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Correlative variations of the free energies for enzyme‐substrate complex formation and the transition‐state stabilization for RNases
Author(s) -
Yakovlev Gennady I.,
Bocharov Alexander L.,
Moiseyev Gennady P.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80767-x
Subject(s) - substrate (aquarium) , enzyme kinetics , enzyme , nucleotide , transition (genetics) , chemistry , biophysics , stereochemistry , crystallography , biochemistry , biology , active site , ecology , gene
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 k cat / K m . This was considered to be a consequence of the strain in the enzyme‐substrate complex.