Hostname: page-component-8448b6f56d-c4f8m Total loading time: 0 Render date: 2024-04-25T04:07:23.637Z Has data issue: false hasContentIssue false
  • English
  • Français

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
Get access Rights & Permissions [Opens in a new window]

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

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Berens, R. L., Marr, J. J. & Brun, R. (1980). Pyrazolo-pyrimidine metabolism in African Trypanosomes: metabolic similarities to Trypanosoma cruzi and Leishmania spp. Molecular and Biochemical Parasitology 1, 69–73.Google Scholar
Berens, R. L., Marr, J. J., La Fon, S. W. & Nelson, D. J. (1981). Purine metabolism in Trypanosoma cruzi. Molecular and Biochemical Parasitology 3, 187–96.CrossRefGoogle ScholarPubMed
Fish, W. R., Marr, J. J. & Berens, R. L. (1982). Purine metabolism in Trypanosoma brucei gambiense. Biochimica el biophysica acta 714, 422–8.Google Scholar
Gutteridge, W. E. & Davies, M. J. (1981). Enzymes of purine salvage in Trypanosoma cruzi. FEBS Letters 127, 211–14.Google Scholar
Gutteridge, W. E., Knowler, J. & Coombs, J. D. (1969). Growth of Trypanosoma cruzi in human heart tissue cells and effects of aminonucleoside of puromycin, trypacydin and aminopterin. Journal of Protozoology 16, 521–5.Google Scholar
Hammond, D. J. & Gutteridge, W. E. (1982). UMP synthesis in the Kinetoplastida. fiiocAiraica et biophysica acta 718, 1–10.Google Scholar
Henderson, J. F. & Paterson, A. R. P. (1973). Nucleotide Metabolism. An Introduction. New York: Academic Press.Google Scholar
Kidder, G. W. & Nolan, L. L. (1979). Adenine aminohydrolase: occurrence and possible significance in trypanosomatid flagellates. Proceedings of the National Academy of Sciences, USA 76, 3670–2.CrossRefGoogle Scholar
Kidder, G. W., Dewey, V. C.& Nolan, L. L. (1977). Adenine deaminase of a eukaryotic animal cell, Crithidia fasciculata. Archives of Biochemistry and Biophysics 183, 7–12.Google Scholar
Konigk, E. & Putfarken, B. (1980). Stage specific differences of a perhaps signal transferring system in Leishmania donovani. Tropenmedizin und Parasitologic 31, 421–4.Google Scholar
Koszalka, G. W. & Krenitsky, T. A. (1979). Nucleosidases from Leishmania donovani. Journal of Biological Chemistry 254, 8185–93.Google Scholar
La Fon, S. W. & Nelson, D. J. (1982). Purine and pyrimidine salvage pathways in Leishmania donovani. Biochemical Pharmacology 31, 231–8.Google Scholar
Lanham, S. M. (1968). Separation of trypanosomes from the blood of infected rats and mice by anion exchangers. Nature 218, 1273–4.Google Scholar
Marr, J. J., Berens, R. L. & Nelson, D. J. (1978 a). Purine metabolism in Leishmania donovani and Leishmania braziliensis. Biochimica et biophysica acta 544, 360–71.CrossRefGoogle ScholarPubMed
Marr, J. J., Berens, R. L. & Nelson, D. J. (1978 b). Antitrypanosomal effect of allopurinol: conversion in vivo to aminopyrazolopyrimidine nucleotides by Trypanosoma cruzi. Science 210, 1018–20.Google Scholar
Nolan, L. L. & Kidder, G. W. (1980). Inhibition of growth and purine metabolising enzymes of trypanosomatid flagellates by N6-methyladenine. Antimicrobial Agents and Chemotherapy 17, 567–71.CrossRefGoogle Scholar
Sanchez, G., Knight, S. & Strickler, J. (1976). Nucleotide transport in African trypanosomes. Comparative Biochemistry and Physiology 53 B, 419–21.Google Scholar
Schmidt, G., Walter, R. D. & Konigk, E. (1975). A purine nucleoside hydrolase from Trypanosoma gambiense, purification and properties. Tropenmedizin und Parasitologic 26, 19–26.Google Scholar
Tuttle, J. V. & Krenitsky, T. A. (1980). Purine phosphoribosyl-transferases from Leishmania donovani. Journal of Biological Chemistry 255, 909–16.Google Scholar