ArticleJournal of experimental botany2017
Heterologous expression and characterization of an Arabidopsis β-l-arabinopyranosidase and α-d-galactosidases acting on β-l-arabinopyranosyl residues.
Article in Journal of experimental botany, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 28 citations in OpenAlex.
- The Achilles Heel of Protein Biochemistry: Insolubility of Recombinant Proteins-A Case Study About Producing a Rice Enzyme.International journal of molecular sciences · 2025Article
- OsAPSE modulates non-covalent interactions between arabinogalactan proteinFrontiers in plant science · 2025Article
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- Analysis of the apoplast fluid proteome during the induction of systemic acquired resistance inPeerJ · 2023Article
- Involvement of α-galactosidase OmAGAL2 in planteose hydrolysis during seed germination of Orobanche minor.Journal of experimental botany · 2022Article
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- Identification and Expression Analysis of the Genes Involved in the Raffinose Family Oligosaccharides Pathway ofPlants (Basel, Switzerland) · 2021Article
- Cracking the "Sugar Code": A Snapshot ofFrontiers in plant science · 2021Review
- An integrative Study Showing the Adaptation to Sub-Optimal Growth Conditions of Natural Populations ofCells · 2020Article
- Three Decades of Advances in Arabinogalactan-Protein Biosynthesis.Frontiers in plant science · 2020Review
- On the Potential Function of Type II ArabinogalactanFrontiers in plant science · 2020Review
- Fine mapping of an up-curling leaf locus (BnUC1) in Brassica napus.BMC plant biology · 2019Article
- Characterization of a GH36 β-L-Arabinopyranosidase inJournal of applied glycoscience · 2018Article
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10 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The major plant sugar l-arabinose (l-Ara) has two different ring forms, l-arabinofuranose (l-Araf) and l-arabinopyranose (l-Arap). Although l-Ara mainly appears in the form of α-l-Araf residues in cell wall components, such as pectic α-1,3:1,5-arabinan, arabinoxylan, and arabinogalactan-proteins (AGPs), lesser amounts of it can also be found as β-l-Arap residues of AGPs. Even though AGPs are known to be rapidly metabolized, the enzymes acting on the β-l-Arap residues remain to be identified. In the present study, four enzymes, which we call β-l-ARAPASE (APSE) and α-GALACTOSIDASE 1 (AGAL1), AGAL2, and AGAL3, are identified as those enzymes that are likely to be responsible for the hydrolysis of the β-l-Arap residues in Arabidopsis thaliana. An Arabidopsis apse-1 mutant showed significant reduction in β-l-arabinopyranosidase activity, and an apse-1 agal3-1 double-mutant exhibited even less activity. The apse-1 and the double-mutants both had more β-l-Arap residues in the cell walls than wild-type plants. Recombinant APSE expressed in the yeast Pichia pastoris specifically hydrolyzed β-l-Arap residues and released l-Ara from gum arabic and larch arabinogalactan. The recombinant AGAL3 also showed weak β-l-arabinopyranosidase activity beside its strong α-galactosidase activity. It appears that the β-l-Arap residues of AGPs are hydrolysed mainly by APSE and partially by AGALs in Arabidopsis.
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