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L-tryptophan + H2O = indole + pyruvate + NH3
L-tryptophan + H2O = indole + pyruvate + NH3

-
-
-
-
L-tryptophan + H2O = indole + pyruvate + NH3
mechanism
-
L-tryptophan + H2O = indole + pyruvate + NH3
mechanism
-
L-tryptophan + H2O = indole + pyruvate + NH3
in the reverse direction NH4+ interacts with bound pyridoxal 5'-phosphate to form an imine. Pyruvate is the second substrate, indole the third. alpha-Aminoacrylate functions as a common enzyme-bound intermediate in both synthetic and degradative reactions
-
L-tryptophan + H2O = indole + pyruvate + NH3
mechanism that requires two catalytic bases
-
L-tryptophan + H2O = indole + pyruvate + NH3
mechanism, solvent effects
-
L-tryptophan + H2O = indole + pyruvate + NH3
reaction mechanism, overview
-
L-tryptophan + H2O = indole + pyruvate + NH3
quinonoid intermediate formation involving Tyr71 and Cys298, mechanism, active site preorganization, overview
-
L-tryptophan + H2O = indole + pyruvate + NH3
an active site base is essential for activity, and alpha-deuterated substrate exhibits modest primary isotope effects on kcat and kcat/Km, suggesting that substrate deprotonation is partially rate-limiting. Pre-steady state kinetics with enzyme TIL show rapid formation of an external aldimine intermediate, followed by deprotonation to give a quinonoid intermediate absorbing at about 500 nm. The mechanism of TIL requires both substrate strain and acid/base catalysis, and substrate strain is probably responsible for the very high substrate specificity of TIL. Acid-base catalysis mechanism of TIL, overview. The indole ring is preorganized into the active conformation before alpha-deprotonation occurs
L-tryptophan + H2O = indole + pyruvate + NH3
an active site base is essential for activity, and alpha-deuterated substrate exhibits modest primary isotope effects on kcat and kcat/Km, suggesting that substrate deprotonation is partially rate-limiting. Pre-steady state kinetics with enzyme TIL show rapid formation of external an aldimine intermediate, followed by deprotonation to give a quinonoid intermediate absorbing at about 500 nm. The mechanism of TIL requires both substrate strain and acid/base catalysis, and substrate strain is probably responsible for the very high substrate specificity of TIL. Acid-base catalysis mechanism of TIL, overview. The indole ring is preorganized into the active conformation before alpha-deprotonation occurs
L-tryptophan + H2O = indole + pyruvate + NH3
catalyses the reaction in which L-tryptophan is degraded to indole, pyruvate and ammonia via alpha,beta-elimination and beta-replacement mechanisms
L-tryptophan + H2O = indole + pyruvate + NH3
proposed mechanism of tryptophan indole-lyase, overview
L-tryptophan + H2O = indole + pyruvate + NH3
reaction via formation of quinonoid intermediate
L-tryptophan + H2O = indole + pyruvate + NH3
reaction mechanism, overview
-
-
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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
2-nitrobenzenethiolate + pyruvate + NH4+
-
-
-
-
ir
S-(2-nitrophenyl)-L-cysteine + H2O
2-nitrophenol + pyruvate + NH4+
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-nitrophenol + pyruvate + NH4+
S-o-nitrophenyl-L-Cys + H2O
o-nitrothiophenol + pyruvate + NH4+
-
-
-
-
?
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
-
-
-
?
S-(2-nitrophenyl)-L-cysteine + H2O

2-nitrophenol + pyruvate + NH4+
-
-
-
-
?
S-(2-nitrophenyl)-L-cysteine + H2O
2-nitrophenol + pyruvate + NH4+
-
-
-
?
S-(2-nitrophenyl)-L-cysteine + H2O
2-nitrophenol + pyruvate + NH4+
-
-
-
?
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-nitrophenol + pyruvate + NH4+
-
-
-
?
S-o-nitrophenyl-L-Cys + H2O
o-nitrophenol + pyruvate + NH4+
-
-
-
-
?
S-o-nitrophenyl-L-Cys + H2O
o-nitrophenol + pyruvate + NH4+
-
-
-
?
S-o-nitrophenyl-L-Cys + H2O
o-nitrophenol + pyruvate + NH4+
-
-
-
-
?
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
-
-
?
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pyridoxal 5'-phosphate

