MULTIPLICITY OF N-TERMINAL STRUCTURES OF MEDIUM-CHAIN ALCOHOL DEHYDROGENASES - MASS-SPECTROMETRIC ANALYSIS OF PLANT, LOWER VERTEBRATE AND HIGHER VERTEBRATE CLASS-I, CLASS-II, AND CLASS-III FORMS OF THE ENZYME

Ten different alcohol dehydrogenases, representing several classes of the enzyme and a wide spread of organisms, were analyzed for patterns of N-terminal structures utilizing a combination of conventional and m ass spectrometric peptide analysis, Results show all forms to be N-ter minally acetylated and allow comparisons of now 40 such alcohol dehydr ogenases covering a large span of forms and origins, Patterns illustra te roles of acetylation in proteins in general, define special importa nce of the class I N-terminal acetylation, and distinguish separate ac etylated structures for all classes, as well as a common alcohol dehyd rogenase motif.