Further studies on the adaptation of fish myofibrillar ATPases to different cell temperatures.
Previous studies on fish Mg2+Ca2+ activated myofibrillar ATPases have been extended to species inhabiting diverse thermal environments. Cold adapted ATPases have considerably higher catalytic centred activities at low temperatures than warm adapted ATPases. Differences in cell temperature have also lead to evolutionary modifications in thermodynamic activation parameters. The free energies (deltaG2+), enthalpies (deltaH2+) and entropies (deltaS2+) of activation of the Mg2+Ca2+ myofibrillar ATPase are positively correlated with adaptation temperature. Myofibrils with CaATP-2 as substrate in the absence of Mg2+ will hydrolyse ATP by a mechanism not associated with fibril shortening. Differences in activation enthalpies (deltaHH) between cold and warm adapted Ca2+-activated myofibrillar ATPases are less pronounced than for the physiological ATPase. Furthermore the Ca2+-activated ATPase showed no relationship between environmental temperature and substrate turnover number or free energy of activation (deltaG2+).
D000064:Acclimatization; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D002118:Calcium / Q000378:metabolism; D002384:Catalysis; D003080:Cold Temperature; D005399:Fishes / Q000502:physiology*; D008274:Magnesium / Q000494:pharmacology; D009210:Myofibrils / Q000201:enzymology*; D013816:Thermodynamics
D000251:Adenosine Triphosphatases; D008274:Magnesium; D002118:Calcium