-
-
677276, 681216, 681998, 691648, 701449, 703486, 704093, 704722, 704847, 705578, 705580, 713955, 715733, 726995, 728262, 728650
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
Shigella alkalescens
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
required
pyridoxal 5'-phosphate
-
contains 4 mol of pyridoxal 5'-phosphate per mol of enzyme
pyridoxal 5'-phosphate
-
contains 4 mol of pyridoxal 5'-phosphate per mol of enzyme
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
-
some coenzyme analogues can replace pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
enzyme contains 4 mol of pyridoxal 5'-phosphate per mol of enzyme at pH 6.8 and 3 mol of pyridoxal 5'-phosphate per mol of enzyme at pH 7.8 in K+ buffer
pyridoxal 5'-phosphate
-
enzyme contains 4 mol of pyridoxal 5'-phosphate per mol of enzyme at pH 6.8 and 3 mol of pyridoxal 5'-phosphate per mol of enzyme at pH 7.8 in K+ buffer
pyridoxal 5'-phosphate
-
enzyme contain 4 mol of pyridoxal 5'-phosphate per mol of enzyme, independently of the pH in presence of K+
pyridoxal 5'-phosphate
Escherichia aurescens
-
enzyme contain 4 mol of pyridoxal 5'-phosphate per mol of enzyme, independently of the pH in presence of K+
pyridoxal 5'-phosphate
-
conversion of apoenzyme into the active holoenzyme is attained at 30ưC in Tris-HCl buffer, pH 8.0, containing pyridoxal 5'-phosphate and K+, no conversion occurs at 5ưC
pyridoxal 5'-phosphate
-
one enzyme molecule contains 4 pyridoxal 5'-phosphate combining sites
pyridoxal 5'-phosphate
-
one enzyme molecule contains 4 pyridoxal 5'-phosphate combining sites
pyridoxal 5'-phosphate
-
one enzyme molecule contains 4 pyridoxal 5'-phosphate combining sites
pyridoxal 5'-phosphate
-
one enzyme molecule contains 4 pyridoxal 5'-phosphate combining sites
pyridoxal 5'-phosphate
-
enzyme contains 2 pyridoxal 5'-phosphate per subunit
pyridoxal 5'-phosphate
-
binds 1 mol of pyridoxal 5'-phosphate per subunit
pyridoxal 5'-phosphate
-
Km: 0.00209 mM
pyridoxal 5'-phosphate
covalent binding required to activate the enzyme
pyridoxal 5'-phosphate
-
one molecule bound per monomer
pyridoxal 5'-phosphate
dependent on, monovalent cations (K+ or NH4+) are required for the binding of pyridoxal 5'-phosphate to a lysine residue in the active site, leading to the functionally active form. Each monomer binds one molecule of pyridoxal 5'-phosphate, which forms an aldimine bond to the Lys270 residue in the active site
pyridoxal 5'-phosphate
dependent on, residue Arg103 plays an important role in orientation of the cofactor pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
dependent on, the active site residues involved in cofactor binding are highly conserved for enzyme TIL
pyridoxal 5'-phosphate
dependent on, the active site residues involved in cofactor binding are highly conserved for enzyme TIL
pyridoxal 5'-phosphate
dependent on, the activity of TPase can be modulated by the concentration of pyridoxal 5'-phosphate
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Cl-
-
bound to enzyme, possibly required for stabilization of subunit interactions
NaCl
-
maximal activity for the enzyme in whole cells: 0.4-0.5 M
sulfate
two ions bound two the active site of the enzyme, one of the sulfate ions interacts with both the transferase and PLP-binding domains and appears to be responsible for holding the enzyme in its closed conformation
K+

-
K+ or NH4+ required
K+
-
kinetics of tryptophanase inactivation/activation by sudden removal/addition of K+ with the aid of a crown ether or cryptand
K+
-
monovalent cation activator required
K+
-
promotes the conversion of the inactive holoenzyme into the active holoenzyme rather than being involved in the conversion of the apoenzyme and pyridoxal 5'-phosphate into the active holoenzyme
K+
-
monovalent cation required for activity
K+
monovalent cation required for activity and for tight cofactor binding
K+
stabilizing, cold inactivation occurs more slowly in the presence of K+
NH4+

-
K+ or NH4+ required
NH4+
-
monovalent cation activator required
NH4+
-
promotes the conversion of the inactive holoenzyme into the active holoenzyme rather than being involved in the conversion of the apoenzyme and pyridoxal 5'-phosphate into the active holoenzyme
NH4+
-
monovalent cation required for activity
NH4+
monovalent cation required for activity and for tight cofactor binding
NH4+
-
K+ or NH4+ required
NH4+
-
K+ or NH4+ required
Rb+

-
activates
Rb+
-
monovalent cation activator required
Tl+

-
activates
Tl+
-
monovalent cation required for activity
Tl+
monovalent cation required for activity and for tight cofactor binding
additional information

monovalent cations (K+ or NH4 + ) are required for the binding of PLP to a lysine residue in the active site, leading to the functionally active form
additional information
-
monovalent cations (K+ or NH4 + ) are required for the binding of PLP to a lysine residue in the active site, leading to the functionally active form
additional information
the enzyme requires a monovalent cation, either K+, NH4+, Rb+ or Cs+ for activity, with Na+ and Li+ giving little or no activity
additional information
-
TnaA is not affected by K+ or Na+
additional information
the enzyme requires a monovalent cation, either K+, NH4+, Rb+ or Cs+ for activity, with Na+ and Li+ giving little or no activity
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(2,3-di-O-methyl)-alpha-cyclodextrin
-
-
(2,3-di-O-methyl)-beta-cyclodextrin
-
-
(2-hydroxypropyl)-alpha-cyclodextrin
-
-
(2-hydroxypropyl)-beta-cyclodextrin
-
-
(S)-4-(benzimidazol-1-yl)-2-aminobutanoic acid
-
2,3-dihydro-L-tryptophan
-
2-amino-4-(benzimidazol-1-yl)butyric acid
-
i.e. homo-BZI-Ala, a potent competitive inhibitor
2-amino-5-(benzimidazol-1-yl)pentanoic acid
-
i.e. bishomo-BZI-Ala, weak inhibition
4-phenyl-2-aminobutyrate
-
-
alpha-amino-9,10-dihydro-9,10-dioxo-2-anthracenepropanoic acid
-
noncompetitive inhibition
anthranilic acid
-
competitive
beta-(benzimidazol-1-yl)-L-alanine
-
competitive, is also a good substrate for the wild-type and mutant enzymes
Bifidobacterium adolescentis SPM0212
-
inhibits the proliferation of human colon cancer cell lines and it inhibits harmful fecal enzymes of rat intestinal microflora, including alpha-glucuronidase, alpha-glucosidase, tryptophanase, and urease
-
cyclodextrin
-
mixed type inhibition, competitive and non-competitive with inhibitor constants for different cyclodextrins between 0.5 and 10 mM
-
D,L-homophenylalanine
-
-
diammonium hydrogen phosphate
-
diammonium hydrogen phosphate serves as an inhibitor of tryptophanase when L-serine is substrate, the activity decreases with increasing diammonium hydrogen phosphate
guanidine hydrochloride
-
-
L-bishomotryptophan
potent inhibitor, formation of an external aldimine. The compound is a selective inhibitor and is a potential lead for the development of antibacterials
L-homotryptophan
a moderate competitive inhibitor, formation of an external aldimine and quinonoid
L-tryptophan ethylester
-
competitive inhibition
N-acetyl-L-tryptophan
-
noncompetitive inhibition
N-[3,6-dioxo-4-(phenylsulfanyl)cyclohexa-1,4-dien-1-yl]-L-tryptophanamide
-
uncompetitive inhibition
profilin 1
-
substrate analog
-
[2,3,6-tri-O-(2'-methoxyethyl)]-alpha-cyclodextrin
-
-
[2,3-di-O-(2'-methoxyethyl)]-alpha-cyclodextrin
-
-
[2,3-di-O-(2'-methoxyethyl)]-beta-cyclodextrin
-
-
[2,3-di-O-methyl-6-O-(2'-methoxyethyl)]-alpha-cyclodextrin
-
-
[2,3-di-O-methyl-6-O-(2'-methoxyethyl)]-beta-cyclodextrin
-
-
Ala

