PMID:9384533

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Citation

Lin, CH, Chen, S, Kwon, DS, Coward, JK and Walsh, CT (1997) Aldehyde and phosphinate analogs of glutathione and glutathionylspermidine: potent, selective binding inhibitors of the E. coli bifunctional glutathionylspermidine synthetase/amidase. Chem. Biol. 4:859-66

Abstract

The tripeptide glutathione is converted to glutathionylspermidine (Gsp) in Escherichia coli and in trypanosomatid parasites by an ATP-cleaving Gsp synthetase activity. In parasites, an additional glutathionylation forms bis-(glutathionyl)-spermidine, trypanothione, believed to be the major surveillance thiol involved in oxidant defense mechanisms in trypanosomatid parasites. In E. coli, the Gsp synthetase is part of a bifunctional enzyme opposed by the hydrolytic Gsp amidase.

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Keywords

Aldehydes; Amide Synthases/antagonists & inhibitors; Binding Sites; Enzyme Inhibitors/chemistry; Enzyme Inhibitors/metabolism; Escherichia coli/enzymology; Glutathione/analogs & derivatives; Glutathione/chemistry; Models, Chemical; Phosphinic Acids/chemistry; Spermidine/analogs & derivatives; Spermidine/chemistry

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