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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
Email : editorijcret@gmail.com

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

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
Copyright: This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike license.