-
competitive
Ethionine

-
competitive with S-o-nitrophenyl-L-Cys
L-Trp

-
competitive with S-o-nitrophenyl-L-Cys
L-tryptophan

-
-
L-tryptophan
weak substrate inhibition
oxindolyl-L-Ala

-
competitive
oxindolyl-L-alanine

-
-
oxindolyl-L-alanine
OIA, a potent competitive inhibitor of the enzyme, transition-state analogue
oxindolyl-L-alanine
an inhibitor which is an analogue of the proposed indolenine intermediate. The pH dependence of Ki for oxindolyl-L-alanine exhibits two basic pKas of 6.0 and 7.6
oxindolyl-L-alanine
OIA, a potent competitive inhibitor of the enzyme, transition-state analogue. The small enzyme domain rotates about 10ư to close the active site, bringing His458 into position to donate a hydrogen bond to Asp133, which also accepts a hydrogen bond from the heterocyclic NH of the inhibitor. This brings Phe37 and Phe459 into van der Waals contact with the aromatic ring of OIA. Four subunits of the tetramer of the OIA complex, the complex is clearly in the quinonoid form, modeled L-tryptophan-PLP quinonoid complex with OIP, structure overview
oxindolyl-L-alanine
OIA, a transition state analogue, serves as substrate and inhibitor for enzyme mutant Y72F and wild-type enzyme
oxindolyl-L-alanine
an inhibitor which is an analogue of the proposed indolenine intermediate
Phe

-
-
additional information

-
inhibitors in aqueous methanol
-
additional information
-
cyclodextrin derivatives cause the inhibition of enzymatic process, both competitive and non-competitive. The competitive inhibition is connected with the formation of inclusion complexes between cyclodextrins and L-tryptophan, related to the geometry of these complexes. The mechanism of the non-competitive inhibition is not so evident
-
additional information
-
when bound to silver nanoparticles, TNase activity decreases significantly by 50% for carbonate coated silver nanoparticles and by over 90% for bare silver nanoparticles
-
additional information
design, synthesis, and evaluation of homotryptophan analogues as possible mechanism-based inhibitors for Escherichia coli tryptophan indole-lyase, overview. As a quinonoid structure is an intermediate in the reaction mechanism of TIL, homologation of the physiological substrate, L-Trp, might provide analogues resembling the transition state for beta-elimination, and potentially inhibit the enzyme. Kinetics show that formation of a quinonoid complex is not required for strong inhibition
-
additional information
-
design, synthesis, and evaluation of homotryptophan analogues as possible mechanism-based inhibitors for Escherichia coli tryptophan indole-lyase, overview. As a quinonoid structure is an intermediate in the reaction mechanism of TIL, homologation of the physiological substrate, L-Trp, might provide analogues resembling the transition state for beta-elimination, and potentially inhibit the enzyme. Kinetics show that formation of a quinonoid complex is not required for strong inhibition
-
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Aberrant Crypt Foci
Effects of Shikunshito-Kamiho on fecal enzymes and formation of aberrant crypt foci induced by 1,2-dimethylhydrazine.
Brain Neoplasms
Intrathecal 5-fluoro-2'-deoxyuridine (FdUrd) for the treatment of solid tumor neoplastic meningitis: an in vivo study.
Brain Neoplasms
[In vitro study on intrathecal application of 5-fluoro-2'-deoxyuridine (FdUrd) for meningeal dissemination of malignant tumor]
Brain Neoplasms
[In vivo study on intrathecal use of 5-fluoro-2'-deoxyuridine (FdUrd) in meningeal dissemination of malignant tumor]
Carcinogenesis
Effects of Shikunshito-Kamiho on fecal enzymes and formation of aberrant crypt foci induced by 1,2-dimethylhydrazine.
Colonic Neoplasms
Tryptophanase of fecal flora as a possible factor in the etiology of colon cancer.
Decompression Sickness
IS911 transpososome assembly as analysed by tethered particle motion.
Glioma
[In vivo study on intrathecal use of 5-fluoro-2'-deoxyuridine (FdUrd) in meningeal dissemination of malignant tumor]
Infections
Disruption of targeted gene in bacterial chromosome by using a temperature-sensitive plasmid.
Infections
Modulation of gene expression in Escherichia coli infected with single-stranded bacteriophage phi X174.
Insulin Resistance
miR-375 prevents high-fat diet-induced insulin resistance and obesity by targeting the aryl hydrocarbon receptor and bacterial tryptophanase (tnaA) gene.
Meningeal Carcinomatosis
Intrathecal 5-fluoro-2'-deoxyuridine (FdUrd) for the treatment of solid tumor neoplastic meningitis: an in vivo study.
Meningeal Carcinomatosis
[In vitro study on intrathecal application of 5-fluoro-2'-deoxyuridine (FdUrd) for meningeal dissemination of malignant tumor]
Neoplasm Metastasis
5'-O-tritylated nucleoside derivatives: inhibition of thymidine phosphorylase and angiogenesis.
Neoplasm Metastasis
Thymidine phosphorylase inhibitors: recent developments and potential therapeutic applications.
Neoplasms
5'-O-tritylated nucleoside derivatives: inhibition of thymidine phosphorylase and angiogenesis.
Neoplasms
Expression and localization of thymidine phosphorylase/platelet-derived endothelial cell growth factor in skin and cutaneous tumors.
Neoplasms
Expression of thymidine phosphorylase in human superficial bladder cancer.
Neoplasms
Increased virulence of the oral microbiome in oral squamous cell carcinoma revealed by metatranscriptome analyses.
Neoplasms
Intrathecal 5-fluoro-2'-deoxyuridine (FdUrd) for the treatment of solid tumor neoplastic meningitis: an in vivo study.
Neoplasms
Physicochemical and nutraceutical properties of moringa (Moringa oleifera) leaves and their effects in an in vivo AOM/DSS-induced colorectal carcinogenesis model.
Neoplasms
Structure and activity of specific inhibitors of thymidine phosphorylase to potentiate the function of antitumor 2'-deoxyribonucleosides.
Neoplasms
The nucleoside derivative 5'-O-trityl-inosine (KIN59) suppresses thymidine phosphorylase-triggered angiogenesis via a noncompetitive mechanism of action.
Neoplasms
Thymidine phosphorylase as a target for imaging and therapy with thymine analogs.
Neoplasms
Thymidine phosphorylase inhibitors: recent developments and potential therapeutic applications.
Neoplasms
[In vivo study on intrathecal use of 5-fluoro-2'-deoxyuridine (FdUrd) in meningeal dissemination of malignant tumor]
Obesity
miR-375 prevents high-fat diet-induced insulin resistance and obesity by targeting the aryl hydrocarbon receptor and bacterial tryptophanase (tnaA) gene.
Paralysis
CsrA and TnaB Coregulate Tryptophanase Activity To Promote Exotoxin-Induced Killing of Caenorhabditis elegansby Enteropathogenic Escherichia coli.
Paralysis
Paralysis and killing of Caenorhabditis elegans by enteropathogenic Escherichia coli requires the bacterial tryptophanase gene.
Shock, Septic
[Prevalence of Staphylococcus aureus isolated from subclinical bovine mastitis in dairies of the city of San Luis]
Starvation
Synthesis of inducible enzyme in Escherichia coli recovering from prolonged energy starvation.
tryptophanase deficiency
New approach to tryptophan production by Escherichia coli: genetic manipulation of composite plasmids in vitro.
Urinary Bladder Neoplasms
Expression of thymidine phosphorylase in human superficial bladder cancer.
Vaginosis, Bacterial
Influence of the tryptophan-indole-IFN? axis on human genital Chlamydia trachomatis infection: role of vaginal co-infections.
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2.7
5-hydroxy-L-Trp
-
alpha,beta-elimination
1.8
5-methyl-L-Trp
-
alpha,beta-elimination
0.6
alpha,beta-diaminopropionic acid
-
strain B/1t7-A
0.0236 - 0.315
beta-(benzimidazol-1-yl)-L-alanine
1.2 - 6.15
beta-chloroalanine
110
cysteine sulfinic acid
-
strain B/1t7-A
0.15 - 5.252
L-tryptophan
0.11
O-benzylserine
-
strain B/1t7-A
4
O-methylserine
-
strain B/1t7-A
0.18
S-(o-nitrophenyl)-L-cysteine
-
pH 8.0, 25ưC
0.346
S-Benzyl-L-cysteine
recombinant His-tagged wild-type enzyme, pH 7.8, 37ưC
0.065 - 0.15
S-benzylcysteine
0.26 - 3.3
S-ethyl-L-cysteine
1
S-ethylcysteine
-
strain B/1t7-A, 25ưC
0.18 - 15.2
S-methyl-L-Cys
0.49 - 16
S-methyl-L-cysteine
10
S-methylcysteine
-
strain B/1t7-A, 37ưC
0.06 - 0.18
S-o-nitrophenyl-L-Cys
additional information
additional information
-
0.0236
beta-(benzimidazol-1-yl)-L-alanine

