Monti Eugenio, Miyagi Taeko
Faculty of Medicine, Department of Biomedical Sciences and Biotechnology, University of Brescia, Brescia, Viale Europa 11, 25123, Brescia, Italy.
Top Curr Chem. 2015;366:183-208. doi: 10.1007/128_2012_328.
The removal of sialic acids, catalyzed by sialidase, is the initial step in degradation of oligosaccharides, glycoproteins, and glycolipids. The catalytic reaction may greatly influence biological processes through changing the conformation of glycoproteins and create or mask binding sites of functional molecules. Recent progress in sialidase research has clarified that mammalian sialidases indeed contribute to the regulation of various cellular functions as well as lysosomal catabolism, unlike the sialidases of microbial origin that probably play roles limited to nutrition and pathogenesis. However, the mammalian enzymes contain consensus sequences in the six-blade β-propeller structural organization typical of microbial sialidases, despite the low degree of similarity to the amino acid sequences of the microbial enzymes. The present review briefly summarizes structural and functional features of mammalian sialidases.
唾液酸酶催化的唾液酸去除是寡糖、糖蛋白和糖脂降解的第一步。催化反应可能通过改变糖蛋白的构象极大地影响生物过程，并产生或掩盖功能分子的结合位点。唾液酸酶研究的最新进展表明，与可能仅在营养和发病机制中起作用的微生物来源的唾液酸酶不同，哺乳动物唾液酸酶确实有助于调节各种细胞功能以及溶酶体分解代谢。然而，尽管与微生物酶的氨基酸序列相似度较低，但哺乳动物酶在微生物唾液酸酶典型的六叶β-螺旋桨结构组织中含有共有序列。本综述简要总结了哺乳动物唾液酸酶的结构和功能特征。
