1.8.1.12: trypanothione-disulfide reductase
This is an abbreviated version!
For detailed information about trypanothione-disulfide reductase, go to the full flat file.
Word Map on EC 1.8.1.12
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1.8.1.12
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trypanosoma
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leishmania
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cruzi
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chagas
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trypanosomatids
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leishmaniasis
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brucei
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trypanocidal
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antileishmanial
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donovani
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promastigotes
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trypanosomiasis
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infantum
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amastigotes
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fasciculata
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antitrypanosomal
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crithidia
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antiparasitic
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flavoenzyme
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phenothiazine
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medicine
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epimastigotes
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nifurtimox
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amazonensis
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antiprotozoal
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trypomastigotes
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tryparedoxin
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kinetoplastida
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leishmanicidal
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congolense
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rhodesiense
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miltefosine
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antimonial
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ts2
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n1,n8-bisglutathionylspermidine
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benznidazole
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clomipramine
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glutathionylspermidine
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antichagasic
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thioridazine
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ovothiols
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nitrofuran
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trypanothione-dependent
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pharmacology
- 1.8.1.12
- trypanosoma
- leishmania
- cruzi
- chagas
-
trypanosomatids
- leishmaniasis
- brucei
-
trypanocidal
-
antileishmanial
- donovani
- promastigotes
- trypanosomiasis
- infantum
- amastigotes
- fasciculata
-
antitrypanosomal
- crithidia
-
antiparasitic
-
flavoenzyme
- phenothiazine
- medicine
- epimastigotes
- nifurtimox
- amazonensis
-
antiprotozoal
- trypomastigotes
- tryparedoxin
- kinetoplastida
-
leishmanicidal
- congolense
- rhodesiense
- miltefosine
-
antimonial
- ts2
-
n1,n8-bisglutathionylspermidine
- benznidazole
- clomipramine
- glutathionylspermidine
-
antichagasic
- thioridazine
-
ovothiols
-
nitrofuran
-
trypanothione-dependent
- pharmacology
Reaction
Synonyms
EC 1.6.4.8, LbTryR, LdTryR, Li-TryR, LiTR, N(1),N(8)-bis(glutathionyl)spermidine reductase, NADPH2:trypanothione oxidoreductase, TbTR, TCDM_11669, TcTR, TPR, TR, trypanothione disulfide reductase, trypanothione reductase, trypanothione-disulfide reductase, TryR
ECTree
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Crystallization
Crystallization on EC 1.8.1.12 - trypanothione-disulfide reductase
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recombinant glutathione-trypanothione reductase-like enzyme, hanging-drop vapour diffusion method, 0.1 M potasssium phosphate, pH 8.0
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molecular docking of 5-nitroimidazole analogues to identify putative inhibitors
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molecular docking of series of febrifugine analogues to identify putative inhibitors
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crystal structure of thr enzyme (LiTR) at 3.6 A resolution in its reduced state (complex with trypanothione) and oxidized state
hanging drop vapour diffusion method, using ammonium sulfate as precipitant agent, at 21°C
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in complex with inhibitor 6-(sec-butoxy)-2-((3-chlorophenyl)thio)pyrimidin-4-amine. The inhibitor binds to the catalytic site and interacts with residues Glu466', Cys57 and Cys52
hanging drop vapor diffusion method, using 0.1 M bis-Tris propane pH 8.0, 5% (v/v) PEG 400, 2M ammonium sulfate
quantitative structureactivity relationship models to predict the activity of inhibitors and investigation on structural requirements for the selective inhibition
molecular docking of inhibitor isopropyl 2-isobutyryl-3-trifluoromethylquinoxaline-7-carboxylate 1,4-di-N-oxide
purified recombinant enzyme, reduced by NADPH, inactivated by binding of quinacrine mustard, 13 mg/ml enzyme-inhibitor complex in Na+ malate, pH 6.0, with precipitant 20% w/v PEG 8000, X-ray diffraction structure determination and analysis at 2.7 A resolution
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substrate binding and crystal structure in complex with trypanothione disulfide, molecular modeling with potential inhibitors
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