4.1.99.1: tryptophanase
This is an abbreviated version!
For detailed information about tryptophanase, go to the full flat file.
Word Map on EC 4.1.99.1
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4.1.99.1
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quinonoid
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transposase
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aldimine
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proteus
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phenol-lyase
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thermonuclease
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beta-elimination
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l-trp
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tryptophan-induced
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antitermination
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pyridoxal-p
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rho-dependent
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rapid-scanning
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phillips
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alvei
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analysis
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food industry
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biotechnology
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drug development
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medicine
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synthesis
- 4.1.99.1
-
quinonoid
- transposase
-
aldimine
- proteus
-
phenol-lyase
- thermonuclease
-
beta-elimination
- l-trp
-
tryptophan-induced
-
antitermination
-
pyridoxal-p
-
rho-dependent
-
rapid-scanning
-
phillips
- alvei
- analysis
- food industry
- biotechnology
- drug development
- medicine
- synthesis
Reaction
Synonyms
L-tryptophan indole-lyase, L-tryptophanase, TIL, tna2, TnaA, tnaA2, TNase, Tpase, Trpase, tryptophan indole lyase, tryptophan indole-lyase, tryptophan-indole lyase, tryptophanase, tryptophanase 2, VcTrpase
ECTree
4.1.99.1 tryptophanaseAdvanced search results
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results (KM Value
KM Value on EC 4.1.99.1 - tryptophanase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.346
S-Benzyl-L-cysteine
recombinant His-tagged wild-type enzyme, pH 7.8, 37°C
0.09
L-Trp
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purified recombinant tryptophanase in 200 mM sodium phosphate buffer (pH 7.5), at 37°C
0.1732
L-Trp
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in the presence of Hfq protein, in 0.1 M potassium phosphate buffer (pH 7.8), at 37°C
0.1901
L-Trp
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in the absence of Hfq protein, in 0.1 M potassium phosphate buffer (pH 7.8), at 37°C
0.2
L-Trp
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purified recombinant tryptophanase in 200 mM potassium phosphate buffer (pH 7.5), at 37°C
5.252
L-tryptophan
recombinant His-tagged wild-type enzyme, pH 7.8, 37°C
0.26
S-ethyl-L-cysteine
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purified recombinant tryptophanase in 200 mM potassium phosphate buffer (pH 7.5), at 37°C
0.49
S-methyl-L-cysteine
recombinant His-tagged wild-type enzyme, pH 7.8, 37°C
2.04
S-methyl-L-cysteine
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purified recombinant tryptophanase in 200 mM potassium phosphate buffer (pH 7.5), at 37°C
additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
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kinetics of mutant H463F, high-pressure stopped-flow measurements, overview
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additional information
additional information
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pre-steady-state and steady-state kinetics of wild-type and mutant enzymes, overview
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additional information
additional information
binding kinetics of enzyme mutant Y72F with substrates L-tryptophan, S-ethyl-L-cysteine, and oxindolyl-L-alanine, overview
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additional information
additional information
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binding kinetics of enzyme mutant Y72F with substrates L-tryptophan, S-ethyl-L-cysteine, and oxindolyl-L-alanine, overview
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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
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additional information
additional information
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Michaelis-Menten kinetics, stopped-flow kinetics, rate and equilibrium constants for pre-steady-state reaction of F464A Escherichia coli enzyme TIL with L-tryptophan
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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 ¼ 3:8 and D2Okcat=Km ¼ 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
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