Abstract
In this chapter the AMP-deaminase activity in hearts of different species is compared with that in skeletal muscle. Some features of the well-characterized skeletal muscle enzyme, like binding to myosin filaments and deficiencies in humans, are described. Experimental models to study the role of cardiac AMP-deaminase, i.e., isolated enzyme, cardiomyocytes and isolated perfused heart, are discussed. Substrate saturation kinetics and regulatory effects of nucleotides, phosphate, and activated fatty acids are summarized; their significance for in vivo regulation considered. In addition the behavior of AMP-deaminase under various adenylate energy charges and its implications for the regulation of enzyme in ischemic tissue is examined. Myocardial AMP-deaminase is shown to be a tissue-specific isoenzyme, with different kinetic and regulatory forms. Developmental changes of AMP-deaminase and other enzymes of adenylate metabolism enzymes in myocardial cells are reviewed. The flux through the pathway catalyzed by AMP-deaminase in normoxic and ischemic heart is analyzed. A probable function of the reaction - preservation of purine nucleotides inside the myocardial cell - is proposed.
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Skladanowski, A.C. (1988). On the Role of Myocardial AMP-Deaminase. In: De Jong, J.W. (eds) Myocardial Energy Metabolism. Developments in Cardiovascular Medicine, vol 91. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-1319-6_6
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DOI: https://doi.org/10.1007/978-94-009-1319-6_6
Publisher Name: Springer, Dordrecht
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