2O
o-nitrothiophenol + pyruvate + NH3
S-o-nitrophenyl-L-Cys + indole
Trp + ?
-
reaction readily proceeds in water, it becomes impossible in water-organic solvents
-
?
S-o-nitrophenyl-L-cysteine + H2O
o-nitrothiophenol + pyruvate + NH4+
-
-
-
-
?
additional information
?
-
5-hydroxy-L-Trp + H2O
?
-
6% of the activity with L-Trp
-
-
?
5-hydroxy-L-Trp + H2O
?
-
14.3% of the activity with L-Trp
-
-
?
5-hydroxy-L-Trp + H2O
?
-
6.7% of the activity with L-Trp
-
-
?
5-hydroxy-L-Trp + H2O
?
-
6.7% of the activity with L-Trp
-
-
?
5-methyl-L-Trp + H2O
?
-
22% of the activity with L-Trp
-
-
?
5-methyl-L-Trp + H2O
?
-
21.1% of the activity with L-Trp
-
-
?
5-methyl-L-Trp + H2O
?
-
15.2% of the activity with L-Trp
-
-
?
5-methyl-L-Trp + H2O
?
-
15.2% of the activity with L-Trp
-
-
?
beta-(benzimidazol-1-yl)-L-alanine + H2O
?
-
reaction via aldimine intermediate, high activity with wild-type enzyme and mutant H463F
-
-
?
beta-(benzimidazol-1-yl)-L-alanine + H2O
?
-
reaction via aldimine intermediate, high activity with wild-type enzyme and mutant H463F
-
-
?
beta-chloro-L-Ala + H2O
?
-
-
-
-
?
beta-chloro-L-Ala + H2O
?
-
-
-
?
beta-chloro-L-Ala + H2O
?
-
-
-
?
beta-chloroalanine + H2O
?
-
-
-
-
?
beta-chloroalanine + H2O
?
-
-
-
-
?
Cys + H2O
?
-
-
-
-
?
Cys + H2O
?
-
36.4% of the activity with L-Trp
-
-
?
Cys + H2O
?
-
L-Cys
-
-
?
Cys + H2O
?
-
L-Cys
-
-
?
Cys + H2O
?
-
18.9% of the activity with L-Trp
-
-
?
Cys + H2O
?
-
L-Cys
-
-
?
Cys + H2O
?
-
18.9% of the activity with L-Trp
-
-
?
Cys + H2O
?
-
L-Cys
-
-
?
Cys + indole
Trp + ?
-
-
-
?
Cys + indole
Trp + ?
-
-
-
?
Cys + indole
Trp + ?
-
-
-
?
D-serine + indole
L-tryptophan + H2O
-
the presence of 20% saturation concentration of diammonium hydrogen phosphate is required for this reaction
-
-
?
D-serine + indole
L-tryptophan + H2O
-
with high diammonium hydrogen phosphate concentration, e.g. 1.2 M
-
-
?
D-Trp + H2O
indole + pyruvate + NH4+
in the presence of high concentrations of ammonium phosphate
-
-
?
D-Trp + H2O
indole + pyruvate + NH4+
in the presence of high concentrations of ammonium phosphate
-
-
?
indole + L-Cys
L-Trp + ?
-
-
-
?
indole + L-Cys
L-Trp + ?
-
beta-replacement reaction
-
?
indole + L-Cys
L-Trp + ?
-
beta-replacement reaction
-
?
indole + pyruvate + NH4+
L-Trp + H2O
-
-
-
?
indole + pyruvate + NH4+
L-Trp + H2O
-
-
-
?
indole + pyruvate + NH4+
L-Trp + H2O
-
-
-
?
indole + pyruvate + NH4+
L-Trp + H2O
-
-
-
?
indole + S-methyl-L-Cys
L-Trp + ?
-
-
-
?
indole + S-methyl-L-Cys
L-Trp + ?
-
beta-replacement reaction
-
?
indole + S-methyl-L-Cys
L-Trp + ?
-
beta-replacement reaction
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
Escherichia aurescens
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
Escherichia aurescens
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
Escherichia aurescens
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
-
r
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
r
L-Trp + H2O
indole + pyruvate + NH4+
-
the product indole is involved in cell signaling, involved in cell cycle regulation
-
-
r
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
r
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
Paracolobactrum coliforme
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
Paracolobactrum sp.
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
Shigella alkalescens
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
Shigella alkalescens
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
Shigella alkalescens
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
pyruvate + NH3 + indole
-
-
-
-
?
L-Trp + H2O
pyruvate + NH3 + indole
-
-
-
-
?
L-tryptophan + H2O
indole + pyruvate + NH3
-
-
-
-
?
L-tryptophan + H2O
indole + pyruvate + NH3
-
-
-
-
r
L-tryptophan + H2O
indole + pyruvate + NH3
-
-
-
?
L-tryptophan + H2O
indole + pyruvate + NH3
-
-
-
-
?
L-tryptophan + H2O
indole + pyruvate + NH3
-
-
-
r
L-tryptophan + H2O
indole + pyruvate + NH3
-
-
-
-
r
L-tryptophan + H2O
indole + pyruvate + NH3
-
active to D-tryptophan in highly concentrated diammonium hydrogen phosphate solution
-
-
?
L-tryptophan + H2O
indole + pyruvate + NH3
-
reversible hydrolytic beta-elimination
-
-
r
L-tryptophan + H2O
indole + pyruvate + NH3
Tnase can act in reverse to form L-tryptophan at high concentrations of pyruvate and ammonia
-
-
r
L-tryptophan + H2O
indole + pyruvate + NH3
very high substrate specificity of TIL
-
-
?
L-tryptophan + H2O
indole + pyruvate + NH3
-
-
-
-
?
L-tryptophan + H2O
indole + pyruvate + NH3
-
-
-
-
?
L-tryptophan + H2O
indole + pyruvate + NH3
-
-
-
r
L-tryptophan + H2O
indole + pyruvate + NH3
-
-
-
r
L-tryptophan + H2O
indole + pyruvate + NH3
-
-
-
?
L-tryptophan + H2O
indole + pyruvate + NH3
-
-
-
?
L-tryptophan + H2O
indole + pyruvate + NH3
-
-
-
?
L-tryptophan + H2O
indole + pyruvate + NH3
-
-
-
-
?
L-tryptophan + H2O
indole + pyruvate + NH3
very high substrate specificity of TIL
-
-
?
L-tryptophan + H2O
indole + pyruvate + NH3
-
-
-
?
L-tryptophan + H2O
indole + pyruvate + NH3
-
-
-
?
L-tryptophan + H2O
indole + pyruvate + NH3
-
-
-
?
L-tryptophan + H2O
indole + pyruvate + NH3
-
-
-
?
S-(2-nitrophenyl)-L-cysteine + H2O
2-nitrobenzenethiolate + pyruvate + NH3
-
-
-
-
?
