Steady-state kinetic study of action of ribonuclease A, involving a conformational change between 30 and 40 degrees C.
The steady-state kinetics of the reaction of ribonuclease A with cyclic cytidine 2',3'-phosphate as substrate are investigated as a function of temperature at pH 5 and ionic strength 0.1 M. The results suggest, but cannot prove, that a conformational change near 32 degrees C is involved in the rate-limiting step of the reaction mechanism. This conformational change is proposed to be the same one that was observed in studies of the free enzyme and of enzyme-inhibitor complexes near the same temperature.
D000818:Animals; D002417:Cattle; D004720:Endonucleases / Q000378:metabolism*; D007700:Kinetics; D010179:Pancreas / Q000201:enzymology; D011487:Protein Conformation; D012260:Ribonucleases / Q000378:metabolism*; D013696:Temperature
D004720:Endonucleases; D012260:Ribonucleases