Molecular characterization of tomato α1,3/4-fucosidase, a member of glycosyl hydrolase family 29, involved in degradation of plant complex type N-glycans.
Molecular characterization of tomato α1,3/4-fucosidase, a member of glycosyl hydrolase family 29, involved in degradation of plant complex type N-glycans.
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番茄 α1,3/4-岩藻糖苷酶（糖基水解酶家族 29 的成员）的分子特征，参与植物复合型 N-聚糖的降解。
DOI：
10.1093/jb/mvw089
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发表时间：
2017
期刊：
影响因子：
--
通讯作者：
Y.
中科院分区：
文献类型：
--
作者：
Rahman;M.D.;Maeda;M.;Itano;S.;Hossain;M.A.;Ishimizu;T.;Kimura;Y.
在这项研究中，我们在番茄中发现了一个编码酸性α-聚焦酶（LOC101254568orSolyc03g006980， α-聚焦酶S1-1）的基因，该基因可能参与植物复合物型聚糖的转换。利用杆状病毒-昆虫细胞表达系统表达重组α-Fuc酶S1-1 （rFuc酶S1-1）。rFuc酶Sl-1的大小为55 kDa，其最佳pH值约为4.5。它能水解LNFP III上的非还原末端α1,3-聚焦残基和植物复合体型聚糖上的lea表位α1,4-聚焦残基，但不能水解LNFP I上的α1,2-聚焦残基或吡啶层合fuc上的α1,3-聚焦残基。此外，我们发现该番茄α-Fuc '酶S1-1对植物复合体型聚糖的核心五寡糖单元[Manβ1-4(Xylβ1-2)GlcNAcβ1-4(Fucα1-3)GlcNAc-PA]无活性。长双歧杆菌α-聚焦酶Sl-1的分子三维建模及结构/序列分析infantis（Blon_2336）指出，残基asp193和glu237可能对底物结合很重要。
In this study, we identified a gene in tomato that encodes an acidic α-fucosidase (LOC101254568orSolyc03g006980, α-Fuc’ase S1-1), which may be involved in the turnover of plant complex-typeN-glycans. Recombinant α-Fuc’ase S1-1 (rFuc’ase S1-1) was expressed using a baculovirus–insect cell expression system. rFuc’ase Sl-1 is 55 kDa in size and has an optimum pH around 4.5. It substantially hydrolyzed the non-reducing terminal α1,3-fucose residue on LNFP III and α1,4-fucose residues of Leaepitopes on plant complex-typeN-glycans, but not the α1,2-fucose residue on LNFP I or the α1,3-fucose residue on pyridylaminated Fucα1-3GlcNAc. Furthermore, we found that this tomato α-Fuc’ase S1-1 was inactive toward the core penta-oligosaccharide unit [Manβ1-4(Xylβ1-2)GlcNAcβ1-4(Fucα1-3)GlcNAc-PA] of plant complex-typeN-glycans. Molecular 3D modelling of α-Fuc’ase Sl-1 and structure/sequence interpretation based on comparison with a homologous α-fucosidase fromBifidobacterium longumsubsp.infantis(Blon_2336) indicated that residues Asp193and Glu237might be important for substrate binding.