-
mutant H463F, pH 8.0, 25ưC
0.315
beta-(benzimidazol-1-yl)-L-alanine
-
wild-type enzyme, pH 8.0, 25ưC
1.2
beta-chloroalanine

-
-
1.2
beta-chloroalanine
-
strain B/1t7-A
6.15
beta-chloroalanine
-
pH 7.8, 37ưC, mutant enzyme Y72F
0.019
indole

-
-
4
indole
-
beta-replacement reaction
4.1
indole
-
reverse of alpha,beta-elimination
1
L-Cys

-
alpha,beta-elimination
2.8
L-Cys
-
beta-replacement reaction
4.64
L-Ser

-
pH 7.8, 37ưC, mutant enzyme Y72F
160
L-Ser
-
strain B/1t7-A, 37ưC
0.00181
L-Trp

-
-
0.09
L-Trp
-
purified recombinant tryptophanase in 200 mM sodium phosphate buffer (pH 7.5), at 37ưC
0.12
L-Trp
-
pH 7.8, 37ưC, mutant enzyme Y72F
0.1732
L-Trp
-
in the presence of Hfq protein, in 0.1 M potassium phosphate buffer (pH 7.8), at 37ưC
0.1901
L-Trp
-
in the absence of Hfq protein, in 0.1 M potassium phosphate buffer (pH 7.8), at 37ưC
0.2
L-Trp
-
purified recombinant tryptophanase in 200 mM potassium phosphate buffer (pH 7.5), at 37ưC
0.3
L-Trp
-
strain B/1t7-A, 25ưC
0.33
L-Trp
-
strain B/1t7-A, 37ưC
0.34
L-Trp
-
immobilized enzyme
0.347
L-Trp
-
pH 8, 18ưC
0.46
L-Trp
-
renatured enzyme
0.6
L-Trp
-
native enzyme
0.15
L-tryptophan

-
wild-type enzyme, pH 8.0, 25ưC
0.23
L-tryptophan
pH 7.5, 37ưC
5.252
L-tryptophan
recombinant His-tagged wild-type enzyme, pH 7.8, 37ưC
10
pyruvate

-
cosubstrate indole, alpha,beta-addition
0.065
S-benzylcysteine

-
strain B/1t7-A, 25ưC
0.067
S-benzylcysteine
-
-
0.15
S-benzylcysteine
-
pH 7.8, 37ưC, mutant enzyme Y72F
0.26
S-ethyl-L-cysteine

