Hydration of vinyl ether groups by unsaturated glycoside hydrolases and their role in bacterial pathogenesis.
Hydration of vinyl ether groups by unsaturated glycoside hydrolases and their role in bacterial pathogenesis.
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发表时间：
2007-12
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通讯作者：
W. Hashimoto;T. Itoh;Y. Maruyama;B. Mikami;K. Murata
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作者：
W. Hashimoto;T. Itoh;Y. Maruyama;B. Mikami;K. Murata
许多病原微生物通过产生多糖降解酶（裂合酶和水解酶）侵入哺乳动物和/或植物细胞。构成细胞表面基质一部分的哺乳动物糖胺聚糖和植物果胶是这些微生物酶的典型目标。不饱和糖苷水解酶催化寡糖中不饱和糖醛酸的水解释放，寡糖是通过基质降解多糖裂合酶的反应产生的。这种酶促能力表明不饱和糖苷水解酶在微生物感染中充当毒力因子。本综述重点关注这些酶的分子鉴定、细菌分布和结构/功能关系。与催化机制涉及异头构型的保留或反转的一般糖苷水解酶相反，不饱和糖苷水解酶独特地触发不饱和糖中乙烯基醚基团的水解，但不触发其糖苷键的水解。
Many pathogenic microorganisms invade mammalian and/or plant cells by producing polysaccharide-degrading enzymes (lyases and hydrolases). Mammalian glycosaminoglycans and plant pectins that form part of the cell surface matrix are typical targets for these microbial enzymes. Unsaturated glycoside hydrolase catalyzes the hydrolytic release of an unsaturated uronic acid from oligosaccharides, which are produced through the reaction of matrix-degrading polysaccharide lyase. This enzymatic ability suggests that unsaturated glycoside hydrolases function as virulence factors in microbial infection. This review focuses on the molecular identification, bacterial distribution, and structure/function relationships of these enzymes. In contrast to general glycoside hydrolases, in which the catalytic mechanism involves the retention or inversion of an anomeric configuration, unsaturated glycoside hydrolases uniquely trigger the hydrolysis of vinyl ether groups in unsaturated saccharides but not of their glycosidic bonds.