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Information on EC 4.1.99.1 - tryptophanase and Organism(s) Escherichia coli and UniProt Accession P0A853
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4.1.99.1 tryptophanaseIUBMB Comments
A pyridoxal-phosphate protein, requiring K+. The enzyme cleaves a carbon-carbon bond, releasing indole and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. Also catalyses 2,3-elimination and beta-replacement reactions of some indole-substituted tryptophan analogues of L-cysteine, L-serine and other 3-substituted amino acids.
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Word Map
- 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
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
tryptophanase, tpase, tnase, trpase, tryptophan indole-lyase, l-tryptophanase, vctrpase, l-tryptophan indole-lyase, tryptophan indole lyase, tnaa2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-tryptophan indole-lyase
L-tryptophanase
TNase
Tpase
tryptophan indole-lyase
L-tryptophan indole-lyase
-
-
-
-
L-tryptophanase
-
-
-
-
TNase
-
-
-
-
Tpase
-
-
-
-
tryptophan indole-lyase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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
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
quinonoid intermediate formation involving Tyr71 and Cys298, mechanism, active site preorganization, overview
-
SYSTEMATIC NAME
IUBMB Comments
L-tryptophan indole-lyase (deaminating; pyruvate-forming)
A pyridoxal-phosphate protein, requiring K+. The enzyme cleaves a carbon-carbon bond, releasing indole and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. Also catalyses 2,3-elimination and beta-replacement reactions of some indole-substituted tryptophan analogues of L-cysteine, L-serine and other 3-substituted amino acids.
CAS REGISTRY NUMBER
COMMENTARY
9024-00-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-Trp + H2O
indole + pyruvate + NH4+
in the presence of high concentrations of ammonium phosphate
-
-
?
S-(2-nitrophenyl)-L-cysteine + H2O
2-nitrobenzenethiolate + pyruvate + NH3
-
-
-
?
beta-(benzimidazol-1-yl)-L-alanine + H2O
?
-
reaction via aldimine intermediate, high activity with wild-type enzyme and mutant H463F
-
-
?
D-serine
pyruvate + NH3
-
with high diammonium hydrogen phosphate concentration, e.g. 1.2 M
-
-
?
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
-
-
?
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+
-
-
-
-
?
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
-
-
?
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
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
the product indole is involved in cell signaling, involved in cell cycle regulation
-
-
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
S-(2-nitrophenyl)-L-cysteine + H2O
2-nitrobenzenethiolate + pyruvate + NH3
-
-
-
-
?
S-(2-nitrophenyl)-L-cysteine + H2O
2-nitrobenzenethiolate + pyruvate + NH3
-
-
-
-
ir
S-o-nitrophenyl-L-Cys + H2O
o-nitrothiophenol + pyruvate + NH3
-
-
-
-
?
