Studies on Human Serum 5′ -Deoxy-5′ -Methylthioadenosine Phosphorylase: Molecular Properties and Clinical Perspectives
5′ -Deoxy-5′ -methylthioadenosine phosphorylase (MTAase) is the only enzyme responsible in eukaryotes for the removal of MTA, a natural sulfur nucleoside produced from S-adenosylmethionine (AdoMet) through several routes1, 2. The enzyme catalyzes the phosphorolytic breakdown of the N-C glycosidic bond of the thioether leading to adenine and 5-methylthioribose-1-phosphate (MTR-1-P)3, 4. The carbon skeleton of phosphorylated sugar (except C-1) is then recycled to methionine5 and the purine base is converted to adenosine 5 ′-monophosphate by adenine phosphoribosyltransferase1: MTAase, therefore, plays a key role in the control of both purine and amino acid pools.
KeywordsAcute Hepatitis Assay Mixture Amino Acid Pool Phosphorylase Activity Adenine Phosphoribosyltransferase1
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- 1.F. Della Ragione, M. Cartení-Farina and V. Zappia, 5′-Deoxy-5′-me-thylthioadenosine: novel metabolic and physiological aspects, in: “The Physiology of Polyamines, ” U. Bachrach and Y.M. Heimer eds, CRC Press, Boca Raton, in press.Google Scholar
- 17.F. Della Ragione, A. Oliva, M. Fioretti, G.L. Russo, R. Palximbo and V. Zappia, Physico-chemical and imnunological properties of bovine liver 5′-deoxy-5′-methylthioadenosine phosphorylase, in this book. Google Scholar