S-(2-nitrophenyl)-L-cysteine + H2O
2-nitrobenzenethiolate + pyruvate + NH3
-
-
-
-
ir
S-(2-nitrophenyl)-L-cysteine + H2O
2-nitrobenzenethiolate + pyruvate + NH3
-
-
-
?
S-(2-nitrophenyl)-L-cysteine + H2O
2-nitrobenzenethiolate + pyruvate + NH3
-
-
-
?
S-(2-nitrophenyl)-L-cysteine + H2O
2-nitrobenzenethiolate + pyruvate + NH3
-
-
-
?
S-(2-nitrophenyl)-L-cysteine + H2O
2-nitrobenzenethiolate + pyruvate + NH3
-
-
-
?
S-benzyl-L-Cys + H2O
phenylmethanethiol + pyruvate + NH4+
-
-
-
-
?
S-benzyl-L-Cys + H2O
phenylmethanethiol + pyruvate + NH4+
-
-
-
?
S-benzyl-L-Cys + H2O
phenylmethanethiol + pyruvate + NH4+
-
-
-
?
S-benzyl-L-cysteine + H2O
phenylmethanethiol + pyruvate + NH3
-
-
-
?
S-benzyl-L-cysteine + H2O
phenylmethanethiol + pyruvate + NH3
-
-
-
?
S-benzylcysteine + H2O
?
-
-
-
-
?
S-benzylcysteine + H2O
?
-
-
-
-
?
S-ethyl-L-Cys + H2O
ethanethiol + pyruvate + NH4+
-
-
-
-
?
S-ethyl-L-Cys + H2O
ethanethiol + pyruvate + NH4+
-
-
-
?
S-ethyl-L-Cys + H2O
ethanethiol + pyruvate + NH4+
-
-
-
?
S-ethyl-L-cysteine + H2O
?
-
-
-
-
?
S-ethyl-L-cysteine + H2O
?
-
-
-
-
?
S-ethyl-L-cysteine + H2O
ethanethiol + pyruvate + NH3
-
-
-
?
S-ethyl-L-cysteine + H2O
ethanethiol + pyruvate + NH3
-
-
-
?
S-ethyl-L-cysteine + H2O
ethanethiol + pyruvate + NH3
S-ethyl-L-cysteine represents a substrate with a better leaving group as compared to L-tryptophan
-
-
?
S-ethyl-L-cysteine + H2O
ethanethiol + pyruvate + NH4+
-
-
-
?
S-ethyl-L-cysteine + H2O
ethanethiol + pyruvate + NH4+
-
-
-
?
S-methyl-L-Cys + H2O
?
-
-
-
-
?
S-methyl-L-Cys + H2O
?
-
-
-
-
?
S-methyl-L-Cys + H2O
?
-
-
-
-
?
S-methyl-L-Cys + H2O
?
-
31.2% of the activity with L-Trp
-
-
?
S-methyl-L-Cys + H2O
?
-
-
-
-
?
S-methyl-L-Cys + H2O
?
-
63.8% of the activity with L-Trp
-
-
?
S-methyl-L-Cys + H2O
?
-
63.8% of the activity with L-Trp
-
-
?
S-methyl-L-Cys + H2O
methanethiol + pyruvate + NH4+
-
-
-
-
?
S-methyl-L-Cys + H2O
methanethiol + pyruvate + NH4+
-
-
-
?
S-methyl-L-Cys + indole
Trp + ?
-
-
-
-
?
S-methyl-L-Cys + indole
Trp + ?
-
-
-
?
S-methyl-L-Cys + indole
Trp + ?
-
-
-
?
S-methyl-L-Cys + indole
Trp + ?
-
-
-
-
?
S-methyl-L-Cys + indole
Trp + ?
-
-
-
?
S-methyl-L-cysteine + H2O
?
-
-
-
-
?
S-methyl-L-cysteine + H2O
?
-
-
-
-
?
S-methyl-L-cysteine + H2O
methanethiol + pyruvate + NH3
-
-
-
?
S-methyl-L-cysteine + H2O
methanethiol + pyruvate + NH3
-
-
-
r
S-methyl-L-cysteine + H2O
methanethiol + pyruvate + NH3
-
-
-
?
S-methyl-L-cysteine + H2O
methanethiol + pyruvate + NH3
-
-
-
?
S-methyl-L-cysteine + H2O
methanethiol + pyruvate + NH4+
-
-
-
?
S-methyl-L-cysteine + H2O
methanethiol + pyruvate + NH4+
-
-
-
?
S-o-nitrophenyl-L-Cys + H2O
o-nitrothiophenol + pyruvate + NH3
-
-
-
?
S-o-nitrophenyl-L-Cys + H2O
o-nitrothiophenol + pyruvate + NH3
-
-
-
-
?
S-o-nitrophenyl-L-Cys + H2O
o-nitrothiophenol + pyruvate + NH3
-
-
-
?
S-o-nitrophenyl-L-Cys + H2O
o-nitrothiophenol + pyruvate + NH3
-
-
-
-
?
S-o-nitrophenyl-L-Cys + H2O
o-nitrothiophenol + pyruvate + NH3
-
-
-
-
?
Ser + H2O
?
-
-
-
-
?
Ser + H2O
?
-
4.6% of the activity with L-Trp
-
-
?
Ser + H2O
?
-
L-Ser
-
-
?
Ser + H2O
?
-
5.3% of the activity with L-Trp
-
-
?
Ser + indole
Trp + ?
-
-
-
-
?
Ser + indole
Trp + ?
-
-
-
?
Ser + indole
Trp + ?
-
-
-
?
Ser + indole
Trp + ?
-
-
-
-
?
Ser + indole
Trp + ?
-
-
-
?
Ser + indole
Trp + H2O
-
-
-
-
?
Ser + indole
Trp + H2O
-
-
-
-
?
additional information
?
-
-
induced by Trp
-
-
?
additional information
?
-
-
tryptophanase displays no activity on D-tryptophan under usual conditions. However, it becomes active toward D-tryptophan degradation in highly concentrated diammonium hydrogen phosphate solutions
-
-
?
additional information
?
-
-
synthesis of L-tryptophan from L-cysteine, pyridoxal 5'-phosphate, and indole by the recombinant enzyme expressed in Escherichia coli strain BL21(DE3)
-
-
?
additional information
?
-
only the correctly protonated form of the enzyme binds the substrate, and the enzyme-substrate complex does not undergo protonation
-
-
?
additional information
?
-
-
tryptophanase does not degrade L-alanine, L-serine or L-cysteine
-
-
?
additional information
?
-
-
tryptophanase does not degrade L-alanine, L-serine or L-cysteine
-
-
?
additional information
?
-
the enzyme is capable to catalyze alpha,beta-elimination reactions with a number of other amino acids, containing better leaving groups compared to L-tryptophan, e.g. S-ethyl-L-cysteine. For the wild-type enzyme the reactions with substrates are described by the same kinetic scheme where binding of holoenzyme with an amino acid, leading to reversible formation of an external aldimine, proceeds very fast, while following transformations, leading finally to reversible formation of a quinonoid intermediate proceed with measureable rates
-
-
?
additional information
?
