ArticleThe Journal of biological chemistry2009
A beta-l-Arabinopyranosidase from Streptomyces avermitilis is a novel member of glycoside hydrolase family 27.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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32 citing papers in PubMed, 89 citations in OpenAlex.
- Crystal structure of endo-β-1,6-galactanase from Streptomyces avermitilis.Acta crystallographica. Section D, Structural biology · 2026Article
- OsAPSE modulates non-covalent interactions between arabinogalactan proteinFrontiers in plant science · 2025Article
- Investigating diversity and similarity between CBM13 modules and ricin-B lectin domains using sequence similarity networks.BMC genomics · 2024Article
- Structural and biochemical analysis of family 92 carbohydrate-binding modules uncovers multivalent binding to β-glucans.Nature communications · 2024Article
- Functional identification of two novel carbohydrate-binding modules of glucuronoxylanase CrXyl30 and their contribution to the lignocellulose saccharification.Biotechnology for biofuels and bioproducts · 2023Article
- Assimilation of arabinogalactan side chains with novel 3-Microbiome research reports · 2023Article
- The Crystal Structure ofToxins · 2022Article
- Integrative structure determination reveals functional global flexibility for an ultra-multimodular arabinanase.Communications biology · 2022Article
- Novel 3-Applied and environmental microbiology · 2021Article
- The Role of Arabinogalactan Type II Degradation in Plant-Microbe Interactions.Frontiers in microbiology · 2021Review
- Characterization of a GH36 α-D-Galactosidase Associated with Assimilation of Gum Arabic inJournal of applied glycoscience · 2021Article
- Cracking the "Sugar Code": A Snapshot ofFrontiers in plant science · 2021Review
- Functional characterization of a novel thermophilic exo-arabinanase from Thermothielavioides terrestris.Applied microbiology and biotechnology · 2020Article
- A subfamily roadmap of the evolutionarily diverse glycoside hydrolase family 16 (GH16).The Journal of biological chemistry · 2019Article
- Characterization of a GH36 β-L-Arabinopyranosidase inJournal of applied glycoscience · 2018Article
- Discovery of α-l-arabinopyranosidases from human gut microbiome expands the diversity within glycoside hydrolase family 42.The Journal of biological chemistry · 2017Article
- Evolutionary relationships and expression analysis of EUL domain proteins in rice (Oryza sativa).Rice (New York, N.Y.) · 2017Article
- Heterologous expression and characterization of an Arabidopsis β-l-arabinopyranosidase and α-d-galactosidases acting on β-l-arabinopyranosyl residues.Journal of experimental botany · 2017Article
- The Mechanism by Which Arabinoxylanases Can Recognize Highly Decorated Xylans.The Journal of biological chemistry · 2016Article
- Metabolism of L-arabinose in plants.Journal of plant research · 2016Review
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Arabinogalactan proteins (AGPs) are a family of plant cell surface proteoglycans and are considered to be involved in plant growth and development. Because AGPs are very complex molecules, glycoside hydrolases capable of degrading AGPs are powerful tools for analyses of the AGPs. We previously reported such enzymes from Streptomyces avermitilis. Recently, a beta-l-arabinopyranosidase was purified from the culture supernatant of the bacterium, and its corresponding gene was identified. The primary structure of the protein revealed that the catalytic module was highly similar to that of glycoside hydrolase family 27 (GH27) alpha-d-galactosidases. The recombinant protein was successfully expressed as a secreted 64-kDa protein using a Streptomyces expression system. The specific activity toward p-nitrophenyl-beta-l-arabinopyranoside was 18 micromol of arabinose/min/mg, which was 67 times higher than that toward p- nitrophenyl-alpha-d-galactopyranoside. The enzyme could remove 0.1 and 45% l-arabinose from gum arabic or larch arabinogalactan, respectively. X-ray crystallographic analysis reveals that the protein had a GH27 catalytic domain, an antiparallel beta-domain containing Greek key motifs, another antiparallel beta-domain forming a jellyroll structure, and a carbohydrate-binding module family 13 domain. Comparison of the structure of this protein with that of alpha-d-galactosidase showed a single amino acid substitution (aspartic acid to glutamic acid) in the catalytic pocket of beta-l-arabinopyranosidase, and a space for the hydroxymethyl group on the C-5 carbon of d-galactose bound to alpha-galactosidase was changed in beta-l-arabinopyranosidase. Mutagenesis study revealed that the residue is critical for modulating the enzyme activity. This is the first report in which beta-l-arabinopyranosidase is classified as a new member of the GH27 family.
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