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 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)
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-Trp + H2O
indole + pyruvate + NH4+
-
the product indole is involved in cell signaling, involved in cell cycle regulation
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
covalent binding required to activate the enzyme
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, 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
pyridoxal 5'-phosphate
-
-
677276, 681216, 681998, 691648, 701449, 703486, 704093, 704722, 704847, 705578, 705580, 713955, 715733, 726995, 728262, 728650
pyridoxal 5'-phosphate
-
some coenzyme analogues can replace pyridoxal 5'-phosphate
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
-
conversion of apoenzyme into the active holoenzyme is attained at 30°C in Tris-HCl buffer, pH 8.0, containing pyridoxal 5'-phosphate and K+, no conversion occurs at 5°C
pyridoxal 5'-phosphate
-
one enzyme molecule contains 4 pyridoxal 5'-phosphate combining sites
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
NH4+
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
Tl+
monovalent cation required for activity and for tight cofactor binding
Cl-
-
bound to enzyme, possibly required for stabilization of subunit interactions
K+
NH4+
Rb+
Tl+
additional information
K+
monovalent cation required for activity and for tight cofactor binding
K+
stabilizing, cold inactivation occurs more slowly in the presence of K+
NH4+
monovalent cation required for activity and for tight cofactor binding
K+
-
kinetics of tryptophanase inactivation/activation by sudden removal/addition of K+ with the aid of a crown ether or cryptand
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
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
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
alpha-amino-9,10-dihydro-9,10-dioxo-2-anthracenepropanoic acid
-
noncompetitive inhibition
beta-(benzimidazol-1-yl)-L-alanine
-
competitive, is also a good substrate for the wild-type and mutant enzymes
cyclodextrin
-
mixed type inhibition, competitive and non-competitive with inhibitor constants for different cyclodextrins between 0.5 and 10 mM
-
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
N-[3,6-dioxo-4-(phenylsulfanyl)cyclohexa-1,4-dien-1-yl]-L-tryptophanamide
-
uncompetitive inhibition
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
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
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diammonium hydrogen phosphate
-
diammonium hydrogen phosphate serves as an activator on tryptophan synthesis from D-serine, maximum activity at 20% saturation concentration
sRNA
-
dimers of plasmid ColE1 make an sRNA that interacts directly with the enzyme and enhance its substrate affinity
-
additional information
-
NaCl, NH4H2PO4, NH4NO3, NH4Cl, (BH4)2CO3, K2HPO4, and Na2HPO4 have no effect on enzyme activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1732
L-Trp
-
in the presence of Hfq protein, in 0.1 M potassium phosphate buffer (pH 7.8), at 37°C
0.1901
L-Trp
-
in the absence of Hfq protein, in 0.1 M potassium phosphate buffer (pH 7.8), at 37°C
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 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
-
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.2
S-(2-nitrophenyl)-L-cysteine
recombinant mutant F464A, pH 7.8, 22°C
38
S-(2-nitrophenyl)-L-cysteine
recombinant wild-type enzyme, pH 7.8, 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
170
S-(2-nitrophenyl)-L-cysteine
recombinant mutant F464A, pH 7.8, 22°C
500
S-(2-nitrophenyl)-L-cysteine
recombinant wild-type enzyme, pH 7.8, 22°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.013
(S)-4-(benzimidazol-1-yl)-2-aminobutanoic acid
pH 8.0, 25°C, recombinant enzyme
0.0134
2-amino-4-(benzimidazol-1-yl)butyric acid
-
wild-type enzyme, pH 8.0, 25°C
0.6
2-amino-5-(benzimidazol-1-yl)pentanoic acid
-
above, wild-type enzyme, pH 8.0, 25°C
174
alpha-amino-9,10-dihydro-9,10-dioxo-2-anthracenepropanoic acid
-
in 50 mM potassium phosphate buffer (pH 7.8), at 25°C
52
L-tryptophan ethylester
-
in 50 mM potassium phosphate buffer (pH 7.8), at 25°C
48
N-acetyl-L-tryptophan
-
in 50 mM potassium phosphate buffer (pH 7.8), at 25°C
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 25°C
0.005
oxindolyl-L-alanine
-
in 50 mM potassium phosphate buffer (pH 7.8), at 25°C
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
-
additional information
additional information
-
Ki-values for reaction in aqueous methanol
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.508
-
cell extract from strain MG1655H, harvested at OD600 of 0.8, at 37°C
0.808
-
cell extract from strain MG1655H, harvested at OD600 of 0.4, at 37°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
the enzyme accumulates as a spherical inclusion (focus) at midcell or at one pole. The D1D3 domain is sufficient for polar localization
additional information
-
the enzyme accumulates as a spherical inclusion (focus) at midcell or at one pole. The D1D3 domain is sufficient for polar localization
additional information
tryptophanase is often overexpressed in stressed cultures
additional information
-
tryptophanase is often overexpressed in stressed cultures
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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
physiological function
metabolism
physiological function
additional information
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
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
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
