[Family of AMP-deaminase genes]

Abstract

AMP-deaminase (AMP-aminohydrolase, EC 3.5.4.6), a highly regulated oligomeric enzyme catalyzing the irreversible deamination of adenylic acid (5'-AMP), is located at a branch point of adenylate nucleotide catabolism. It plays an important role in the stabilization of adenylate energy charge (AEC) and the regulation of the purine nucleotide pool in several types of animal tissue. Tissue- and stage-specific isoforms of AMP-deaminase were described in mammals. In humans, three isozymes of AMP-deaminase, i.e. M (muscle), L (liver), and E (erythrocyte), exhibiting different physical, catalytic, and regulatory properties, were identified. AMP-deaminase activity is encoded by a multigene family in which two genes produce at least three mRNAs through alternative splicing of one of the primary transcripts. In this study we present all found and so far unpublished detailed knowledge about AMP-deaminase gene structures. We also present basic information on the effects of these gene mutations.