Abstract
This chapter discusses the ligand binding properties and subunit interactions in yeast alcohol dehydrogenase. The research work on the molecular structure and the mechanism of action of yeast alcohol dehydrogenase so far has suffered in the first place from the lack of pure and homogeneous enzyme preparations readily available to investigators. Various commercial and labortory-obtained enzyme preparations have displayed variable properties with respect to their specific activity, zinc content, coenzyme binding capacity, reactivity of -SH groups and other properties, indicating that laboratories have been working with enzyme preparations of different purities and in different states of nativeness. The experimental results indicate that the molecule of yeast alcohol dehydrogenase has an assymetric quaternary structure; they are consistent with an enzyme model in which the four monomeric subunits are arranged in two mutually symmetrical pairs. Such a tetrameric protein molecule could be described as a dimer of dimers with a structure (αα)2. The precise nature and extent of assymetry in such a model remains to be established.
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