Correlative variations of the free energies for enzyme-substrate complex formation and the transition-state stabilization for RNases
| Autor: | Gennady I. Yakovlev, Bocharov Al, G. P. Moiseyev |
|---|---|
| Rok vydání: | 1984 |
| Předmět: |
RNase P
Biophysics Transition state Biology Biochemistry Ribonucleases Structural Biology Genetics RNase Nucleotide Enzyme kinetics skin and connective tissue diseases Molecular Biology Enzyme substrate complex chemistry.chemical_classification Transition (genetics) Strain (chemistry) Ribonuclease Pancreatic Cell Biology Kinetics Crystallography chemistry Enzyme-substrate complex Thermodynamics Free energies sense organs Protein Binding |
| Zdroj: | FEBS Letters. 175:356-358 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(84)80767-x |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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