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Crystal structure of a GH1 β‐glucosidase from Hamamotoa singularis
Author(s) -
Uehara Ryo,
Iwamoto Riki,
Aoki Sayaka,
Yoshizawa Takuya,
Takano Kazufumi,
Matsumura Hiroyoshi,
Tanaka Shunichi
Publication year - 2020
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.3916
Subject(s) - catalysis , substrate (aquarium) , chemistry , enzyme , substrate specificity , lactose , crystal structure , crystal (programming language) , glycoside hydrolase , stereochemistry , biochemistry , biology , crystallography , computer science , ecology , programming language
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.