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2016•International Journal of Current Research and Academic ReviewOpen access

Enzymes of the De novo Pyrimidine Biosynthetic Pathway in Leishmania tropica

Husain F. Hassan

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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.

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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.

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Available 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.

Key concepts: Aspartate carbamoyltransferase, Pyrimidine metabolism, Dihydroorotate dehydrogenase, Biochemistry, Enzyme, Chemistry, Phosphoribosyltransferase, Amastigote

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