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
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
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
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
220000
50000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
tetramer
additional information
tetramer
enzyme TnaA probably dimerizes before assembling into the functional tetramer
tetramer
-
4 * 57000, equilibrium sedimentation in 6 M guanidine hydrochloride
additional information
of the two subunits in the asymmetric unit, one is found in the holoform, while the other appears to be in the apoform in a wide-open conformation with two sulfate ions bound in the vicinity of the active site. Enzyme Trpase is flexible in the apoform
additional information
-
of the two subunits in the asymmetric unit, one is found in the holoform, while the other appears to be in the apoform in a wide-open conformation with two sulfate ions bound in the vicinity of the active site. Enzyme Trpase is flexible in the apoform
additional information
peptide mass-fingerprinting of purified recombinant enzyme, mass spectrometry
additional information
-
peptide mass-fingerprinting of purified recombinant enzyme, mass spectrometry
additional information
-
upon cooling to 2°C, inactivation and dissociation of tetramer to dimer occurs, spectrofluorometry data
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo-form of enzyme without bound pyridoxal 5-phosphate but with two bound sulfate ions, hanging drop vapor diffusion method
mutant enzymes Y74F and C298S, hanging drop vapor diffusion method, using 30% (w/v) PEG 400, 100 mM HEPES pH 7.5, 200 mM MgCl2, 5 mM 2-mercaptoethanol
purified recombinant apo-enzyme in an open conformation, hanging drop vapour diffusion method with 25-30% PEG 4000, 30 mM ammonium sulfate, 20 mM 2-mercaptoethanol, 100 mM Tris-HCl, pH 9.0, X-ray diffraction structur determination and analysis at 2.8 A resolution
purified recombinant tryptophanase in holo- and semi-holoforms, hanging drop vapour diffusion method, mixing of 15-25 mg/ml protein in 50 mM sodium phosphate, pH 6.0, 5 mM 2-mercaptoethanol, and 0.5-2 mM pyridoxal 5'-phosphate in a ratio of 3:1 with precipitant solution containing 10-15% w/v ammonium sulfate, 25 mM potassium acetate, pH 5.4, and 3-10 mM2-mercaptoethanol, 2-7 days, X-ray diffraction structure determination and analysis at 2.9-3.2 A resolution, both crystal forms belong to the same space group P43212 but have slightly different unit-cell parameters, molecular replacement using the structure of apo Trpase, PDB ID 2oqx, as the search model
strong crystal contacts occur on the flat surface of the protein and that the size of crystal contact surface seems to correlate with the diffraction quality of the crystal. The tryptophanase structure, solved in its apo form, does not have covalent PLP bound in the active site, but two sulfate ions. The sulfate ions occupy the phosphoryl-binding site of PLP and the binding site of the alpha-carboxyl of the natural substrate tryptophan. One of the sulfate ions makes extensive interactions with both the transferase and PLP-binding domains of the protein and appears to be responsible for holding the enzyme in its closed conformation
crystallized in the apo form by the hanging-drop vapour-diffusion method using polyethylene glycol 400 as a precipitant and magnesium chloride as an additive. The crystals belong to the orthorhombic space group F222, with unit-cell parameters a = 118.4 A, b = 120.1 A, c = 171.2 A. Contains a monomer in the asymmetric unit with a solvent content of 55%. Tryptophanase mutants W330F and Y74F are crystallized under the same conditions and the crystals diffracted to a resolution limit of 1.9 A
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
E9A/R12A/R14A
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
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
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
S398A
S398A/R403A/D404A
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
T60A/Q61A/S62A/Q64A
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
H463F
W330F
-
as in wild type, upon cooling to 2°C, inactivation and dissociation of tetramer to dimer occurs, spectrofluorometry data
additional information
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
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
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
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
-
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2
-
upon cooling to 2°C, inactivation and dissociation of teramer to dimer occurs, spectrofluorometry data
55
60
additional information
2
subsequent to incubation at 2°C, wild type Trpase loses about 35% of its activity followed by dissociation into dimers. Complete dissociation/inactivation occurs after incubation for 20 h at 2°C and association/reactivation occurs upon warming for few hours
additional information
inactivation of the enzyme at low temperatures due to dissociation of the active tetramer into dimers upon cold incubation
additional information
-
inactivation of the enzyme at low temperatures due to dissociation of the active tetramer into dimers upon cold incubation
additional information
-
mutant strain ts6 with an enzyme with higher thermostability
additional information
-
about 80% activity at 50°C after 2 hours, about 20% activity after incubation at 0°C for 3 hours
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity decreases at pressures above 50 MPa, and by 100 MPa is less than 10% of the activity at 1 bar, initial increase in activity with pressure, reaching a maximum of about 140% at 30 MPa.
