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Application of linear free energy relationships to the serpin–proteinase inhibition mechanism
Author(s) -
Nash Piers,
McFadden Grant,
Whitty Adrian
Publication year - 2000
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/s0014-5793(00)01620-3
Subject(s) - serpin , chemistry , reaction rate constant , folding (dsp implementation) , covalent bond , serine , protein folding , serine proteinase inhibitors , free energy relationship , equilibrium constant , constant (computer programming) , kinetics , biophysics , enzyme , biochemistry , serine protease , biology , protease , organic chemistry , physics , programming language , quantum mechanics , computer science , electrical engineering , gene , engineering
Linear free energy relationships can be used to link the changes in rate constant for a reaction to changes in the equilibrium caused by alterations in structure. While they have most often been used in the analysis of chemical reactions, they have also been employed to resolve questions in enzymology and protein folding. Here we analyze the reaction of a serpin with a panel of six serine proteinases, and observe that a linear free energy relationship exists between the true second‐order rate constant for reaction, k inh , and the inhibition constant, K I , indicating that formation of the covalent serpin–enzyme complex may be reversible.