Correlative variations of the free energies for enzyme-substrate complex formation and the transition-state stabilization for RNases.
It was found for RNases of different specificities that changes in the free energy for substrate-enzyme binding induced by variations in the nucleotide base structure are accompanied by proportional changes in kcat/Km. This was considered to be a consequence of the strain in the enzyme-substrate complex.
D007700:Kinetics; D011485:Protein Binding; D012259:Ribonuclease, Pancreatic / Q000378:metabolism; D012260:Ribonucleases / Q000378:metabolism*; D013816:Thermodynamics
D012260:Ribonucleases; D012259:Ribonuclease, Pancreatic