-
immobilized enzyme shows higher thermal stability and resistance to a denaturing agent such as guanidine-HCl than the soluble enzyme
-
rapid inactivation by visible light irradiation in presence of pyridoxal 5'-phosphate. Photoinactivation follows pseudo-first-order kinetics
-
when used repeatedly in a batch system or continously in a flow system in the absence of added pyridoxal 5'-phosphate, immobilized holo-tryptophanase gradually loses its original activity, pyridoxal 5'-phosphate restores its initial activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
stored as a suspension under nitrogen in 0.1 M potassium phosphate, pH 8.0, 0.2 mM dithiothreitol, 1 mM EDTA, and 2 M (NH4)2SO4
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Sephadex A-50 gel filtration or DEAE-Sepharose 4B column chromatography, and Sephacryl S-300 gel filtration
gene tnaA, recombinant enzyme from Escherichia coli strain Rosetta (DE3) pLysS by ammnoium sulfate fractionation, dialysis, anion exchange and hydrophobic interaction chromatography, followed by preparative gel filtration, and ultrafiltration
no added pyridoxal 5-phosphate during purification procedure resulting in the inactive apo-form of the enzyme
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by protamine sulfate treatment, hydrophobic interaction chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene tnaA, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene tnaA, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain GL619
gene tnaA, recombinant overexpression of the enzyme in Escherichia coli strain Rosetta (DE3) pLysS
expressed in wine yeast strains Saccharomyces cerevisiae strains YHUM272a and VIN13, expression of enzyme results in a strong increase of passion fruit aroma in wine
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
tryptophanase is often overexpressed in stressed cultures, e.g. under alkaline stress
the endogenous oxidative stress in ibpAB cells leads to increased expression of tryptophanase
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
the metabolic enzyme tryptophanase (TPase) is the key component in an odor-based sensor system. The enzyme is able to convert an odorless substrate like S-methyl-L-cysteine or L-tryptophan into the odorous products methyl mercaptan or indole. 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 biotin-labeled molecular recognition elements, thereby enabling a broad range of applications for this odor-based reporting system
food industry
-
expression of enzyme in wine yeast results in a strong increase of passion fruit aroma in wine
medicine
-
transposon insertion in gene results in a strain unable to form biofilm on polystyrene and to adhere to human pneumocyte cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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
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
-
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.
Raibaud, O.; Goldberg, M.E.
The dissociated tryptophanase subunit is inactive
J. Biol. Chem.
251
2820-2824
1976
Escherichia coli
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
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
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
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
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
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
-
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
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
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
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
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
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
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
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
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
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
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
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
-
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
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
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
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
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)
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
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
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)
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
-
Chattoraj, D.K.
Tryptophanase in sRNA control of the Escherichia coli cell cycle
Mol. Microbiol.
63
1-3
2007
Escherichia coli
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
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
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
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)
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
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
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
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
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
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
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
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
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
Hara, R.; Kino, K.
Enhanced synthesis of 5-hydroxy-L-tryptophan through tetrahydropterin regeneration
AMB Express
3
70
2013
Escherichia coli
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
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
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
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
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
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
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
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)
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
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)
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