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首页> 外文期刊>Crystallography reports >Small-angle scattering study of Aspergillus awamori glycoprotein glucoamylase
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Small-angle scattering study of Aspergillus awamori glycoprotein glucoamylase

机译：泡盛曲霉糖蛋白葡糖淀粉酶的小角散射研究

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摘要

Glucoamylase from fungus Aspergillus awamori is glycoside hydrolase that catalyzes the hydrolysis of alpha-1,4- and alpha-1,6-glucosidic bonds in glucose polymers and oligomers. This glycoprotein consists of a catalytic domain and a starch-binding domain connected by an O-glycosylated polypeptide chain. The conformation of the linker, the relative arrangement of the domains, and the structure of the full-length enzyme are unknown. The structure of the recombinant glucoamylase GA1 was studied by molecular modelling and small-angle neutron scattering (SANS) methods. The experimental SANS data provide evidence that glucoamylase exists as a monomer in solution and contains a glycoside component, which makes a substantial contribution to the scattering. The model of full-length glucoamylase, which was calculated without taking into account the effect of glycosylation, is consistent with the experimental data and has a radius of gyration of 33.4 +/- 0.6 angstrom.
机译：来自泡盛曲霉的真菌的葡糖淀粉酶是糖苷水解酶，其催化葡萄糖聚合物和低聚物中α-1,4-和α-1,6-葡糖苷键的水解。该糖蛋白由通过O-糖基化的多肽链连接的催化结构域和淀粉结合结构域组成。接头的构象，结构域的相对排列以及全长酶的结构尚不清楚。通过分子模拟和小角度中子散射（SANS）方法研究了重组葡糖淀粉酶GA1的结构。实验性SANS数据提供了证据，表明葡糖淀粉酶以单体形式存在于溶液中并含有糖苷成分，这对散射起了重要作用。在不考虑糖基化作用的情况下计算的全长葡糖淀粉酶模型与实验数据一致，并且回转半径为33.4 +/- 0.6埃。

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