-
purified recombinant tryptophanase in 200 mM potassium phosphate buffer (pH 7.5), at 37ưC
0.81
S-ethyl-L-cysteine
-
pH 7.8, 37ưC, mutant enzyme Y72F
3.3
S-ethyl-L-cysteine
pH 7.6, 37ưC
0.18
S-methyl-L-Cys

-
pH 7.8, 37ưC, mutant enzyme Y72F
3.1
S-methyl-L-Cys
-
beta-replacement reaction
5
S-methyl-L-Cys
-
alpha,beta-elimination
0.49
S-methyl-L-cysteine

recombinant His-tagged wild-type enzyme, pH 7.8, 37ưC
0.87
S-methyl-L-cysteine
pH 7.6, 37ưC
2.04
S-methyl-L-cysteine
-
purified recombinant tryptophanase in 200 mM potassium phosphate buffer (pH 7.5), at 37ưC
16
S-methyl-L-cysteine
-
pH 8.0, 25ưC
0.06
S-o-nitrophenyl-L-Cys

-
-
0.18
S-o-nitrophenyl-L-Cys
-
pH 7.8, 37ưC, mutant enzyme Y72F
additional information
additional information

-
-
-
additional information
additional information
-
-
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
kinetics of mutant H463F, high-pressure stopped-flow measurements, overview
-
additional information
additional information
-
pre-steady-state and steady-state kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
binding kinetics of enzyme mutant Y72F with substrates L-tryptophan, S-ethyl-L-cysteine, and oxindolyl-L-alanine, overview
-
additional information
additional information
-
binding kinetics of enzyme mutant Y72F with substrates L-tryptophan, S-ethyl-L-cysteine, and oxindolyl-L-alanine, overview
-
additional information
additional information
Michaelis-Menten kinetics, stopped-flow kinetics, rate and equilibrium constants for pre-steady-state reaction of F464A Escherichia coli enzyme TIL with L-tryptophan
-
additional information
additional information
-
Michaelis-Menten kinetics, stopped-flow kinetics, rate and equilibrium constants for pre-steady-state reaction of F464A Escherichia coli enzyme TIL with L-tryptophan
-
additional information
additional information
pre-steady state kinetics and steady state kinetic study, stopped-flow measurements and stopped-flow spectra of the reaction of TIL with L-tryptophan, overview. The pH dependence of kcat/Km of Escherichia coli TIL for tryptophan exhibits 2 basic groups, with pKas of 6.0 and 7.6. The base with pKa of 7.6 is involved in the deprotonation of the alpha-carbon of substrates, and the base with pKa of 6.0 activates the indole ring of the tryptophan substrate for elimination. There is a pH-independent primary isotope effect on kcat (Dkcat = 2.5) and kcat/Km (Dkcat/Km = 2.8) for alpha-[2H]-L-tryptophan, indicating that a step (or steps) involving transfer of the alpha-proton is partially rate-limiting. The TIL reaction shows pD-independent solvent isotope effects in D2O (D2Okcat ü 3:8 and D2Okcat=Km ü 2:8), and the substrate isotope effect is reduced in D2O (Dkcat = 1.25 and Dkcat/Km = 1.82), suggesting that the steady-state solvent and substrate isotope effects are on different steps. The proton inventory for the reaction of TIL is concave downward, indicating that multiple waters are involved in the transition state of the solvent sensitive step
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.22 - 5.6
beta-(benzimidazol-1-yl)-L-alanine
3 - 12.4
beta-chloro-L-Ala
0.0932
beta-chloroalanine
-
pH 7.8, 37ưC, mutant enzyme Y72F
0.0303
L-Ser
-
pH 7.8, 37ưC, mutant enzyme Y72F
2.2 - 44
S-(2-nitrophenyl)-L-cysteine
0.346
S-Benzyl-L-cysteine
recombinant His-tagged wild-type enzyme, pH 7.8, 37ưC
0.00046
S-benzylcysteine
-
pH 7.8, 37ưC, mutant enzyme Y72F
0.035 - 6
S-ethyl-L-cysteine
0.0051 - 5
S-methyl-L-Cys
0.2 - 0.5
S-methyl-L-cysteine
0.423
S-o-nitrophenyl-L-Cys
-
pH 7.8, 37ưC, mutant enzyme Y72F
0.00004
Trp
-
pH 7.8, 37ưC, mutant enzyme Y72F
0.22
beta-(benzimidazol-1-yl)-L-alanine

-
mutant H463F, pH 8.0, 25ưC
5.6
beta-(benzimidazol-1-yl)-L-alanine
-
wild-type enzyme, pH 8.0, 25ưC
3
beta-chloro-L-Ala

pH 8.0, 25ưC
12.4
beta-chloro-L-Ala
-
pH 8.0, 25ưC
0.24
L-Trp

-
purified recombinant tryptophanase in 200 mM sodium phosphate buffer (pH 7.5), at 37ưC
1.37
L-Trp
-
purified recombinant tryptophanase in 200 mM potassium phosphate buffer (pH 7.5), at 37ưC
0.009
L-tryptophan

recombinant mutant F464A, pH 7.8, 22ưC
0.45
L-tryptophan
pH 7.5, 37ưC
2.5
L-tryptophan
pH 8.0, 25ưC
4
L-tryptophan
-
wild-type enzyme, pH 8.0, 25ưC
5.252
L-tryptophan
recombinant His-tagged wild-type enzyme, pH 7.8, 37ưC
6
L-tryptophan
recombinant wild-type enzyme, pH 7.8, 22ưC
6.8
L-tryptophan
-
pH 8.0, 25ưC
2.2
S-(2-nitrophenyl)-L-cysteine

recombinant mutant F464A, pH 7.8, 22ưC
13.9
S-(2-nitrophenyl)-L-cysteine
pH 8.0, 25ưC
38
S-(2-nitrophenyl)-L-cysteine
recombinant wild-type enzyme, pH 7.8, 22ưC
44
S-(2-nitrophenyl)-L-cysteine
-
pH 8.0, 25ưC
1.1
S-benzyl-L-Cys

