4.1.99.1: tryptophanase
This is an abbreviated version!
For detailed information about tryptophanase, go to the full flat file.
Word Map on EC 4.1.99.1
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4.1.99.1
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quinonoid
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transposase
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aldimine
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proteus
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phenol-lyase
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thermonuclease
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beta-elimination
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l-trp
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tryptophan-induced
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antitermination
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pyridoxal-p
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rho-dependent
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rapid-scanning
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phillips
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alvei
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analysis
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food industry
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biotechnology
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drug development
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medicine
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synthesis
- 4.1.99.1
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quinonoid
- transposase
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aldimine
- proteus
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phenol-lyase
- thermonuclease
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beta-elimination
- l-trp
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tryptophan-induced
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antitermination
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pyridoxal-p
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rho-dependent
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rapid-scanning
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phillips
- alvei
- analysis
- food industry
- biotechnology
- drug development
- medicine
- synthesis
Reaction
Synonyms
L-tryptophan indole-lyase, L-tryptophanase, TIL, tna2, TnaA, tnaA2, TNase, Tpase, Trpase, tryptophan indole lyase, tryptophan indole-lyase, tryptophan-indole lyase, tryptophanase, tryptophanase 2, VcTrpase
ECTree
4.1.99.1 tryptophanaseAdvanced search results
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results (Inhibitors
Inhibitors on EC 4.1.99.1 - tryptophanase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
2-amino-4-(benzimidazol-1-yl)butyric acid
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i.e. homo-BZI-Ala, a potent competitive inhibitor
2-amino-5-(benzimidazol-1-yl)pentanoic acid
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i.e. bishomo-BZI-Ala, weak inhibition
alpha-amino-9,10-dihydro-9,10-dioxo-2-anthracenepropanoic acid
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noncompetitive inhibition
beta-(benzimidazol-1-yl)-L-alanine
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competitive, is also a good substrate for the wild-type and mutant enzymes
Bifidobacterium adolescentis SPM0212
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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
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cyclodextrin
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mixed type inhibition, competitive and non-competitive with inhibitor constants for different cyclodextrins between 0.5 and 10 mM
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diammonium hydrogen phosphate
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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
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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
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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
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additional information
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when bound to silver nanoparticles, TNase activity decreases significantly by 50% for carbonate coated silver nanoparticles and by over 90% for bare silver nanoparticles
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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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additional information
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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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