| Abstract: | Adaptation to environmental temperature is examined in beef heart, beef muscle, and flounder muscle lactate dehydrogenases (EC 1.1.1.27). Low temperature adaptation in the ectothermic (flounder) enzyme is indicated by a reduced enthalpy of activation for kcat (enzyme turnover number, s-1) and increased catalytic efficiency. Also, the reaction rate at low substrate concentrations has a maximum at a lower temperature than in the endothermic enzymes. This is a result of altered bonding in the enzyme-substrate complexes. Adaptation to higher temperatures in the endothermic (beef) enzymes is suggested by a decreased sensitivity to heat denaturation, especially in the presence of substrates. A direct correlation is found between the degree of bonding in the enzyme-substrate complexes and the decrease in rate of heat denaturation caused by addition of substrates. |