pH 8.0, 25ưC
5.2
S-benzyl-L-Cys
-
pH 8.0, 25ưC
0.4
S-ethyl-L-Cys

pH 8.0, 25ưC
6
S-ethyl-L-Cys
-
pH 8.0, 25ưC
0.035
S-ethyl-L-cysteine

-
pH 7.8, 37ưC, mutant enzyme Y72F
0.074
S-ethyl-L-cysteine
recombinant mutant F464A, pH 7.8, 22ưC
1.79
S-ethyl-L-cysteine
pH 7.6, 37ưC
1.87
S-ethyl-L-cysteine
-
purified recombinant tryptophanase in 200 mM potassium phosphate buffer (pH 7.5), at 37ưC
6
S-ethyl-L-cysteine
recombinant wild-type enzyme, pH 7.8, 22ưC
0.0051
S-methyl-L-Cys

-
pH 7.8, 37ưC, mutant enzyme Y72F
0.2
S-methyl-L-Cys
pH 8.0, 25ưC
5
S-methyl-L-Cys
-
pH 8.0, 25ưC
0.2
S-methyl-L-cysteine

pH 7.6, 37ưC
0.49
S-methyl-L-cysteine
recombinant His-tagged wild-type enzyme, pH 7.8, 37ưC
0.5
S-methyl-L-cysteine
-
purified recombinant tryptophanase in 200 mM potassium phosphate buffer (pH 7.5), at 37ưC
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
9.3 - 18.67
beta-(benzimidazol-1-yl)-L-alanine
0.77 - 2.4
beta-chloro-L-Ala
6.87
L-Trp
-
purified recombinant tryptophanase in 200 mM potassium phosphate buffer (pH 7.5), at 37ưC
29 - 510
S-(2-nitrophenyl)-L-cysteine
1.648
S-Benzyl-L-cysteine
recombinant His-tagged wild-type enzyme, pH 7.8, 37ưC
0.6 - 9
S-ethyl-L-cysteine
0.06 - 0.33
S-methyl-L-Cys
0.016 - 0.25
S-methyl-L-cysteine
9.3
beta-(benzimidazol-1-yl)-L-alanine

-
mutant H463F, pH 8.0, 25ưC
18.67
beta-(benzimidazol-1-yl)-L-alanine
-
wild-type enzyme, pH 8.0, 25ưC
0.77
beta-chloro-L-Ala

pH 8.0, 25ưC
2.4
beta-chloro-L-Ala
-
pH 8.0, 25ưC
0.067
L-tryptophan

recombinant mutant F464A, pH 7.8, 22ưC
1.96
L-tryptophan
pH 77.5, 37ưC
7.6
L-tryptophan
pH 8.0, 25ưC
8.582
L-tryptophan
recombinant His-tagged wild-type enzyme, pH 7.8, 37ưC
27
L-tryptophan
-
wild-type enzyme, pH 8.0, 25ưC
30
L-tryptophan
-
pH 8.0, 25ưC
30
L-tryptophan
recombinant wild-type enzyme, pH 7.8, 22ưC
29
S-(2-nitrophenyl)-L-cysteine

pH 8.0, 25ưC
170
S-(2-nitrophenyl)-L-cysteine
recombinant mutant F464A, pH 7.8, 22ưC
500
S-(2-nitrophenyl)-L-cysteine
recombinant wild-type enzyme, pH 7.8, 22ưC
510
S-(2-nitrophenyl)-L-cysteine
-
pH 8.0, 25ưC
11
S-benzyl-L-Cys

pH 8.0, 25ưC
81
S-benzyl-L-Cys
-
pH 8.0, 25ưC
0.28
S-ethyl-L-Cys

pH 8.0, 25ưC
9
S-ethyl-L-Cys
-
pH 8.0, 25ưC
0.6
S-ethyl-L-cysteine

pH 7.6, 37ưC
0.672
S-ethyl-L-cysteine
recombinant mutant F464A, pH 7.8, 22ưC
7.15
S-ethyl-L-cysteine
-
purified recombinant tryptophanase in 200 mM potassium phosphate buffer (pH 7.5), at 37ưC
9
S-ethyl-L-cysteine
recombinant wild-type enzyme, pH 7.8, 22ưC
0.06
S-methyl-L-Cys

pH 8.0, 25ưC
0.33
S-methyl-L-Cys
-
pH 8.0, 25ưC
0.016
S-methyl-L-cysteine

recombinant His-tagged wild-type enzyme, pH 7.8, 37ưC
0.23
S-methyl-L-cysteine
pH 7.6, 37ưC
0.25
S-methyl-L-cysteine
-
purified recombinant tryptophanase in 200 mM potassium phosphate buffer (pH 7.5), at 37ưC
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4.77
(2,3-di-O-methyl)-alpha-cyclodextrin
-
-
11.94
(2,3-di-O-methyl)-beta-cyclodextrin
-
-
4.97
(2-hydroxypropyl)-alpha-cyclodextrin
-
-
2.97
(2-hydroxypropyl)-beta-cyclodextrin
-
-
0.013
(S)-4-(benzimidazol-1-yl)-2-aminobutanoic acid
pH 8.0, 25ưC, recombinant enzyme
0.002
2,3-dihydro-L-tryptophan
pH 8.0, 25ưC, recombinant enzyme
0.0134
2-amino-4-(benzimidazol-1-yl)butyric acid
-
wild-type enzyme, pH 8.0, 25ưC
0.6
2-amino-5-(benzimidazol-1-yl)pentanoic acid
-
above, wild-type enzyme, pH 8.0, 25ưC
0.005
2-oxindolyl-L-alanine
pH 8.0, 25ưC, recombinant enzyme
174
alpha-amino-9,10-dihydro-9,10-dioxo-2-anthracenepropanoic acid
-
in 50 mM potassium phosphate buffer (pH 7.8), at 25ưC
0.3
beta-(benzimidazol-1-yl)-L-alanine
-
wild-type enzyme, pH 8.0, 25ưC
0.067
D,L-homophenylalanine
-
pH 7.8
0.0047
L-bishomotryptophan
pH 8.0, 25ưC, recombinant enzyme
0.067
L-homotryptophan
pH 8.0, 25ưC, recombinant enzyme
10.3
L-methionine
-
pH 7.8
14.2
L-phenylalanine
-
pH 7.8
52
L-tryptophan ethylester
-
in 50 mM potassium phosphate buffer (pH 7.8), at 25ưC
48
N-acetyl-L-tryptophan
-
in 50 mM potassium phosphate buffer (pH 7.8), at 25ưC
101
N-[3,6-dioxo-4-(phenylsulfanyl)cyclohexa-1,4-dien-1-yl]-L-tryptophanamide
-
in 50 mM potassium phosphate buffer (pH 7.8), at 25ưC
0.005 - 0.0614
oxindolyl-L-alanine
0.24
[2,3,6-tri-O-(2'-methoxyethyl)]-alpha-cyclodextrin
-
-
2.15
[2,3-di-O-(2'-methoxyethyl)]-alpha-cyclodextrin
-
-
0.68
[2,3-di-O-(2'-methoxyethyl)]-beta-cyclodextrin
-
-
0.52
[2,3-di-O-methyl-6-O-(2'-methoxyethyl)]-alpha-cyclodextrin
-
-
1.36
[2,3-di-O-methyl-6-O-(2'-methoxyethyl)]-beta-cyclodextrin
-
-
additional information
additional information
-
0.2
L-tryptophan

