α-甘露糖苷酶研究进展

Advance in α-mannosidase

α-甘露糖苷酶多具有糖苷水解酶38、47家族保守序列,目前已测序的α-甘露糖苷酶基因序列超过2000多种,根据α-甘露糖苷酶基因保守序列可将其分为三类,即Ⅰ类α-甘露糖苷酶、Ⅱ类α-甘露糖苷酶和未分类α-甘露糖苷酶。α-甘露糖苷酶主要参与蛋白质糖基化修饰和糖蛋白聚糖水解修饰。其代谢异常可以引起多种疾病,目前研究较多的是由α-甘露糖苷酶功能障碍引起的先天性红细胞生成异常性贫血Ⅱ型和α-甘露糖苷贮积症。论文主要对α-甘露糖苷酶的分类及其在糖基化过程中的作用,以及与之有关的疾病进行介绍,以期为苦马豆素毒性作用机制研究提供理论参考。

There are more than 2 000 sequenced gene sequences of α-mannosidases,most of which belong to glycosylhydrolase families 47 and 38.Based on the conserved sequence,α-mannosidases can be devided into 3 groups： α-mannosidases Ⅰ,α-mannosidases Ⅱ,and unclassified α-mannosidases.α-mannosidases mainly take part in two actions： glycosylation modification of proteins and proteoglycan hydrolysis modification of glycoprotein.The abnormal metabolism of α-mannosidases can cause many diseases,like congenital dyserythropoietic anemia type Ⅱ and α-mannosidosis.This review focused on the classification of this enzyme,its function on glycosylation processing of protein and the relative disease resulted from its mutation,in order to provide certain theory reference for the study on SW.