ArticlePlant physiology2007
Enzymatic properties and subcellular localization of Arabidopsis beta-N-acetylhexosaminidases.
Article in Plant physiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 56 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
56 citing papers in PubMed, 116 citations in OpenAlex.
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- Ethylene-Mediated Regulation of a Ripening-Specific N-glycan-processing enzyme β-D-N-Acetylhexosaminidase.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Trafficking and localization of Golgi-residentFrontiers in plant science · 2025Review
- Advances and challenges in plant N-glycoengineering: when fucosylation matters.Frontiers in plant science · 2025Review
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- Genome-Wide Identification of a Maize Chitinase Gene Family and the Induction of Its Expression byGenes · 2024Article
- Genetic and functional diversity of β-N-acetylgalactosamine-targeting glycosidases expanded by deep-sea metagenome analysis.Nature communications · 2024Article
- Functional Characterization of Lycopene β- and ε-Cyclases from a Lutein-Enriched Green MicroalgaMarine drugs · 2023Article
- Review
- Towards understanding the extensive diversity of protein N-glycan structures in eukaryotes.Biological reviews of the Cambridge Philosophical Society · 2022Review
- Glyco-Engineering Plants to Produce Helminth Glycoproteins as Prospective Biopharmaceuticals: Recent Advances, Challenges and Future Prospects.Frontiers in plant science · 2022Review
- Recent Developments in Deciphering the Biological Role of Plant ComplexFrontiers in plant science · 2022Review
- Inactivation of the β (1, 2)-xylosyltransferase and the α (1, 3)-fucosyltransferase gene in rice (Oryza sativa) by multiplex CRISPR/Cas9 strategy.Plant cell reports · 2021Article
- The N-glycan processing enzymes β-D-N-acetylhexosaminidase are involved in ripening-associated softening in strawberry fruit.Journal of food science and technology · 2021Article
- Glyco-Engineering of Plant-Based Expression Systems.Advances in biochemical engineering/biotechnology · 2021Article
- β-Hexosaminidases Along the Secretory Pathway ofFrontiers in plant science · 2021Article
- ComplexFrontiers in plant science · 2021Article
- Cracking the "Sugar Code": A Snapshot ofFrontiers in plant science · 2021Review
- Inactivation ofFrontiers in plant science · 2021Article
Corrections and comments
- Erratum issued
Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Plant glycoproteins contain substantial amounts of paucimannosidic N-glycans lacking terminal GlcNAc residues at their nonreducing ends. It has been proposed that this is due to the action of beta-hexosaminidases during late stages of N-glycan processing or in the course of N-glycan turnover. We have now cloned the three putative beta-hexosaminidase sequences present in the Arabidopsis (Arabidopsis thaliana) genome. When heterologously expressed as soluble forms in Spodoptera frugiperda cells, the enzymes (termed HEXO1-3) could all hydrolyze the synthetic substrates p-nitrophenyl-2-acetamido-2-deoxy-beta-d-glucopyranoside, p-nitrophenyl-2-acetamido-2-deoxy-beta-d-galactopyranoside, 4-methylumbelliferyl-2-acetamido-2-deoxy-beta-d-glucopyranoside, and 4-methylumbelliferyl-6-sulfo-2-acetamido-2-deoxy-beta-d-glucopyranoside, albeit to a varying extent. HEXO1 to HEXO3 were further able to degrade pyridylaminated chitotriose, whereas pyridylaminated chitobiose was only cleaved by HEXO1. With N-glycan substrates, HEXO1 displayed a much higher specific activity than HEXO2 and HEXO3. Nevertheless, all three enzymes were capable of removing terminal GlcNAc residues from the alpha1,3- and alpha1,6-mannosyl branches of biantennary N-glycans without any strict branch preference. Subcellular localization studies with HEXO-fluorescent protein fusions transiently expressed in Nicotiana benthamiana plants showed that HEXO1 is a vacuolar protein. In contrast, HEXO2 and HEXO3 are mainly located at the plasma membrane. These results indicate that HEXO1 participates in N-glycan trimming in the vacuole, whereas HEXO2 and/or HEXO3 could be responsible for the processing of N-glycans present on secretory glycoproteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.