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Literature summary extracted from

  • Fata, F.; Silvestri, I.; Ardini, M.; Ippoliti, R.; Di Leandro, L.; Demitri, N.; Polentarutti, M.; Di Matteo, A.; Lyu, H.; Thatcher, G.R.J.; Petukhov, P.A.; Williams, D.L.; Angelucci, F.
    Probing the surface of a parasite drug target thioredoxin glutathione reductase using small molecule fragments (2021), ACS Infect. Dis., 7, 1932-1944 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.8.1.B1 sitting drop method Schistosoma mansoni

Protein Variants

EC Number Protein Variants Comment Organism
1.8.1.B1 E330A/D334A mutation of two key residues interacting with the inhibitor 4-aminopiazthiole. Inhibition at 0.5 mM 4-aminopiazthiole is indistinguishable from that of the wild type enzyme Schistosoma mansoni
1.8.1.B1 E337A mutation of E337 an interacting residue of the inhibitor indole-3-carbinol, Inhibition at 0.5 mM indole-3-carbinol is indistinguishable from that of the wild type enzyme Schistosoma mansoni

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.8.1.B1 4-aminopiazthiole inhibit the enzyme in a NADPH-dependent manner, and the inhibition appears to be irreversible even upon extensive dilution of the inhibited protein Schistosoma mansoni
1.8.1.B1 indole-3-carbinol inhibit the enzyme in a NADPH-dependent manner, and the inhibition appears to be irreversible even upon extensive dilution of the inhibited protein Schistosoma mansoni

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.B1 Schistosoma mansoni A0A3Q0KFL1
-
-

Synonyms

EC Number Synonyms Comment Organism
1.8.1.B1 TGR
-
 Schistosoma mansoni
1.8.1.B1 thioredoxin glutathione reductase
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 Schistosoma mansoni