A comparison of lactate dehydrogenase from an ectothermic and an endothermic animal.
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.
D000222:Adaptation, Physiological; D000818:Animals; D002417:Cattle / Q000378:metabolism*; D004789:Enzyme Activation; D005399:Fishes / Q000378:metabolism*; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D009132:Muscles / Q000201:enzymology*; D011485:Protein Binding; D013045:Species Specificity; D013696:Temperature; D013816:Thermodynamics
D007770:L-Lactate Dehydrogenase