Die Alkoholdehydrogenase Ihre Wirkungsweisen und Komplexverbindungen

Summary Liver alcohol dehydrogenase (LADH) is one of the most intensely studied of all enzymes because it is easily available in crystalline form and has many properties which are favourable for experimentation. Its mode of action has been elucidated to some extent mainly by kinetic experiments with and without inhibitors.Its substrate specificity is very low, since the enzyme attacks a great variety of primary and secondary alcohols, or reversibly aldehydes and ketones. Its main physiological function is still unknown, but may be found by the aid of pyrazole which acts as a specific inhibitor in vivo.Complexes of the enzyme with coenzyme, or coenzyme + inhibitors have been crystallized and are presently being studied by X-ray crystallography in the hope of determining the three-dimensional structure of the molecule. The formation of the ternary complexes leads to a profound change of conformation (monoclinic instead ofortho-rhombic crystals). Simultaneously the optical rotatory dispersion is drastically changed.

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Paul-Karrer-Vorlesung, gehalten am 30. Juni 1965, an der Universität Zürich (Schweiz).