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Final model of TryS


ABSTRACT: Final model of TryS

SUBMITTER: Jurgen Haanstra 

PROVIDER: 108 | FAIRDOMHub | 2014-07-31

REPOSITORIES: FAIRDOMHub

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Publications

Dissecting the catalytic mechanism of Trypanosoma brucei trypanothione synthetase by kinetic analysis and computational modeling.

Leroux Alejandro E AE   Haanstra Jurgen R JR   Bakker Barbara M BM   Krauth-Siegel R Luise RL  

The Journal of biological chemistry 20130628 33


In pathogenic trypanosomes, trypanothione synthetase (TryS) catalyzes the synthesis of both glutathionylspermidine (Gsp) and trypanothione (bis(glutathionyl)spermidine (T(SH)2)). Here we present a thorough kinetic analysis of Trypanosoma brucei TryS in a newly developed phosphate buffer system at pH 7.0 and 37 °C, mimicking the physiological environment of the enzyme in the cytosol of bloodstream parasites. Under these conditions, TryS displays Km values for GSH, ATP, spermidine, and Gsp of 34,  ...[more]

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