Kinetic studies of yeast alcohol dehydrogenase with NAD+ and ethanol, hexanol or decanol as substrates invariably result in non-linear Lineweaver-Burk plots if the alcohol is the variable substrate. The kinetic coefficients determined from secondary plots are consistent with an ‘equilibrium random-order‘ mechanism for extremely low alcohol concentrations and for all alcohols, the transformation of the ternary complexes being the rate-limiting step of the reaction. This mechanism also applies to long-chain substrates at high concentrations, whereas the rate of the ethanol-NAD+ reaction at high ethanol concentrations is determined by the dissociation of the enzyme-NADH complex. The dissociation constants for the enzyme-NAD+ complex and for the enzyme-alcohol complexes obtained from the kinetic quotients satisfactorily correspond to the dissociation constants obtained by use of other techniques. It is suggested that the non-linear curves may be attributed to a structural change in the enzyme itself, caused by the alcohol.
Research Article|July 01 1976
Kinetics and reaction mechanism of yeast alcohol dehydrogenase with long-chain primary alcohols
Biochem J (1976) 157 (1): 15-22.
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W Schöpp, H Aurich; Kinetics and reaction mechanism of yeast alcohol dehydrogenase with long-chain primary alcohols. Biochem J 1 July 1976; 157 (1): 15–22. doi: https://doi.org/10.1042/bj1570015
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