Multiplicity of N‐terminal structures of medium‐chain alcohol dehydrogenases Mass‐spectrometric analysis of plant, lower vertebrate and higher vertebrate class I, II, and III forms of the enzyme

3 July 1995

journal article
research article
Published by Wiley in FEBS Letters

Vol. 367 (3) , 237-240
https://doi.org/10.1016/0014-5793(95)00572-q

Abstract

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 mass spectrometric peptide analysis. Results show all forms to be N‐terminally acetylated and allow comparisons of now 40 such alcohol dehydrogenases covering a large span of forms and origins. Patterns illustrate roles of acetylation in proteins in general, define special importance of the class I N‐terminal acetylation, and distinguish separate acetylated structures for all classes, as well as a common alcohol dehydrogenase motif.

Keywords

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