-
-
the enzyme is capable to catalyze alpha,beta-elimination reactions with a number of other amino acids, containing better leaving groups compared to L-tryptophan, e.g. S-ethyl-L-cysteine. For the wild-type enzyme the reactions with substrates are described by the same kinetic scheme where binding of holoenzyme with an amino acid, leading to reversible formation of an external aldimine, proceeds very fast, while following transformations, leading finally to reversible formation of a quinonoid intermediate proceed with measureable rates
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
inducible enzyme
-
-
?
additional information
?
-
coupled assay: the decrease in NADH absorbance at 340 nm in the presence of LDH is used to determine Trpase activity after adding the substrate. L-Phenylalanine and L-serine are no substrates
-
-
?
additional information
?
-
coupled assay: the decrease in NADH absorbance at 340 nm in the presence of LDH is used to determine Trpase activity after adding the substrate. L-Phenylalanine and L-serine are no substrates
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
the enzyme is induced by Trp and its analogs, and partially repressed by 0.5% glucose or glycerol
-
-
?
additional information
?
-
-
the enzyme is induced by Trp and its analogs, and partially repressed by 0.5% glucose or glycerol
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
analysis
the metabolic enzyme tryptophanase (TPase) is used for biosensor construction, TPase is biotinylated so that it can be coupled with a molecular recognition element, such as an antibody, to develop an ELISA-like assay. This method is used for the detection of an antibody present in nM concentrations by the human nose. TPase can also be combined with the enzyme pyridoxal kinase (PKase) for use in a coupled assay to detect adenosine 5'-triphosphate (ATP). When ATP is present in the low mM concentration range, the coupled enzymatic system generates an odor that is easily detectable by the human nose. Biotinylated TPase can be combined with various biotinlabeled molecular recognition elements, thereby enabling a broad range of applications for this odor-based reporting system
C298S
the mutant displays reduced activity, subsequent to incubation at 2°C, the mutant Trpase loses about 90% of its activity
C352A/Q353A/Q354A
site-directed mutagenesis, the mutation delays TnaA focus disassembly in stationary phase
D363A/K366A
site-directed mutagenesis, the mutation does neither affect the enzyme localization nor the enzyme activity
D404A
site-directed mutagenesis, the mutation does neither affect the enzyme localization nor the enzyme activity
D42A/S43A/E44A/D45A
site-directed mutagenesis, the mutation delays TnaA focus disassembly in stationary phase
D49A/T52A/D53A/S54A
site-directed mutagenesis, the mutation delays TnaA focus disassembly in stationary phase
E17A/K20A/R21A
site-directed mutagenesis, the mutation does neither affect the enzyme localization nor the enzyme activity
E346A/E347A
site-directed mutagenesis, the mutation does neither affect the enzyme localization nor the enzyme activity
E384A/K387A/R392A
site-directed mutagenesis, the mutation delays TnaA focus disassembly in stationary phase
E416A
site-directed mutagenesis, the mutation alters TnaA focus formation during exponential growth
E416A/R419A
site-directed mutagenesis, the mutation alters TnaA focus formation during exponential growth
E437A/K440A/H441A
site-directed mutagenesis, the mutation does neither affect the enzyme localization nor the enzyme activity
F464A
site-directed mutagenesis, the mutation results in a 500fold decrease in kcat/Km for L-tryptophan, with less effect on the reaction of other nonphysiological elimination substrates. The mutation has no effect on the formation of quinonoid intermediates
H370A/D374A/Q375A
site-directed mutagenesis, the mutation does neither affect the enzyme localization nor the enzyme activity
K115A
site-directed mutagenesis, the mutation does neither affect the enzyme localization nor the enzyme activity
K156A
site-directed mutagenesis, the mutation does neither affect the enzyme localization nor the enzyme activity
K239A
site-directed mutagenesis, the mutation does neither affect the enzyme localization nor the enzyme activity
K270A
site-directed mutagenesis, the mutation delays TnaA focus disassembly in stationary phase
K33A/S34A
site-directed mutagenesis, the mutation does neither affect the enzyme localization nor the enzyme activity
K406A/K409A/Q410A
site-directed mutagenesis, the mutation does neither affect the enzyme localization nor the enzyme activity
K443A/E444A/N445A/N448A
site-directed mutagenesis, the mutation does neither affect the enzyme localization nor the enzyme activity
K450A
site-directed mutagenesis, the mutation does neither affect the enzyme localization nor the enzyme activity
K459A
site-directed mutagenesis, the mutation does neither affect the enzyme localization nor the enzyme activity
K467A/K469A/E470A
site-directed mutagenesis, the mutation does neither affect the enzyme localization nor the enzyme activity
K5A
site-directed mutagenesis, the mutation does neither affect the enzyme localization nor the enzyme activity
K5A/K115A/K156A/K239A/K450A/K459A
site-directed mutagenesis, the mutation does neither affect the enzyme localization nor the enzyme activity
N327A/D329A
site-directed mutagenesis, the mutation does neither affect the enzyme localization nor the enzyme activity
Q339A/Y340A/D343A
site-directed mutagenesis, the mutation does neither affect the enzyme localization nor the enzyme activity
Q429A/T430A/H431A/D433A
site-directed mutagenesis, the mutation alters TnaA focus formation during exponential growth
R27A/E28A/E29A
site-directed mutagenesis, the mutation delays TnaA focus disassembly in stationary phase
R403A
site-directed mutagenesis, the mutation does neither affect the enzyme localization nor the enzyme activity
R462A
site-directed mutagenesis, the mutation alters TnaA focus formation during exponential growth
R462A/H463A/T465A
site-directed mutagenesis, the mutation alters TnaA focus formation during exponential growth
T23A/R24A/Y26A
site-directed mutagenesis, the mutation does neither affect the enzyme localization nor the enzyme activity
T426A/Y427A/T428A
site-directed mutagenesis, the mutation alters TnaA focus formation during exponential growth
T453A/T455A/Y456A/E457A
site-directed mutagenesis, the mutation delays TnaA focus disassembly in stationary phase
T465A
site-directed mutagenesis, the mutation does neither affect the enzyme localization nor the enzyme activity
Y74F
the mutant displays reduced activity, the Y74F mutant has low activity at 25°C and its residual activity is further reduced by cooling
H463F
-
site-directed mutagenesis, the mutant shows very low activity for elimination of indole but is still competent to form a quinonoid intermediate from L-tryptophan, it shows high activity with substrate beta-(benzimidazol-1-yl)-L-alanine
-
C298S
-
the mutant displays reduced activity, subsequent to incubation at 2°C, the mutant Trpase loses about 90% of its activity
-
W330F
-
the mutant displays reduced activity, subsequent to incubation at 2°C, the mutant Trpase loses about 90% of its activity
-
Y74F
-
the mutant displays reduced activity, the Y74F mutant has low activity at 25°C and its residual activity is further reduced by cooling
-
D133A
site-directed mutagenesis, inactive mutant
F448H
site-directed mutagenesis, the imidazole of F448H TPL forms a hydrogen bond to the substrate, consistent with the histidine being capable of hydrogen bonding to the substrate in TIL
H458A
site-directed mutagenesis, the almost inactive mutant shows 99% reduced activity compared to the wild-type enzyme
M383I
-
Tna2, slight increase of catalytic activity
S395G
-
