Purine metabolism in Leishmania donovani amastigotes and promastigotes |
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Authors: | D L Looker R L Berens J J Marr |
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Affiliation: | University of Colorado Health Sciences Center, Department of Medicine, Division of Infectious Diseases, 4200 East 9th Avenue, Denver, CO 80262, U.S.A. |
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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. |
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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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