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- W2065720507 abstract "Despite their phylogenetic divergence, several Proteobacteria species and the eclectic Euglenozoa lineage have in common the capacity to synthesize mono- and/or bis-glutathionyl polyamines. At variance with Proteobacteria, in trypanosomatid parasites (Euglenozoa Phylum), the irruption of thiol-polyamine conjugates leads to major genetic and molecular changes and adaptions in the enzymatic systems that, in most organisms, operate with glutathione and thioredoxin. Whereas enterobacteria can dispense of glutathionylspermidine, in pathogenic trypanosomatids, the dithiol bisglutathionyl-spermidine (common name: trypanothione) has a dominant and essential role in thiol-redox metabolism. This chapter addresses aspects related to the occurrence, biosynthesis, and physicochemical properties of (mono/bis)glutathionyl-spermidine, as well as the major molecular features and biological functions of the oxidoreductases depending on this redox cofactor/ligand. Given the essential role of trypanothione for trypanosomatids and the medical relevance of the diseases they cause, the pharmacological potential of components from this redox system is also discussed." @default.
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- W2065720507 date "2002-11-01" @default.
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- W2065720507 title "Silencing of the thioredoxin gene in Trypanosoma brucei brucei" @default.
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- W2065720507 doi "https://doi.org/10.1016/s0166-6851(02)00215-3" @default.
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