Tna2, slight increase of catalytic activity
V382M
-
Tna2, slight reduction of catalytic activity
V382M/M383I/S395G
-
Tna2, 2fold increase in catalytic activity
D137A
site-directed mutagenesis, inactive mutant
H463A
site-directed mutagenesis, the mutant shows 96% reduced activity compared to the wild-type
K269A
site-directed mutagenesis, inactive mutant
K270A
site-directed mutagenesis, the mutation possibly eliminates this cofactor-protein interaction in the enzyme, inactive mutant
R103A
site-directed mutagenesis, the mutation alters orientation of the cofactor pyridoxal 5'-phosphate, inactive mutant
R230A
site-directed mutagenesis, inactive mutant
Y52A
site-directed mutagenesis, inactive mutant
Y74A
site-directed mutagenesis, inactive mutant
D137A
-
site-directed mutagenesis, inactive mutant
-
K270A
-
site-directed mutagenesis, the mutation possibly eliminates this cofactor-protein interaction in the enzyme, inactive mutant
-
R103A
-
site-directed mutagenesis, the mutation alters orientation of the cofactor pyridoxal 5'-phosphate, inactive mutant
-
Y52A
-
site-directed mutagenesis, inactive mutant
-
Y74A
-
site-directed mutagenesis, inactive mutant
-
E9A/R12A/R14A
site-directed mutagenesis, the mutation alters TnaA focus formation during exponential growth
E9A/R12A/R14A
site-directed mutagenesis, the mutation delays TnaA focus disassembly in stationary phase
H463F
-
the rate constant for quinonoid intermediate formation from L-Trp is about 10fold lower for H463F Trpase than for wild-type Trpase, but the rate constant for reaction of L-Met is similar for H463F Trpase and wild-type Trpase
H463F
-
site-directed mutagenesis, the mutant shows very low activity for elimination of indole but is still competent to form a quinonoid intermediate from L-tryptophan, it shows high activity with substrate beta-(benzimidazol-1-yl)-L-alanine
H463F
-
site-directed mutagenesis, the mutant shows very low activity for elimination of indole but is still competent to form a quinonoid intermediate from L-tryptophan, pH dependence of quinonoid intermediate formation, overview
H463F
site-directed mutagenesis, the mutation results in a 103fold decrease in tryptophan elimination activity and in a 1000fold decrease in tryptophan elimination activity and loss of the pKa of 6.0 in the pH dependence of kcat/Km, suggesting that His463 is that base. In contrast, kcat is pH-independent, demonstrating that only the correctly protonated form of the enzyme binds the substrate, and the enzyme-substrate complex does not undergo protonation
S398A
site-directed mutagenesis, the mutation alters TnaA focus formation during exponential growth
S398A
site-directed mutagenesis, the mutation delays TnaA focus disassembly in stationary phase
S398A/R403A/D404A
site-directed mutagenesis, the mutation alters TnaA focus formation during exponential growth
S398A/R403A/D404A
site-directed mutagenesis, the mutation delays TnaA focus disassembly in stationary phase
T60A/Q61A/S62A/Q64A
site-directed mutagenesis, the mutation alters TnaA focus formation during exponential growth
T60A/Q61A/S62A/Q64A
site-directed mutagenesis, the mutation delays TnaA focus disassembly in stationary phase
W330F
-
as in wild type, upon cooling to 2°C, inactivation and dissociation of tetramer to dimer occurs, spectrofluorometry data
W330F
the mutant displays reduced activity, subsequent to incubation at 2°C, the mutant Trpase loses about 90% of its activity
Y72F
-
mutation leads to a decrease in activity for L-tryptophan by 50000fold and to a considerable rearrangement of the active site. This rearrangement leads to an increase of room around the alpha -C atom of any bound amino acid, such that covalent binding of alpha -methyl-substituted amino acids becomes possible (which cannot be realized in wild-type Trpase)
Y72F
site-directed mutagenesis, the replacement leads to a drastic decrease in activity for L-tryptophan by 50000fold. On the other hand considerable activities are retained with respect to substrates bearing good leaving groups and to L-serine. Kinetics show a coexistence of induced fit and selected fit in the reaction mechanism of a mutant tryptophan indole lyase Y72F, analysis of interaction of the mutant tryptophan indole-lyase (TIL) from Proteus vulgaris Y72F with the transition state analogue, oxindolyl-L-alanine (OIA), with the natural substrate, L-tryptophan, and with a substrate S-ethyl-L-cysteine, overview. The change of Tyr 72 to Phe leads to a considerable increase in the enzyme affinity to OIA, and to a very strong decrease of kf and kr values
additional information
-
transposon insertion in tnaA gene is associated with a decrease in both A549 cells adherence and biofilm formation by Escherichia coli
additional information
-
construction of tnaA deletion and insertion mutant strains, overview
additional information
-
synthesis of L-tryptophan from L-cysteine, pyridoxal 5'-phosphate, and indole by the recombinant enzyme expressed in Escherichia coli strain BL21(DE3), co-reaction with Pseudomonas sp. TS1138 cells that convert DL-2-amino-delta2-thiazoline-4-carboxylic acid to L-cysteine
additional information
-
tnaA gene disruption of tryptophanase in Escherichia coli strain BL21(DE3) to prevent L-tryptophan and 5-hydroxy-L-tryptophan degradation for enhanced whole cell synthesis of 5-hydroxy-L-tryptophan using modified L-phenylalanine 4-hydroxylase, PAH-L101Y-W180F, from Chromobacterium violaceum in Escherichia coli, overview
additional information
construction of 42 TnaA variants: 6 truncated forms and 36 missense mutants in which different combinations of 83 surface-exposed residues are converted to alanine. A truncated TnaA protein containing only domains D1 and D3 (D1D3) localized to the pole. Mutations affecting the D1D3-to-D1D3 interface do not affect polar localization of D1D3 but do delay assembly of wild-type TnaA foci. In contrast, alterations to the D1D3-to-D2 domain interface produce diffuse localization of the D1D3 variant but do not affect the wild-type protein. Altering several surface-exposed residues decreases TnaA activity, implying that tetramer assembly may depend on interactions involving these sites. Changing any of three amino acids at the base of a loop near the catalytic pocket decreases TnaA activity and causes it to form elongated ovoid foci in vivo, indicating that the alterations affect focus formation and may regulate how frequently tryptophan reaches the active site. Mutant phenotypes, detailed overview
additional information
-
construction of 42 TnaA variants: 6 truncated forms and 36 missense mutants in which different combinations of 83 surface-exposed residues are converted to alanine. A truncated TnaA protein containing only domains D1 and D3 (D1D3) localized to the pole. Mutations affecting the D1D3-to-D1D3 interface do not affect polar localization of D1D3 but do delay assembly of wild-type TnaA foci. In contrast, alterations to the D1D3-to-D2 domain interface produce diffuse localization of the D1D3 variant but do not affect the wild-type protein. Altering several surface-exposed residues decreases TnaA activity, implying that tetramer assembly may depend on interactions involving these sites. Changing any of three amino acids at the base of a loop near the catalytic pocket decreases TnaA activity and causes it to form elongated ovoid foci in vivo, indicating that the alterations affect focus formation and may regulate how frequently tryptophan reaches the active site. Mutant phenotypes, detailed overview
additional information
-
construction of tnaA deletion and insertion mutant strains, overview
-
additional information
-
chimeric forms of Tna1/Tna2, thermal stability increases as the contnent of the N-terminal portion of Tna1 in the chimera increases
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Kiick, D.M.; Phillips, R.S.
