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Information on EC 4.1.99.1 - tryptophanase
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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
- alvei
-
rapid-scanning
-
phillips
-
rho-dependent
- medicine
- analysis
- drug development
- food industry
- synthesis
- biotechnology
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
L-tryptophan indole-lyase, L-tryptophanase, TIL, tna2, TnaA, tnaA2, TNase, Tpase, Trpase, tryptophan indole lyase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-tryptophan indole-lyase
L-tryptophanase
TIL
tna2
TnaA
tnaA2
TNase
Tpase
Trpase
tryptophan indole lyase
tryptophan indole-lyase
tryptophanase
tryptophanase 2
VcTrpase
L-tryptophan indole-lyase
-
-
-
-
L-tryptophanase
-
-
-
-
TNase
-
-
-
-
Tpase
-
-
-
-
tryptophan indole-lyase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-tryptophan + H2O = indole + pyruvate + NH3
-
-
-
-
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
-
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
beta-elimination
elimination
replacement
-
-
beta-position of amino acid
-
elimination
-
-
beta-position of amino acid
-
elimination
-
-
alpha,beta-position of amino acid
-
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9024-00-4
-
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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-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
-
-
?
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 + NH4+
-
-
-
-
ir
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+
-
-
-
-
?
5-hydroxy-L-Trp + H2O
?
-
6.7% 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
-
-
?
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 + S-methyl-L-Cys
L-Trp + ?
-
beta-replacement reaction
-
?
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-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
L-Trp + H2O
indole + pyruvate + NH4+
-
-
-
?
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
very high substrate specificity of TIL
-
-
?
L-tryptophan + H2O
indole + pyruvate + NH3
Symbiobacterium thermophilum T / IAM 14863 / JCM 14929
-
-
-
?
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-cysteine + H2O
phenylmethanethiol + pyruvate + NH3
-
-
-
?
S-benzyl-L-cysteine + H2O
phenylmethanethiol + pyruvate + NH3
-
-
-
?
S-ethyl-L-Cys + H2O
ethanethiol + pyruvate + NH4+
-
-
-
?
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-methyl-L-Cys + H2O
?
-
63.8% of the activity with L-Trp
-
-
?
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+
-
-
-
-
?
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
?
-
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
?
-
-
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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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-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
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
very high substrate specificity of TIL
-
-
?
L-tryptophan + H2O
indole + pyruvate + NH3
Symbiobacterium thermophilum T / IAM 14863 / JCM 14929
-
-
-
?
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
-
677276, 681216, 681998, 691648, 701449, 703486, 704093, 704722, 704847, 705578, 705580, 713955, 715733, 726995, 728262, 728650
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
-
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 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
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
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, 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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cl-
-
bound to enzyme, possibly required for stabilization of subunit interactions
K+
NH4+
Rb+
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+
additional information
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
K+
monovalent cation required for activity and for tight cofactor binding
K+
stabilizing, cold inactivation occurs more slowly in the presence of K+
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 and for tight cofactor binding
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
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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
-
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
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
N-[3,6-dioxo-4-(phenylsulfanyl)cyclohexa-1,4-dien-1-yl]-L-tryptophanamide
-
uncompetitive inhibition
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 10° 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
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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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
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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
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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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
-
purified recombinant tryptophanase in 200 mM sodium phosphate buffer (pH 7.5), at 37°C
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
0.2
L-Trp
-
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
-
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
-
purified recombinant tryptophanase in 200 mM potassium phosphate buffer (pH 7.5), at 37°C
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 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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.346
S-Benzyl-L-cysteine
recombinant His-tagged wild-type enzyme, pH 7.8, 37°C
0.24
L-Trp
-
purified recombinant tryptophanase in 200 mM sodium phosphate buffer (pH 7.5), at 37°C
1.37
L-Trp
-
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
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
1.87
S-ethyl-L-cysteine
-
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
0.5
S-methyl-L-cysteine
-
purified recombinant tryptophanase in 200 mM potassium phosphate buffer (pH 7.5), at 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.87
L-Trp
-
purified recombinant tryptophanase in 200 mM potassium phosphate buffer (pH 7.5), at 37°C
1.648
S-Benzyl-L-cysteine
recombinant His-tagged wild-type enzyme, pH 7.8, 37°C
8.582
L-tryptophan
recombinant His-tagged wild-type enzyme, pH 7.8, 37°C
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
7.15
S-ethyl-L-cysteine
-
purified recombinant tryptophanase in 200 mM potassium phosphate buffer (pH 7.5), at 37°C
0.016
S-methyl-L-cysteine
recombinant His-tagged wild-type enzyme, pH 7.8, 37°C
0.25
S-methyl-L-cysteine
-
purified recombinant tryptophanase in 200 mM potassium phosphate buffer (pH 7.5), at 37°C
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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
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, 22°C
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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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
0.747
-
cell extract from strain MG1655, harvested at OD600 of 0.4, at 37°C
0.774
-
cell extract from strain MG1406, harvested at OD600 of 0.4, at 37°C
0.808
-
cell extract from strain MG1655H, harvested at OD600 of 0.4, at 37°C
0.818
-
cell extract from strain MG1655, harvested at OD600 of 0.8, at 37°C
1.475
-
cell extract from strain MG1406, harvested at OD600 of 0.8, at 37°C
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9.8
-
pH 7: about 45% of maximal activity, pH 9.8: about 90% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
25
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
37334, 37335, 37336, 37337, 37339, 37340, 37341, 37342, 37348, 37351, 37354, 37355, 37357, 37358, 37359, 37360, 37362, 37364, 650374, 650435, 650757, 651028, 663488, 664076
-
-
brenda
amount of tryptophanase is diminished in mutants DELTAdnaJ and DELTAdnaKdnaJ. DnaJ and DnaK molecular chaperones influence the amount of tryptophanase
-
-
brenda
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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
brenda
additional information
-
the enzyme accumulates as a spherical inclusion (focus) at midcell or at one pole. The D1D3 domain is sufficient for polar localization
brenda
additional information
tryptophanase is often overexpressed in stressed cultures
brenda
additional information
-
tryptophanase is often overexpressed in stressed cultures
brenda
additional information
tryptophanase-positive Symbiobacterium thermophilum is a free-living syntrophic bacterium that grows effectively in a coculture with Geobacillus stearothermophilus strain S (JCM 30104)
brenda
additional information
-
tryptophanase-positive Symbiobacterium thermophilum is a free-living syntrophic bacterium that grows effectively in a coculture with Geobacillus stearothermophilus strain S (JCM 30104)
brenda
additional information
Symbiobacterium thermophilum T / IAM 14863 / JCM 14929
-
tryptophanase-positive Symbiobacterium thermophilum is a free-living syntrophic bacterium that grows effectively in a coculture with Geobacillus stearothermophilus strain S (JCM 30104)
-
brenda
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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
metabolism
physiological function
additional information
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
Symbiobacterium thermophilum T / IAM 14863 / JCM 14929
-
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
-
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
-
Show AA Sequence and Transmembrane Helices (2636 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
210000
216000
-
aggregation to form species with MW 432000 Da, 648000 Da, and 864000 Da, sucrose density gradient centrifugation, equilibrium sedimentation
220000
50000
52000
52500
55000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
tetramer
additional information
homodimer