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Purine metabolism in Leishmania donovani amastigotes and promastigotes
Authors:D L Looker  R L Berens  J J Marr
Affiliation:University of Colorado Health Sciences Center, Department of Medicine, Division of Infectious Diseases, 4200 East 9th Avenue, Denver, CO 80262, U.S.A.
Abstract:
Purine metabolism in Leishmania donovani amastigotes was found to be similar to that of promastigotes with the exception of adenosine metabolism. Adenosine kinase activity in amastigotes is approximately 50-fold greater than in promastigotes. Amastigotes deaminate adenosine to inosine through adenosine deaminase, an enzyme not present in promastigotes. Inosine is cleaved to hypoxanthine and phosphoribosylated by hypoxanthine-guanine phosphoribosyltransferase. Promastigotes cleave adenosine to adenine and deaminate adenine to hypoxanthine via adenase, an enzyme not present in amastigotes. Hypoxanthine is phosphoribosylated by hypoxanthine-guanine phosphoribosyltransferase.
Keywords:Amastigotes  Promastigotes  Purine metabolism  Transformation  Adenine aminohydrolase  APRTase, adenine phosphoribosyltransferase  HGPRTase, hypoxanthine-guanine phosphoribosyltransferase  HPLC, high pressure liquid chromatography  PRPP, 5-phosphorylribose-1-pyrophosphate  PRTase, phosphoribosyltransferase  XPRTase, xanthine phosphoribosyltransferase
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