Mechanistic deductions from multiple kinetic and solvent deuterium isotope effects and pH studies of pyridoxal phosphate dependent carbon-carbon lyases: Escherichia coli tryptophan indole-lyase
Biochemistry
27
7339-7344
1988
Escherichia coli
brenda
Behbahani-Nejad, I.; Dye, J.L.; Suelter, C.H.
Tryptophanase from Escherichia coli B/1t7-A
Methods Enzymol.
142
414-422
1987
Escherichia coli, Escherichia coli B/1t7-A
brenda
Honda, T.; Tokushige, M.
Effects of temperature and monovalent cations on activity and quaternary structure of tryptophanase
J. Biochem.
100
679-685
1986
Escherichia coli
brenda
Behbahani-Nejad, I.; Suelter, C.H.; Dye, J.L.
Kinetics of tryptophanase inactivation/activation by sudden removal/addition of potassium ions with the aid of a crown ether or cryptand
Curr. Top. Cell. Regul.
24
219-228
1984
Escherichia coli, Escherichia coli B/1t7-A
brenda
Whitt, D.D.; Klug, M.J.; DeMoss, R.D.
Trypotophanase from a marine bacterium, Vibrio K-7 synthesis, purification and some chemical catalytic properties
Arch. Microbiol.
122
169-175
1979
Vibrio sp., Vibrio sp. K-7
brenda
Suelter, C.H.; Snell, E.E.
Monovalent cation activation of tryptophanase
J. Biol. Chem.
252
1852-1857
1977
Escherichia coli, Escherichia coli B/1t7-A
brenda
Toraya, T.; Nihira, T.; Fukui, S.
Essential role of monovalent cations in the firm binding of pyridoxal 5'-phosphate to tryptophanase and beta-tyrosinase
Eur. J. Biochem.
69
411-419
1976
Escherichia coli, Escherichia coli B/1t7-A
-
brenda
Snell, E.E.
Tryptophanase: structure, catalytic activities, and mechanism of action
Adv. Enzymol. Relat. Areas Mol. Biol.
42
287-333
1975
Aeromonas hydrophila, Aeromonas sp., Paenibacillus alvei, Bacillus sp. (in: Bacteria), Bacteroides sp., Corynebacterium sp., Escherichia coli, Enterobacter sp., Erwinia sp., Kluyvera sp., Micrococcus sp., no activity in Acetobacter sp., no activity in Achromobacter sp., no activity in Agrobacterium sp., no activity in Alcaligenes sp., no activity in Azotobacter sp., no activity in Clostridium sp., no activity in Flavobacterium sp., no activity in Mycoplasma sp., no activity in Pseudomonas sp., no activity in Rhizobium sp., no activity in Salmonella sp., no activity in Serratia sp., no activity in Xanthomonas sp., Paracolobactrum sp., Pasteurella sp., Photobacterium sp., Providencia rettgeri, Proteus sp., Sphaerophorus sp., Vibrio sp.
brenda
Raibaud, O.; Goldberg, M.E.
The dissociated tryptophanase subunit is inactive
J. Biol. Chem.
251
2820-2824
1976
Escherichia coli
brenda
Simard, C.; Mardini, A.; Bordeleau, L.M.
Differentiation of tryptophanases of five species of Enterobacteriaceae by sulfhydryl groups
Can. J. Microbiol.
21
841-845
1975
Escherichia aurescens, Escherichia coli, Escherichia coli B / ATCC 11303, Morganella morganii, Proteus vulgaris, Shigella alkalescens
brenda
Simard, C.; Mardini, A.; Bordeleau, L.M.
The effect of pyridoxal phosphate on the tryptophanases of five species of Enterobacteriaceae
Can. J. Microbiol.
21
834-840
1975
Escherichia aurescens, Escherichia coli, Escherichia coli B / ATCC 11303, Morganella morganii, Proteus vulgaris, Shigella alkalescens
brenda
Simard, C.; Mardini, A.; Bordeleau, L.M.
Physical and chemical properties of tryptophenases of five species of Enterobacteriaceae
Can. J. Microbiol.
21
828-833
1975
Escherichia aurescens, Escherichia coli, Escherichia coli B / ATCC 11303, Morganella morganii, Proteus vulgaris, Shigella alkalescens
brenda
Yoshida, H.; Kumagai, H.; Yamada, H.; Matsubara, H.
The tryptophanase from Proteus rettgeri, improved purification and properties of crystalline holotryptophanase
Biochim. Biophys. Acta
391
494-503
1975
Providencia rettgeri
brenda
Cecchini, G.; Bojanowski, R.J.; DeMoss, R.D.
Tryptophanase from Sphaerophorus funduliformis. Purification, molecular weight and subunit properties
Biochim. Biophys. Acta
386
340-351
1975
Fusobacterium necrophorum subsp. funduliforme
brenda
Fukui, S.; Ikeda, S.; Fujimura, M.
Comparative studies on the properties of tryptophanase and tyrosine phenol-lyase immobilized directly on Sepharose or by use of Sepharose-bound pyridoxal 5 -phosphate
Eur. J. Biochem.
51
155-164
1975
Escherichia coli, Escherichia coli B/1t7-A
brenda
Yoshida, H.; Utagawa, T.; Kumagai, H.; Yamada, H.
Purification, crystallization and properties of tryptophanase from Proteus rettgeri
Agric. Biol. Chem.
38
2065-2072
1974
Providencia rettgeri
-
brenda
Yoshida, H.; Kumagai, H.; Yamada, H.
Cofactor requirement of tryptophanase from Proteus rettgeri
Agric. Biol. Chem.
38
2073-2079
1974
Providencia rettgeri
-
brenda
London, J.; Skrzynia, C.; Goldberg, M.E.
Renaturation of Escherichia coli tryptophanase after exposure to 8 M urea. Evidence for the existence of nucleation centers
Eur. J. Biochem.
