Genetic analysis of adenine metabolism in Leishmania donovani promastigotes. Evidence for diploidy at the adenine phosphoribosyltransferase locus.
نویسندگان
چکیده
منابع مشابه
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...
متن کاملSubcellular 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...
متن کاملCloning and characterization of Leishmania tarentolae adenine phosphoribosyltransferase.
a Department of Molecular, Cell and De6elopmental Biology, Howard Hughes Medical Institute, UCLA School of Medicine, UCLA, Los Angeles, CA 90095-1662, USA b Howard Hughes Medical Institute, UCLA School of Medicine, UCLA, Los Angeles, CA 90095-1662, USA c Department of Medical Microbiology, Immunology and Molecular Genetics, Howard Hughes Medical Institute, UCLA School of Medicine, UCLA, Los Ang...
متن کاملAdenine phosphoribosyltransferase deficiency
Key-words Disease name and synonyms Definition Excluded diseases Diagnosis criteria Differential diagnosis Prevalence Molecular defect Clinical description Management including treatment Etiology Diagnostic methods Antenatal diagnosis Unresolved questions References Abstract Adenine phosphoribosyltransferase (APRT) catalyzes the synthesis of AMP (adenosine monophosphate) from adenine and 5'-pho...
متن کاملHuman Adenine Phosphoribosyltransferase
Human adenine phosphoribosyltransferase has been purified 33,000-fold from erythrocytes to a specific activity of 9.58 pmoles of AMP formed per mg of protein per min. The native enzyme has a molecular weight of 34,000 and is composed of three subunits of equal molecular weight which appear to be associated by noncovalent forces. The highly purified enzyme is maximally active over a broad pH ran...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1984
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)42646-9