ArticlePloS one2018
Structural basis of product inhibition by arabinose and xylose of the thermostable GH43 β-1,4-xylosidase from Geobacillus thermoleovorans IT-08.
Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 30 citations in OpenAlex.
- Computational design and structure dynamics analysis of bifunctional chimera of endoxylanase from3 Biotech · 2023Article
- Arabinan saccharification by biogas reactor metagenome-derived arabinosyl hydrolases.Biotechnology for biofuels and bioproducts · 2022Article
- Ultrahigh-Throughput Screening of High-β-Xylosidase-ProducingJournal of fungi (Basel, Switzerland) · 2022Article
- Characterization of a GH Family 43 β-Xylosidase Having a Novel Carbohydrate-binding Module fromJournal of applied glycoscience · 2022Article
- Degradation of complex arabinoxylans by human colonic Bacteroidetes.Nature communications · 2021Article
- High-Throughput Generation of Product Profiles for Arabinoxylan-Active Enzymes from Metagenomes.Applied and environmental microbiology · 2020Article
- Consolidated bioprocessing of corn cob-derived hemicellulose: engineered industrialBiotechnology for biofuels · 2020Article
- β-Xylosidases: Structural Diversity, Catalytic Mechanism, and Inhibition by Monosaccharides.International journal of molecular sciences · 2019Review
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Complete degradation of the xylan backbone of hemicellulosic plant cell walls requires the synergistic action of endo-xylanases and β-1,4-xylosidases. While endo-xylanases produce xylooligosaccharides from xylan, β-1,4-xylosidases degrade the xylooligosaccharides into xylose monomers. The glycoside hydrolase family 43 β-1,4-xylosidase from Geobacillus thermoleovorans IT-08 is a promising, heat stable catalyst for the saccharification of hemicellulosic material into simple fermentable sugars, but it is competitively inhibited by its products arabinose and xylose. As a first step to help overcome this problem, we elucidated crystal structures of the enzyme in the unliganded form and with bound products, at 1.7-2.0 Å resolution. The structures are very similar to those of other enzymes belonging to glycoside hydrolase family 43. Unexpectedly, the monosaccharides are bound in very different ways. Arabinose preferentially binds in subsite -1, while xylose exclusively interacts with subsite +1. These structures and sugar binding preferences suggest ways for improving the catalytic performance of the enzyme by rational mutational design.
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Registered trials
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