47
409-415
1974
Escherichia coli
brenda
Yoshida, H.; Kumagai, H.; Yamada, H.
Catalytic properties of tryptophanase from Proteus rettgeri
Agric. Biol. Chem.
38
463-464
1974
Providencia rettgeri, Providencia rettgeri AJ2770
-
brenda
Cowell, J.L.; DeMoss, R.D.
Trytophanase from Aeromonas liquefaciens. Subunit structure and aggregation of the enzyme into enzymatically active polymeric species
J. Biol. Chem.
248
6262-6269
1973
Aeromonas hydrophila
brenda
Cowell, J.L.; Moser, K.; DeMoss, R.D.
Tryptophanase from Aeromonas liquefaciens. Purification, molecular weight and some chemical, catalytic and immunochemical properties
Biochim. Biophys. Acta
315
449-463
1973
Aeromonas hydrophila, Paenibacillus alvei, Escherichia coli, Micrococcus aerogenes, Paracolobactrum coliforme, Fusobacterium necrophorum subsp. funduliforme
-
brenda
Raibaud, O.; Goldberg, M.E.
The tryptophanase from Escherichia coli K-12. II. Comparison of the thermal stabilities of apo-, holo-, and hybrid enzymes
J. Biol. Chem.
248
3451-3455
1973
Escherichia coli
brenda
O'Neill Hoch, S.; DeMoss, R.D.
Catalytic studies on tryptophanase from Bacillus alvei
J. Bacteriol.
114
341-350
1973
Paenibacillus alvei
brenda
Watanabe, T.; Snell, E.E.
Reversibility of the tryptophanase reaction: synthesis of tryptophan from indole, pyruvate, and ammonia
Proc. Natl. Acad. Sci. USA
69
1086-1090
1972
Escherichia coli
brenda
London, J.; Goldberg, M.E.
The tryptophanase from Escherichia coli K-12. I. Purification, physical properties, and quaternary structure
J. Biol. Chem.
247
1566-1570
1972
Escherichia coli
brenda
Nihira, T.; Toraya, T.; Fukui, S.
Pyridoxal-5 -phosphate-sensitized photoinactivation of tryptophanase and evidence for essential histidyl residues in the active sites
Eur. J. Biochem.
101
341-347
1979
Escherichia coli, Escherichia coli B/1t7-A
brenda
Tani, S.; Tsujimoto, N.; Kawata, Y.; Tokushige, M.
Overproduction and crystallization of tryptophanase from recombinant cells of Escherichia coli
Biotechnol. Appl. Biochem.
12
28-33
1990
Escherichia coli, Escherichia coli B/1t7-A
brenda
Taylor, H.V.; Yudkin, M.D.
Synthesis of tryptophanase in Escherichia coli: isolation and characterization of a structural-gene mutant and two regulatory mutants
Mol. Gen. Genet.
165
95-102
1978
Escherichia coli
brenda
Kawasaki, K.; Yokota, A.; Tomita, F.
Enzymatic synthesis of L-tryptophan by Enterobacter aerogenes tryptophanase highly expressed in Escherichia coli, and some properties of the purified enzyme
Biosci. Biotechnol. Biochem.
59
1938-1943
1995
Klebsiella aerogenes, Escherichia coli, Klebsiella aerogenes SM-18
brenda
Suzuki, S.; Hirahara, T.; Horinouchi, S.; Beppu, T.
Purification and properties of thermostable tryptophanase from an obligately symbiotic thermophile, Symbiobacterium thermophilum
Agric. Biol. Chem.
55
3059-3066
1991
Symbiobacterium thermophilum, Symbiobacterium thermophilum T
brenda
Faleev, N.G.; Dementieva, I.S.; Zakomirdina, L.N.; Gogoleva, O.I.; Belikov, V.M.
Tryptophanase from Escherichia coli: catalytic and spectral properties in water-organic solvents
Biochem. Mol. Biol. Int.
34
209-216
1994
Escherichia coli
brenda
Isupov, M.N.; Antson, A.A.; Dodson, E.J.; Dodson, G.G.; Dementieva, I.S.; Zakomirdina, L.N.; Wilson, K.S.; Dauter, Z.; Lebedev, A.A.; Harutyunyan, E.M.
Crystal structure of tryptophanase
J. Mol. Biol.
276
603-623
1998
Proteus vulgaris
brenda
Kawasaki, K.; Yokota, A.; Oita, S.; Kobayashi, C.; Yoshikawa, S.; Kawamoto, S.i.; Takao, S.; Tomita, F.
Cloning and characterization of a tryptophanase gene from Enterobacter aerogenes SM-18 [published erratum appears in J Gen Microbiol 1994 Apr;140(Pt 4):999
J. Gen. Microbiol.
139
3275-3281
1993
Klebsiella aerogenes, Klebsiella aerogenes SM-18
brenda
Erez, T.; Gdalevsky, G.Y.; Hariharan, C.; Pines, D.; Pines, E.; Phillips, R.S.; Cohen-Luria, R.; Parola, A.H.
Cold-induced enzyme inactivation: how does cooling lead to pyridoxal phosphate-aldimine bond cleavage in tryptophanase?
Biochim. Biophys. Acta
1594
335-340
2002
Escherichia coli
brenda
Ikushiro, H.; Kagamiyama, H.
Activation of the coenzyme at the early step of the catalytic cycle of tryptophanase
Biofactors
11
97-99
2000
Escherichia coli
brenda
Di Martino, P.; Merieau, A.; Phillips, R.; Orange, N.; Hulen, C.
Isolation of an Escherichia coil strain mutant unable to form biofilm on polystyrene and to adhere to human pneumocyte cells: involvement of tryptophanase
Can. J. Microbiol.
48
132-137
2002
Escherichia coli
brenda
Gogoleva, O.I.; Zakomirdina, L.N.; Demidkina, T.V.; Phillips, R.S.; Faleev, N.G.
Tryptophanase in aqueous methanol: the solvent effects and a probable mechanism of the hydrophobic control of substrate specificity
Enzyme Microb. Technol.
32
843-850
2003
Escherichia coli
-
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
21592-21597
2002
Proteus vulgaris
brenda
Kudo, H.; Natsume, R.; Nishiyama, M.; Horinouchi, S.
Analysis of stability and catalytic properties of two tryptophanases from a thermophile
Protein Eng.
12
687-692
1999
Symbiobacterium thermophilum
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
Protein Sci.
13
913-924
2004
Proteus vulgaris
brenda
Kogan, A.; Gdalevsky, G.Y.; Cohen-Luria, R.; Parola, A.H.; Goldgur, Y.
Crystallization and preliminary X-ray analysis of the apo form of Escherichia coli tryptophanase
Acta Crystallogr. Sect. D
60
2073-2075
2004
Escherichia coli
brenda
Phillips, R.S.; Holtermann, G.
