Open AccessKinetics and Dissociation Constants of Liver Alcohol Dehydrogenase with 3‐Acetyl Pyridine NAD + and NADH
Author(s) -
Shore J. D.,
Theorell H.
Publication year - 1967
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1967.tb00101.x
Subject(s) - nad+ kinase , pyridine , alcohol dehydrogenase , chemistry , dissociation constant , stereochemistry , dissociation (chemistry) , alcohol , enzyme , cofactor , amide , medicinal chemistry , biochemistry , organic chemistry , receptor
Binary complex dissociation constants and kinetic φ values of liver alcohol dehydrogenase were determined for 3‐acetyl pyridine NAD + and NADH. The reduced analog was bound 24 times less tightly than NADH to liver alcohol dehydrogenase whereas no significant difference was found between the binding of 3‐acetyl pyridine NAD + and NAD + to liver alcohol dehydrogenate. The rates of interaction of substrates with binary complexes were one tenth as fast when the acetyl pyridine analogs were used. These results were interpreted with reference to the significance of the pyridine ring amide group in binding, and the interaction of binary complexes with substrates.