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The enzymes of purine salvage in Trypanosoma cruzi, Trypanosoma brucei and Leishmania mexicana

Published online by Cambridge University Press:  06 April 2009

Mary J. Davies ,
A. M. Ross  and
W. E. Gutteridge
Mary J. Davies
Affiliation:
Biological Laboratory, University of Kent, Canterbury, Kent CT2 7N J
A. M. Ross
Affiliation:
Biological Laboratory, University of Kent, Canterbury, Kent CT2 7N J
W. E. Gutteridge
Affiliation:
Biological Laboratory, University of Kent, Canterbury, Kent CT2 7N J
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Summary

We have previously shown the presence of various purine salvage enzymes in Trypanosoma cruzi, including phosphoribosyltransferase, aminohydrolase, kinase, phosphorylase and hydrolase activities. We now report that a similar situation occurs in Leishmania mexicana amazonensis and Trypanosoma brucei brucei. In all three organisms we found higher levels of activity for the phosphoribosyltransferase enzymes than for the nucleoside kinases, suggesting a preference for the salvage of purine bases rather than nucleosides. Similarly, absence of inosine phosphorylase activity suggests that only one route for the salvage of hypoxanthine is available to the three organisms. The most striking difference was that whereas T. cruzi and T. brucei possessed adenosine aminohydrolase activity, this was not detected in L. mexicana; instead adenine amino-hydrolase activity was found. The overall similarity, as judged by the distribution of enzyme activities, of purine salvage in these three members of the kinetoplastida suggest a broad spectrum of activity for any inhibitor acting in this area; the plethora of alternative salvage pathways, however, suggests that in no case would such inhibition be cidal.

Type
Research Article
Information
Parasitology , Volume 87 , Issue 2 , October 1983 , pp. 211 - 217
Copyright
Copyright © Cambridge University Press 1983

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