Differential effects of temperature and hydrostatic pressure on the formation of quinonoid intermediates from L-Trp and L-Met by H463F mutant Escherichia coli tryptophan indole-lyase
Biochemistry
44
14289-14297
2005
Escherichia coli
brenda
Kulikova, V.V.; Zakomirdina, L.N.; Dementieva, I.S.; Phillips, R.S.; Gollnick, P.D.; Demidkina, T.V.; Faleev, N.G.
Tryptophanase from Proteus vulgaris: The conformational rearrangement in the active site, induced by the mutation of tyrosine 72 to phenylalanine, and its mechanistic consequences
Biochim. Biophys. Acta
1764
750-757
2006
Proteus vulgaris
brenda
Grudniak, A.M.; Nowicka-Sans, B.; Maciag, M.; Wolska, K.I.
Influence of Escherichia coli DnaK and DnaJ molecular chaperones on tryptophanase (TnaA) amount and GreA, GreB stability
FEMS Microbiol. Rev.
49
507-512
2004
Escherichia coli
brenda
Mateus, D.M.; Alves, S.S.; Da Fonseca, M.M.
Kinetics of L-tryptophan production from indole and L-serine catalyzed by whole cells with tryptophanase activity
J. Biosci. Bioeng.
97
289-293
2004
Escherichia coli, Escherichia coli B1t-7A
brenda
Ku, S.Y.; Yip, P.; Howell, P.L.
Structure of Escherichia coli tryptophanase
Acta Crystallogr. Sect. D
62
814-823
2006
Escherichia coli (P0A853), Escherichia coli, Escherichia coli JM109 (P0A853)
brenda
Swiegers, J.H.; Capone, D.L.; Pardon, K.H.; Elsey, G.M.; Sefton, M.A.; Francis, I.L.; Pretorius, I.S.
Engineering volatile thiol release in Saccharomyces cerevisiae for improved wine aroma
Yeast
24
561-574
2007
Escherichia coli
brenda
Tsesin, N.; Kogan, A.; Gdalevsky, G.Y.; Himanen, J.P.; Cohen-Luria, R.; Parola, A.H.; Goldgur, Y.; Almog, O.
The structure of apo tryptophanase from Escherichia coli reveals a wide-open conformation
Acta Crystallogr. Sect. D
D63
969-974
2007
Escherichia coli
brenda
Almog, O.; Kogan, A.; de Leeuw, M.; Gdalevsky, G.Y.; Cohen-Luria, R.; Parola, A.H.
Structural insights into cold inactivation of tryptophanase and cold adaptation degrees of subtilisin S41: Minireview
Biopolymers
89
354-359
2008
Escherichia coli (P0A853)
brenda
Gubica, T.; Boroda, E.; Temeriusz, A.; Kanska, M.
Effects of native and permethylated cyclodextrins on the catalytic activity of L-tryptophan indole lyase
J. Inclusion Phenom. Macrocyclic Chem.
54
283-288
2006
Escherichia coli
-
brenda
Chattoraj, D.K.
Tryptophanase in sRNA control of the Escherichia coli cell cycle
Mol. Microbiol.
63
1-3
2007
Escherichia coli
brenda
Kim, Y.; Lee, D.; Kim, D.; Cho, J.; Yang, J.; Chung, M.; Kim, K.; Ha, N.
Inhibition of proliferation in colon cancer cell lines and harmful enzyme activity of colon bacteria by Bifidobacterium adolescentis SPM0212
Arch. Pharm. Res.
31
468-473
2008
Rattus norvegicus
brenda
Gubica, T.; Winnicka, E.; Temeriusz, A.; Kanska, M.
The influence of selected O-alkyl derivatives of cyclodextrins on the enzymatic decomposition of l-tryptophan by l-tryptophan indole-lyase
Carbohydr. Res.
344
304-130
2008
Escherichia coli
brenda
Yang, R.; Cruz-Vera, L.R.; Yanofsky, C.
23S rRNA nucleotides in the peptidyl transferase center are essential for tryptophanase operon induction
J. Bacteriol.
191
3445-3450
2009
Escherichia coli
brenda
hang, Y.; Hong, G.
Evidences of Hfq associates with tryptophanase and affects extracellular indole levels
Acta Biochim. Biophys. Sin.
41
709-717
2009
Escherichia coli
brenda
Kogan, A.; Gdalevsky, G.Y.; Cohen-Luria, R.; Goldgur, Y.; Phillips, R.S.; Parola, A.H.; Almog, O.
Conformational changes and loose packing promote E. coli tryptophanase cold lability
BMC Struct. Biol.
9
65
2009
Escherichia coli (P0A853), Escherichia coli, Escherichia coli SVS 370 (P0A853)
brenda
Wigginton, N.S.; Titta, A.; Piccapietra, F.; Dobias, J.; Nesatyy, V.J.; Suter, M.J.; Bernier-Latmani, R.
Binding of silver nanoparticles to bacterial proteins depends on surface modifications and inhibits enzymatic activity
Environ. Sci. Technol.
44
2163-2168
2010
Escherichia coli
brenda
Shimada, A.; Ozaki, H.; Saito, T.; Noriko, F.
Tryptophanase-catalyzed L-tryptophan synthesis from D-serine in the presence of diammonium hydrogen phosphate
Int. J. Mol. Sci.
10
2578-2590
2009
Escherichia coli
brenda
Chi, F.; Wang, Y.; Gallaher, T.K.; Wu, C.H.; Jong, A.; Huang, S.H.
Identification of IbeR as a stationary-phase regulator in meningitic Escherichia coli K1 that carries a loss-of-function mutation in rpoS
J. Biomed. Biotechnol.
2009
520283
2009
Escherichia coli, Escherichia coli K1
brenda
Scherzer, R.; Gdalevsky, G.; Goldgur, Y.; Cohen-Luria, R.; Bittner, S.; Parola, A.
New tryptophanase inhibitors: Towards prevention of bacterial biofilm formation
J. Enzyme Inhib. Med. Chem.
24
350-355
2009
Escherichia coli
brenda
Hirakawa, H.; Kodama, T.; Takumi-Kobayashi, A.; Honda, T.; Yamaguchi, A.
Secreted indole serves as a signal for expression of type III secretion system translocators in enterohaemorrhagic Escherichia coli O157:H7
Microbiology
155
541-550
2009
Escherichia coli, Escherichia coli O157:H7 Sakai
brenda
Yoshida, Y.; Sasaki, T.; Ito, S.; Tamura, H.; Kunimatsu, K.; Kato, H.
Identification and molecular characterization of tryptophanase encoded by tnaA in Porphyromonas gingivalis
Microbiology
155
968-978
2009
Porphyromonas gingivalis, Porphyromonas gingivalis W83
brenda
Kuczynska-Wisnik, D.; Matuszewska, E.; Laskowska, E.
