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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

Reaction

trypanothione
+
NADP+
=
trypanothione disulfide
 +
NADPH
 +
H+

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

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.1 With NAD+ or NADP+ as acceptor
                1.8.1.12 trypanothione-disulfide reductase

Crystallization

Crystallization on EC 1.8.1.12 - trypanothione-disulfide reductase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant glutathione-trypanothione reductase-like enzyme, hanging-drop vapour diffusion method, 0.1 M potasssium phosphate, pH 8.0
-
substrate-binding and structure analysis
-
molecular docking of 5-nitroimidazole analogues to identify putative inhibitors
-
molecular docking of series of febrifugine analogues to identify putative inhibitors
-
crystal structure of thr enzyme (LiTR) at 3.6 A resolution in its reduced state (complex with trypanothione) and oxidized state
hanging drop vapor diffusion method
hanging drop vapour diffusion method, using ammonium sulfate as precipitant agent, at 21°C
-
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
hanging drop vapor diffusion method
quantitative structure–activity relationship models to predict the activity of inhibitors and investigation on structural requirements for the selective inhibition
hanging drop method in presence of 2 M (NH4)2SO4 at 4°C
-
identification of putative inhibitors by molecular docking
-
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
-
substrate binding and crystal structure in complex with trypanothione disulfide, molecular modeling with potential inhibitors
-