Adenine Aminohydrolase from Leishmania donovani

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Crystal structures of adenine phosphoribosyltransferase from Leishmania donovani.

The enzyme adenine phosphoribosyltransferase (APRT) functions to salvage adenine by converting it to adenosine-5-monophosphate (AMP). APRT deficiency in humans is a well characterized inborn error of metabolism, and APRT may contribute to the indispensable nutritional role of purine salvage in protozoan parasites, all of which lack de novo purine biosynthesis. We determined crystal structures f...

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Subcellular localization of adenine and xanthine phosphoribosyltransferases in Leishmania donovani.

The subcellular location of a protein is a critical factor in its physiological function and an important consideration in therapeutic paradigms that target the protein. Because Leishmania donovani cannot synthesize purine nucleotides de novo, they rely predominantly upon therapeutically germane phosphoribosyltransferase (PRT) enzymes, hypoxanthine-guanine PRT (HGPRT), adenine PRT (APRT), and x...

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Aspartate Transcarbamylase from Leishmania donovani

Leishmania donovani is a protozoal pathogen that belongs to the kinetoplastida order. Unlike in other eucaryotic systems, the first three enzymes of the de novo pyrimidine biosynthetic pathway are not components of a multifunctional protein system. The three enzyme activities in the crude extract were separated on a Sephacryl S-200 column. Aspartate carbamoyltransferase (EC 2.1.3.2) has been pu...

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Adenine aminohydrolase. An investigation of specificity.

In addition to their action upon adenine, the adenine aminohydrolases of Azofobacfer vinelandii and of Candida ufilis have been found capable of acting upon 6-chloropurine, 6-iodopurine, 6-hydrazinopurine, 2-amino-6-chloropurine, 2,6-diaminopurine, and 7-aminothiazolo[5,4-dlpyrimidine. In each case the enzyme catalyzes the replacement by a hydroxyl group of the substituent on position 6 or on t...

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Glycobiology of Leishmania donovani.

Leishmania donovani, the causative organism of visceral leishmaniasis (VL) is one of the deadliest of the entire known Leishmania species. This protozoan parasite displays immense adaptability to survive under extremely harsh conditions. Cell surface glycoconjugates play a pivotal role in parasite virulence and infectivity. This review mainly highlights on the importance of these molecules and ...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 2012

ISSN: 0021-9258

DOI: 10.1074/jbc.m111.307884