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Abstract                 Volume:4  Issue-4  Year-2016          Original Research Articles


Online ISSN : 2347 - 3215
Issues : 12 per year
Publisher : Excellent Publishers
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Enzymes of the De novo Pyrimidine Biosynthetic Pathway in Leishmania tropica
Husain F. Hassan*
Department of Biology, College of Science, University of Kirkuk, Iraq
*Corresponding author
Abstract:

The pathway of de novo pyrimidine biosynthesis in the amastigote and Promastigote forms of Leishmania tropica has been investigated.Both parasite forms contained all six enzyme activities. Carbamoyl phosphate synthase (CPSase) utilizes L- glutamine and not ammonia as the amine group donor. Dihydroorotate dehydrogenase (DHO-DHase) was found to be cytoplasmic, where as orotate phosphoribosyltransferase (OPRTase) and orotidylate decarboxylase (ODCase) were found to be particulate. N-(phosphonacetyl)-L-aspartate, dihydro-5azaorotate, 5-azaorotate and 6-aza-UMP were found to be a potent inhibitor of the aspartate transcarbamoylase (ATCase), DHO-DHase, OPRTase, and ODCase, respectively.

Keywords: Leishmania,de novo,pyrimidine,enzymes.
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How to cite this article:

Husain F. Hassan. 2016. Enzymes of the De novo Pyrimidine Biosynthetic Pathway in Leishmania tropica.Int.J.Curr.Res.Aca.Rev. 4(4): 185-192
doi: http://dx.doi.org/10.20546/ijcrar.2016.404.023