Factors limiting adenosine triphosphatase function during high intensity exercise. Thermodynamic and regulatory considerations

Sports Medicine
P Korge

Abstract

It is widely accepted that a structural organisation favouring interaction between functionally-related enzymes is required for the economy and efficiency of metabolic reactions. Many functionally-related enzymes have been shown to be reversibly bound to cellular structures and to other enzymes at the sites where they are required. Resulting from this binding, close structural proximity and concentration of enzymes, a microenvironment is generated where the product of one enzyme is the substrate of the other. This reduces the diffusion distance for the substrate, saturates binding sites with maximal speed and, as a final outcome, increases the efficiency and economy of function behind these metabolic reactions. Available data indicate that the above-described association between adenosine triphosphatase (ATPase) and enzymes regenerating ATP has an important role in the regulation of ATPase function. A general consensus exists among published studies that the concentration of ATP ([ATP]) is not significantly decreased in fatigued muscle, even in those with severely diminished power output. However, in studies with isolated perfused hearts it has been possible to significantly reduce [ATP] in muscle cells without compromising mec...Continue Reading

Citations

Jun 17, 2004·Canadian Journal of Applied Physiology = Revue Canadienne De Physiologie Appliquée·A Russell Tupling
Aug 18, 2001·Sports Medicine·A St Clair GibsonT D Noakes
Apr 5, 2012·Canadian Journal of Physiology and Pharmacology·Howard J GreenSusan Tupling
May 13, 1998·Acta Physiologica Scandinavica·K SahlinK Söderlund
Nov 4, 2017·Journal of Animal Physiology and Animal Nutrition·Z-P LvY-M Guo
May 10, 2007·American Journal of Physiology. Endocrinology and Metabolism·H J GreenA R Tupling
Feb 4, 2003·The Journal of Biological Chemistry·Edwin JanssenBé Wieringa

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