Escherichia coli heat-shock proteins IbpA and IbpB affect biofilm formation by influencing the level of extracellular indole
Microbiology
156
148-157
2010
Escherichia coli
brenda
An, H.M.; Baek, E.H.; Jang, S.; Lee, d.o..K.; Kim, M.J.; Kim, J.R.; Lee, K.O.; Park, J.G.; Ha, N.J.
Efficacy of Lactic Acid Bacteria (LAB) supplement in management of constipation among nursing home residents
Nutr. J.
9
5-5
2010
Homo sapiens
brenda
Phillips, R.S.; Ghaffari, R.; Dinh, P.; Lima, S.; Bartlett, D.
Properties of tryptophan indole-lyase from a piezophilic bacterium, Photobacterium profundum SS9
Arch. Biochem. Biophys.
506
35-41
2011
Escherichia coli, Photobacterium profundum (Q6LP64), Photobacterium profundum, Photobacterium profundum SS9 (Q6LP64), Photobacterium profundum SS9
brenda
Sasaki-Imamura, T.; Yoshida, Y.; Suwabe, K.; Yoshimura, F.; Kato, H.
Molecular basis of indole production catalyzed by tryptophanase in the genus Prevotella
FEMS Microbiol. Lett.
322
51-59
2011
Prevotella intermedia (E9RK37), Prevotella intermedia, Prevotella intermedia ATCC 25611 (E9RK37)
brenda
Bhatt, S.; Anyanful, A.; Kalman, D.
CsrA and TnaB coregulate tryptophanase activity to promote exotoxin-induced killing of Caenorhabditis elegans by enteropathogenic Escherichia coli
J. Bacteriol.
193
4516-4522
2011
Escherichia coli
brenda
Shimada, A.; Ozaki, H.; Saito, T.; Fujii, N.
Reaction pathway of tryptophanase-catalyzed L-tryptophan synthesis from D-serine
J. Chromatogr. B
879
3289-3295
2011
Escherichia coli
brenda
Hara, R.; Kino, K.
Enhanced synthesis of 5-hydroxy-L-tryptophan through tetrahydropterin regeneration
AMB Express
3
70
2013
Escherichia coli
brenda
Phillips, R.S.; Kalu, U.; Hay, S.
Evidence of preorganization in quinonoid intermediate formation from L-Trp in H463F mutant Escherichia coli tryptophan indole-lyase from effects of pressure and pH
Biochemistry
51
6527-6533
2012
Escherichia coli
brenda
Harris, A.P.; Phillips, R.S.
Benzimidazole analogs of (L)-tryptophan are substrates and inhibitors of tryptophan indole lyase from Escherichia coli
FEBS J.
280
1807-1817
2013
Escherichia coli, Escherichia coli JM109
brenda
Li, G.; Young, K.D.
Indole production by the tryptophanase TnaA in Escherichia coli is determined by the amount of exogenous tryptophan
Microbiology
159
402-410
2013
Escherichia coli, Escherichia coli MG1655
brenda
Du, J.; Duan, J.J.; Zhang, Q.; Hou, J.; Bai, F.; Chen, N.; Bai, G.
Enzymatic synthesis of L-tryptophan from D,L-2-amino-delta2-thiazoline-4-carboxylic acid and indole by Pseudomonas sp. TS1138 L-2-amino-delta2-thiazoline-4-carboxylic acid hydrolase, S-carbamyl-L-cysteine amidohydrolase, and Escherichia coli L-tryptophanase
Prikl. Biokhim. Mikrobiol.
48
183-190
2012
Escherichia coli
brenda
Phillips, R.S.; Buisman, A.A.; Choi, S.; Hussaini, A.; Wood, Z.A.
The crystal structure of Proteus vulgaris tryptophan indole-lyase complexed with oxindolyl-L-alanine implications for the reaction mechanism
Acta Crystallogr. Sect. D
74
748-759
2018
Escherichia coli (P0A853), Escherichia coli, Proteus vulgaris (P28796), Proteus vulgaris
brenda
Rety, S.; Deschamps, P.; Leulliot, N.
Structure of Escherichia coli tryptophanase purified from an alkaline-stressed bacterial culture
Acta Crystallogr. Sect. F
71
1378-1383
2015
Escherichia coli (P0A853), Escherichia coli
brenda
Kogan, A.; Raznov, L.; Gdalevsky, G.; Cohen-Luria, R.; Almog, O.; Parola, A.; Goldgur, Y.
Structures of Escherichia coli tryptophanase in holo and semi-holo forms
Acta Crystallogr. Sect. F
71
286-290
2015
Escherichia coli (P0A853), Escherichia coli
brenda
Xu, Y.; Zhang, Z.; Ali, M.M.; Sauder, J.; Deng, X.; Giang, K.; Aguirre, S.D.; Pelton, R.; Li, Y.; Filipe, C.D.
Turning tryptophanase into odor-generating biosensors
Angew. Chem. Int. Ed. Engl.
53
2620-2622
2014
Escherichia coli (P0A853)
brenda
Nuidate, T.; Tansila, N.; Chomchuen, P.; Phattaranit, P.; Eangchuan, S.; Vuddhakul, V.
Characterization of tryptophanase from Vibrio cholerae
Appl. Biochem. Biotechnol.
175
243-252
2015
Vibrio cholerae O1 (A5EYI0), Vibrio cholerae O1 ATCC 39541 (A5EYI0)
brenda
Watsuji, T.O.; Takano, H.; Yamabe, T.; Tamazawa, S.; Ikemura, H.; Ohishi, T.; Matsuda, T.; Shiratori-Takano, H.; Beppu, T.; Ueda, K.
Analysis of the tryptophanase expression in Symbiobacterium thermophilum in a coculture with Geobacillus stearothermophilus
Appl. Microbiol. Biotechnol.
98
10177-10186
2014
Symbiobacterium thermophilum (P31015), Symbiobacterium thermophilum, Symbiobacterium thermophilum T / IAM 14863 / JCM 14929 (P31015)
brenda
Do, Q.T.; Nguyen, G.T.; Celis, V.; Phillips, R.S.
Inhibition of Escherichia coli tryptophan indole-lyase by tryptophan homologues
Arch. Biochem. Biophys.
560
20-26
2014
Escherichia coli (P0A853), Escherichia coli
brenda
Faleev, N.G.; Zakomirdina, L.N.; Vorobev, M.M.; Tsvetikova, M.A.; Gogoleva, O.I.; Demidkina, T.V.; Phillips, R.S.
A straightforward kinetic evidence for coexistence of induced fit and selected fit in the reaction mechanism of a mutant tryptophan indole lyase Y72F from Proteus vulgaris
Biochim. Biophys. Acta
1844
1860-1867
2014
Proteus vulgaris (P28796), Proteus vulgaris
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
Escherichia coli (P0A853), Proteus vulgaris (P28796)
brenda
Li, G.; Young, K.D.
A new suite of tnaA mutants suggests that Escherichia coli tryptophanase is regulated by intracellular sequestration and by occlusion of its active site
BMC Microbiol.
15
14
2015
Escherichia coli (P0A853), Escherichia coli
brenda