Abstract
Adenine phosphoribosyltransferase (APRT) catalyzes the magnesium dependent conversion of adenine to adenosine 5’-monophosphate (AMP) utilizing the high energy compound, 5-phosphoribosyl-lpyrophosphate (PP-ribose-P) as a cosubstrate. In humans this enzyme provides the only apparent pathway for conversion of dietary adenine into utilizable nucleotides. The finding of elevated levels of APRT activity in patients with the Lesch-Nyhan syndrome (Seegmiller, Rosenbloom and Kelley, 1967; Kelley, 1968) and the discovery of at least three families with a genetically determined partial deficiency of APRI activity in circulating erythrocytes (Kelley, et al., 1968; Kelley, Fox and Wyngaarden, 1970; Emmerson, et al., present symposium) stimulated our study of a highly purified preparation of human adenine phosphoribosyltransferase.
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