ArticleApplied microbiology and biotechnology2023
Crystal structure and identification of amino acid residues for catalysis and binding of GH3 AnBX β-xylosidase from Aspergillus niger.
Article in Applied microbiology and biotechnology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 6 citations in OpenAlex.
- Expression and Characterization of a Rice β-Xylosidase with Xylooligosaccharide Hydrolysis and Transglycosylation Activities.Journal of agricultural and food chemistry · 2025Article
- Novel glycosidase from Paenibacillus lactis 154 hydrolyzing the 28-O-β-D-glucopyranosyl ester bond of oleanane-type saponins.Applied microbiology and biotechnology · 2024Article
- Characterization of BrGH3A, a bovine rumen-derived glycoside hydrolase family 3 β-glucosidase with a permuted domain arrangement.PloS one · 2024Article
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
Abstract
β-Xylosidases catalyze the hydrolysis of xylooligosaccharides to xylose in the final step of hemicellulose degradation. AnBX, which is a GH3 β-xylosidase from Aspergillus niger, has a high catalytic efficiency toward xyloside substrates. In this study, we report the three-dimensional structure and the identification of catalytic and substrate binding residues of AnBX by performing site-directed mutagenesis, kinetic analysis, and NMR spectroscopy-associated analysis of the azide rescue reaction. The structure of the E88A mutant of AnBX, determined at 2.5-Å resolution, contains two molecules in the asymmetric unit, each of which is composed of three domains, namely an N-terminal (β/α)
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