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- W2335996976 abstract "Platyhelminth thioredoxin glutathione reductase (TGR) is a multifunctional enzyme that crosstalk between the conventional thioredoxin (Trx) and glutathione (GSH) system. It has been validated as a potential drug target in blood flukes. In the present study, we have performed a biochemical study on Fasciola gigantica TGR with substrates DTNB and GSSG. The Michaelis constant (Km) with DTNB was found to be 4.34 ± 0.12 μM while it was 61.15 ± 1.50 μM with GSSG. The kinetic results were compared with the TGR activities of other helminths. FgTGR showed typical hysteretic behavior with GSSG as other TGRs. We also described a homology-based structure of FgTGR. The cofactors (NADPH and FAD) and substrates (GSSG and DTNB) were docked, and two possible binding sites for substrates were identified in a single chain. The substrates were found to bind more favorably in the second site of TrxR domains. We also presented the first report on binding interaction of DTNB with a TGR. DTNB forms H-bond with His204 and Arg450 of chain A, Sec597, and Gly598 from chain B, salt-bridge with Lys124, and numerous other hydrophobic interactions. Helminth TGR represents an important enzyme in the redox and antioxidant system; hence, its inhibition can be used as an effective strategy against liver flukes." @default.
- W2335996976 created "2016-06-24" @default.
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- W2335996976 date "2016-08-01" @default.
- W2335996976 modified "2023-10-17" @default.
- W2335996976 title "Fasciola gigantica thioredoxin glutathione reductase: Biochemical properties and structural modeling" @default.
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- W2335996976 doi "https://doi.org/10.1016/j.ijbiomac.2016.04.063" @default.
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