A GH1 β‐glucosidase from the fungus Hamamotoa singularis (HsBglA) has high transgalactosylation activity and efficiently converts lactose to galactooligosaccharides. Consequently, HsBglA is among the most widely used enzymes for industrial galactooligosaccharide production. Here, we present the first crystal structures of HsBglA with and without 4′‐galactosyllactose, a tri‐galactooligosaccharide, at 3.0 and 2.1 Å resolutions, respectively. These structures reveal details of the structural elements that define the catalytic activity and substrate binding of HsBglA, and provide a possible interpretation for its high catalytic potency for transgalactosylation reaction.

中文翻译：

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来自 Hamamotoa singleis 的 GH1 β-葡萄糖苷酶的晶体结构。

来自真菌Hamamotoa singleis (HsBglA)的 GH1 β-葡萄糖苷酶具有高转半乳糖基化活性，可有效地将乳糖转化为低聚半乳糖。因此，HsBglA 是用于工业低聚半乳糖生产的最广泛使用的酶之一。在这里，我们分别以 3.0 和 2.1 Å 的分辨率展示了 HsBglA 的第一个晶体结构，其中包含和不包含 4'-半乳糖基乳糖（一种三聚半乳糖）。这些结构揭示了定义 HsBglA 催化活性和底物结合的结构元素的细节，并为其对转半乳糖基化反应的高催化效力提供了可能的解释。