Deacetylation of N-acetylhexosamine residues in structural polysaccharides and glycoconjugates is catalyzed by different families of carbohydrate esterases that, despite different structural folds, share a common metal-assisted acid/base mechanism with the metal cation coordinated with a conserved Asp-His-His triad. These enzymes serve diverse biological functions in the modification of cell-surface polysaccharides in bacteria and fungi as well as in the metabolism of hexosamines in the biosynthesis of cellular glycoconjugates. Focusing on carbohydrate de-N-acetylases, this article summarizes the background of the different families from a structural and functional viewpoint and covers advances in the characterization of novel enzymes over the last 2–3 years. Current research is addressed to the identification of new deacetylases and unravel their biological functions as they are candidate targets for the design of antimicrobials against pathogenic bacteria and fungi. Likewise, some families are also used as biocatalysts for the production of defined glycostructures with diverse applications.

结构多糖和糖缀合物中N-乙酰己糖胺残基的脱乙酰化由不同家族的碳水化合物酯酶催化，尽管结构折叠不同，但具有共同的金属辅助酸/碱机制，金属阳离子与保守的 Asp-His-His 三联体配位. 这些酶在细菌和真菌中细胞表面多糖的修饰以及细胞糖缀合物生物合成中己糖胺的代谢中发挥着多种生物学功能。专注于碳水化合物去氮-乙酰酶，这篇文章从结构和功能的角度总结了不同家族的背景，并涵盖了过去 2-3 年新酶表征方面的进展。目前的研究是针对新的脱乙酰酶的鉴定并阐明它们的生物学功能，因为它们是设计针对病原细菌和真菌的抗菌剂的候选靶标。同样，一些家族也被用作生物催化剂，用于生产具有多种应用的特定糖结构。