Buschiazzo Alejandro, Alzari Pedro M
Département de Biologie Structurale & Chimie, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris, France.
Curr Opin Chem Biol. 2008 Oct;12(5):565-72. doi: 10.1016/j.cbpa.2008.06.017.
Sialic acids are a diverse family of negatively charged sugars that play essential biological roles. Their presence and relative abundance in different cells is ultimately regulated by the concerted action of a large set of enzymes. In this review, we focus on the most recent advances on the enzymes that govern sialic acid metabolism, with emphasis on structural work. Major progress has been made in dissecting the catalytic mechanism of sialidases, revealing a modified scenario of the typical glycosidase ping-pong mechanism. Similarly, X-ray structures of sialyltransferases uncover significant variations of formerly known glycosyltransferase foldings. Both sialidases and sialyltransferases seem to tell us that sialic acid-handling enzymes have evolved important modifications related to the distinctive features of sialic acid itself.
唾液酸是一类多样的带负电荷的糖类,发挥着重要的生物学作用。它们在不同细胞中的存在及相对丰度最终由一大组酶的协同作用来调控。在本综述中,我们聚焦于调控唾液酸代谢的酶的最新进展,重点是结构研究工作。在剖析唾液酸酶的催化机制方面已取得重大进展,揭示了典型糖苷酶乒乓机制的一种修正情形。同样,唾液酸转移酶的X射线结构揭示了此前已知的糖基转移酶折叠的显著差异。唾液酸酶和唾液酸转移酶似乎都在告诉我们,处理唾液酸的酶已经进化出与唾液酸自身独特特征相关的重要修饰。