Open AccessComparison of the chemical mechanisms of action of yeast and equine liver alcohol dehydrogenase
Author(s) -
Leskovac Vladimir,
Trivić Svetlana,
Anderson Bruce M.
Publication year - 1999
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1327.1999.00675.x
Subject(s) - enzyme , yeast , cofactor , alcohol dehydrogenase , chemistry , mechanism of action , biochemistry , stereochemistry , liver enzyme , biology , in vitro , endocrinology
The pH‐dependence of the steady‐state kinetic parameters and the ligand‐binding parameters for competitive dead‐end inhibitors for the yeast alcohol dehydrogenase ( EC 1.1.1.1 , constitutive, cytoplasmic) reaction was studied in the pH range 6–10. These studies were designed in order to assign the appropriate p K a values to all dissociation forms of enzyme in the chemical mechanism of action for the yeast enzyme, previously proposed by Cook and Cleland [P. F. Cook & W. W. Cleland (1981) Biochemistry 20, 1796–1816]. In addition, the chemical mechanism of action for the yeast enzyme, proposed in this work, was compared with a similar mechanism of action for the horse liver enzyme, proposed by Cook and Cleland. Substantial differences were found, especially in the binding of coenzymes and in the structure of enzyme–coenzyme complexes.