InterPro: IPR001864 Trypanothione reductase

Trypanothione reductase from Leishmania, and African and South American trypanosomes, has been purified and characterised [1]. The enzymes have similar physical, mechanistic and kinetic properties, and are members of the flavoprotein disulphide oxidoreductase family. Trypanothione is the parasite analogue of glutathione, hence this enzyme is equivalent to glutathione reductase. It catalyses the reaction:

NADPH + trypanothione = NADP(+) + reduced trypanothione

Trypanothione reductase shows pronounced specificty for its disulphide substrates, trypanothione disulphide or glutathionylspermidine disulphide. The 3D structure of the enzyme has been determined and its mode of substrate binding revealed in detail [2], offering hope for the design of drugs to combat Chagas disease. The structure belongs to the alpha+beta class, i.e. with mainly anti-parallel beta-sheets separated by alpha and beta regions. It contains an alpha-beta sandwich characteristic of FAD/NAD-linked reductases and a C-terminal dimerisation domain.