A novel α1,2-L-fucosidase acting on xyloglucan oligosaccharides is associated with endo-β-mannosidase
A novel α1,2-L-fucosidase acting on xyloglucan oligosaccharides is associated with endo-β-mannosidase
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DOI：
10.1093/jb/mvm186
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发表时间：
2007-12-01
影响因子：
2.7
通讯作者：
Hase, Sumihiro
中科院分区：
文献类型：
--
作者：
Ishimizu, Takeshi;Hashimoto, Chikako;Hase, Sumihiro
在植物中发现了内切-β-甘露糖苷酶，其以内切方式水解N-聚糖的Man β 1-4GlcNAc键。在从百合花中纯化该酶的过程中，我们发现了该酶的高分子量形式（命名为EBM II）。EBM II通过柱层析纯化至均一，其分子组成显示EBM H由内切β-甘露糖苷酶和相关蛋白组成。该相关蛋白的cDNA编码与双歧杆菌A&A的岩藻糖苷酶结构域具有轻微同源性的蛋白。EBM II具有α 1，2-L-岩藻糖苷酶活性并作用于岩藻糖基化木葡聚糖九糖。该相关蛋白的氨基酸序列与已知的植物α-L-岩藻糖苷酶没有相似性。这些结果表明EBM II是一种新的α 1，2-L，-岩藻糖苷酶和含有内切-β-甘露糖苷酶的蛋白质复合物。
Endo-p-mannosidase, which hydrolyses the Man beta 1-4GlcNAc linkage of N-glycans in an endo-manner, was discovered in plants. During the course of the purification of the enzyme from lily flowers, we found a higher molecular mass form of the enzyme (designated as EBM II). EBM II was purified by column chromatography to homogeneity and its molecular composition revealed EBM H to be comprised of endo-p-mannosidase and an associated protein. The cDNA of this associated protein encodes a protein with slight homology to the fucosidase domain of bifidus A&A. EBM II has alpha 1,2-L-fucosidase activity and acts on a fucosylated xyloglucan nonasaccharide. The amino acid sequence of this associated protein has no similarity to known plant alpha-L-fucosidases. These results show that EBM II is a novel alpha 1,2-L,-fucosidase and a protein complex containing endo-beta-mannosidase.