pH 8.0, 25ưC, recombinant enzyme
0.21
L-tryptophan
-
pH 7.8
0.005
oxindolyl-L-alanine

-
in 50 mM potassium phosphate buffer (pH 7.8), at 25ưC
0.005
oxindolyl-L-alanine
pH and temperature not specified in the publication
0.005
oxindolyl-L-alanine
recombinant wild-type enzyme, pH 7.8, 22ưC
0.0614
oxindolyl-L-alanine
recombinant mutant F464A, pH 7.8, 22ưC
additional information
additional information

-
Ki-values for reaction in aqueous methanol
-
additional information
additional information
pre-steady-state inhibition kinetics, rapid-scanning stopped-flow experiments
-
additional information
additional information
-
pre-steady-state inhibition kinetics, rapid-scanning stopped-flow experiments
-
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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malfunction
a truncated TnaA protein containing only domains D1 and D3 (D1D3) localizes to the cell 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
evolution

enzyme Trpase is classified as beta-eliminating lyase
evolution
residue Phe464 in Escherichia coli TIL is homologous to Phe459 in Proteus vulgaris TIL
evolution
residue Phe464 in Escherichia coli TIL is homologous to Phe459 in Proteus vulgaris TIL
evolution
the carbon-carbon lyases, tryptophan indole lyase (TIL) and tyrosine phenol-lyase (TPL, EC 4.1.99.2) are bacterial enzymes which catalyze the reversible elimination of indole and phenol from L-tryptophan and L-tyrosine, respectively. These pyridoxal 5'-phosphate-dependent enzymes show high sequence homology (about 40% identity) and both form homotetrameric structures. Pre-steady state kinetics with TPL and TIL show rapid formation of external aldimine intermediates, followed by deprotonation to give quinonoid intermediates absorbing at about 500 nm. The active sites of TIL and TPL are highly conserved with the exceptions of these residues: Arg381(TPL)/Ile396 (TIL), Thr124 (TPL)/Asp137 (TIL), and Phe448 (TPL)/His463 (TIL). The conserved tyrosine, Tyr71 (TPL)/Tyr74 (TIL) is essential for elimination activity with both enzymes, and likely plays a role as a proton donor to the leaving group. A unique feature of TIL and TPL is another strictly conserved lysine immediately preceding the pyridoxal 5'-phosphate-binding lysine, and hydrogen bonded to a water molecule bound to the monovalent cation. The mechanisms of TPL and TIL require both substrate strain and acid/base catalysis, and substrate strain is probably responsible for the very high substrate specificity of TPL and TIL. Both enzymes require a monovalent cation, either K+, NH4+, Rb+ or Cs+ for activity, with Na+ and Li+ giving little or no activity. The active site residues involved in PLP binding are highly conserved for both TIL and TPL. Sequence comparisons
evolution
the carbon-carbon lyases, tryptophan indole lyase (TIL) and tyrosine phenol-lyase (TPL, EC 4.1.99.2) are bacterial enzymes which catalyze the reversible elimination of indole and phenol from L-tryptophan and L-tyrosine, respectively. These pyridoxal 5'-phosphate-dependent enzymes show high sequence homology (about 40% identity) and both form homotetrameric structures. Pre-steady state kinetics with TPL and TIL show rapid formation of external aldimine intermediates, followed by deprotonation to give quinonoid intermediates absorbing at about 500 nm. The active sites of TIL and TPL are highly conserved with the exceptions of these residues: Arg381(TPL)/Ile396 (TIL), Thr124 (TPL)/Asp137 (TIL), and Phe448 (TPL)/His463 (TIL). The conserved tyrosine, Tyr71 (TPL)/Tyr74 (TIL) is essential for elimination activity with both enzymes, and likely plays a role as a proton donor to the leaving group. A unique feature of TIL and TPL is another strictly conserved lysine immediately preceding the pyridoxal 5'-phosphate-binding lysine, and hydrogen bonded to a water molecule bound to the monovalent cation. The mechanisms of TPL and TIL require both substrate strain and acid/base catalysis, and substrate strain is probably responsible for the very high substrate specificity of TPL and TIL. Both enzymes require a monovalent cation, either K+, NH4+, Rb+ or Cs+ for activity, with Na+ and Li+ giving little or no activity. The active site residues involved in PLP binding are highly conserved for both TIL and TPL. Sequence comparisons
metabolism

-
indole production requires TnaB responsible for exogenous L-tryptophan import
metabolism
-
tryptophanase is an initial enzyme for the degradation of L-tryptophan and 5-hydroxytryptophan in Escherichia coli
metabolism
-
indole production requires TnaB responsible for exogenous L-tryptophan import
-
physiological function

