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Acetaldehyde-derived modifications on cytosolic human carbonic anhydrases

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Details

Original languageEnglish
Pages (from-to)862-870
Number of pages9
JournalJOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
Volume26
Issue number6
DOIs
Publication statusPublished - Dec 2011
Publication typeA1 Journal article-refereed

Abstract

Acetaldehyde can generate modifications in several proteins, such as carbonic anhydrase (CA) II. In this study, we extended in vitro investigations on acetaldehyde adduct formation by focusing on the other human cytosolic CA enzymes I, III, VII, and XIII. High-resolution mass spectrometric analysis indicated that acetaldehyde most efficiently formed covalent adducts with CA II and XIII. The binding of up to 19 acetaldehydes in CA II is probably attributable to the high number of lysine residues (n=24) located mainly on the surface of the enzyme molecule. CA XIII formed more adducts (up to 25) than it contains lysine residues (n=16) in its primary structure. Acetaldehyde treatment induced only minor changes in CA catalytic activity in most cases. The present study provides the first evidence that acetaldehyde can bind to several cytosolic CA isozymes. The functional consequences of such modifications will be further investigated in vivo by using animal models.

ASJC Scopus subject areas

Keywords

  • Acetaldehyde, Adduct, Alcohol, Mass spectrometry, Modification