6m55

Publication Abstract from PubMed

A GH1 beta-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 A 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.

Crystal structure of a GH1 beta-glucosidase from Hamamotoa singularis.,Uehara R, Iwamoto R, Aoki S, Yoshizawa T, Takano K, Matsumura H, Tanaka SI Protein Sci. 2020 Jul 26. doi: 10.1002/pro.3916. PMID:32713015^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.