-
Hfq protein associates with tryptophanase under relatively higher extracellular indole levels, suggesting this is a feedback control of indole production
physiological function
-
tryptophan indole lyase produces indole from L-tryptophan, indole is a signaling molecule in bacteria, affecting biofilm formation, pathogenicity and antibiotic resistance
physiological function
the enzyme is responsible for the production of indole, an important intra- and interspecies signaling molecule in bacteria
physiological function
the Escherichia coli enzyme tryptophanase (TnaA) converts tryptophan to indole, which triggers physiological changes and regulates interactions between bacteria and their mammalian hosts. Tryptophanase production is induced by external tryptophan, but the activity of TnaA is also regulated by other mechanisms. TnaA activity is regulated by subcellular localization and by a loop-associated occlusion of its active site, formation of TnaA foci might regulate TnaA function. Model of post-translational regulation of TnaA activity by focus formation, overview
physiological function
the metabolic enzyme tryptophanase (TPase) is able to convert an odorless substrate like S-methyl-L-cysteine or L-tryptophan into the odorous products methyl mercaptan or indole
physiological function
tryptophanase is a bacterial enzyme involved in the degradation of tryptophan to indole, pyruvate and ammonia, which are compounds that are essential for bacterial survival. Tryptophanase is often overexpressed in stressed cultures
physiological function
-
tryptophan indole lyase produces indole from L-tryptophan, indole is a signaling molecule in bacteria, affecting biofilm formation, pathogenicity and antibiotic resistance
-
physiological function
-
the enzyme is responsible for the production of indole, an important intra- and interspecies signaling molecule in bacteria
-
additional information

determination of residues that affect assembly and localization of TnaA foci, overview
additional information
-
determination of residues that affect assembly and localization of TnaA foci, overview
additional information
eight catalytically important residues Thr52, Tyr74, Arg103, Asp137, Arg230, Lys269, Lys270, and His463 are located close to the Trpase active site and are absolutely conserved in Trpases. Five of them are located in the conserved regions and are reported to confer a crucial role for binding of the substrate and cofactor to produce the formation of the best intermediate that will lead to substrate degradation. Despite the apparent diversity in the protein sequences, these regions may be essential for enzyme activity to generate indole, which is an important agent for bacterial physiology, ecological balance, and virulence
additional information
the conformation of all holo subunits is the same in both crystal forms. The structures suggest that Trpase is flexible in the apoform. Its conformation partially closes upon binding of PLP. The closed conformation might correspond to the enzyme in its active state with both cofactor and substrate bound in a similar way as in tyrosine phenol-lyase
additional information
-
the conformation of all holo subunits is the same in both crystal forms. The structures suggest that Trpase is flexible in the apoform. Its conformation partially closes upon binding of PLP. The closed conformation might correspond to the enzyme in its active state with both cofactor and substrate bound in a similar way as in tyrosine phenol-lyase
additional information
the conserved Phe449 in TPL locates within 3 A of the substrate aromatic ring in the closed conformation
additional information
the conserved Phe459 in TPL locates within 3 A of the substrate aromatic ring in the closed conformation. Asp133 may be the residue that contacts the substrate
additional information
the reaction intermediate quinonoid complex of pyridoxal 5'-phosphate with L-tryptophan is modeled, based on the structure with inhibitor oxindolyl-L-alanine, by replacement of the oxindole ring with indole, and then docked manually into the active site by overlaying the pyridoxal 5'-phosphate rings of OIP and the L-tryptophan-pyridoxal 5'-phosphate complex
additional information
-
the reaction intermediate quinonoid complex of pyridoxal 5'-phosphate with L-tryptophan is modeled, based on the structure with inhibitor oxindolyl-L-alanine, by replacement of the oxindole ring with indole, and then docked manually into the active site by overlaying the pyridoxal 5'-phosphate rings of OIP and the L-tryptophan-pyridoxal 5'-phosphate complex
additional information
tryptophanase-positive Symbiobacterium thermophilum is a free-living syntrophic bacterium that grows effectively in a coculture with Geobacillus stearothermophilus, indole accumulation occurs when bicarbonate is added to the medium. The transcription of some genes involved in amino acid metabolism is sigma54-dependent, and a bacterial enhancer-binding protein containing a PAS domain controls the transcription under the presence of high levels of bicarbonate. sigma54-Dependent expression of tryptophanase in Symbiobacterium thermophilum, overview
additional information
-
tryptophanase-positive Symbiobacterium thermophilum is a free-living syntrophic bacterium that grows effectively in a coculture with Geobacillus stearothermophilus, indole accumulation occurs when bicarbonate is added to the medium. The transcription of some genes involved in amino acid metabolism is sigma54-dependent, and a bacterial enhancer-binding protein containing a PAS domain controls the transcription under the presence of high levels of bicarbonate. sigma54-Dependent expression of tryptophanase in Symbiobacterium thermophilum, overview
additional information
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tryptophanase-positive Symbiobacterium thermophilum is a free-living syntrophic bacterium that grows effectively in a coculture with Geobacillus stearothermophilus, indole accumulation occurs when bicarbonate is added to the medium. The transcription of some genes involved in amino acid metabolism is sigma54-dependent, and a bacterial enhancer-binding protein containing a PAS domain controls the transcription under the presence of high levels of bicarbonate. sigma54-Dependent expression of tryptophanase in Symbiobacterium thermophilum, overview
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additional information
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eight catalytically important residues Thr52, Tyr74, Arg103, Asp137, Arg230, Lys269, Lys270, and His463 are located close to the Trpase active site and are absolutely conserved in Trpases. Five of them are located in the conserved regions and are reported to confer a crucial role for binding of the substrate and cofactor to produce the formation of the best intermediate that will lead to substrate degradation. Despite the apparent diversity in the protein sequences, these regions may be essential for enzyme activity to generate indole, which is an important agent for bacterial physiology, ecological balance, and virulence
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