ArticleThe Journal of biological chemistry2011
Structural determinants of an insect beta-N-Acetyl-D-hexosaminidase specialized as a chitinolytic enzyme.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 101 citations in OpenAlex.
- Discovery of Pyrroloquinazoline-1,3-diamines as Dual-function Insecticide Candidates Targeting β-N-acetyl-D-hexosaminidase.Current medicinal chemistry · 2026Article
- Article
- Virtual screening of a random tripeptide library for easily prepared inhibitors of insect chitinolytic enzymes.Cell surface (Amsterdam, Netherlands) · 2025Article
- Rational design of azo-aminopyrimidine derivatives as the potent lepidoptera-exclusive chitinase inhibitors.Plant biotechnology journal · 2025Article
- Molecular Dynamics Simulations Suggest That Side-Chain Motions of Charged Amino Acids Determine Long-Range Effects in Proteins: An Egg of Coulomb.International journal of molecular sciences · 2024Article
- Structure-guided computational insecticide discovery targetingJournal of biomolecular structure & dynamics · 2024Article
- Increased RNAi Efficiency by dsInsects · 2022Article
- Release of Mediator Enzyme β-Hexosaminidase and Modulated Gene Expression Accompany Hemocyte Degranulation in Response to Parasitism in the Silkworm Bombyx mori.Biochemical genetics · 2021Article
- Structural basis of chitin utilization by a GH20 β-N-acetylglucosaminidase from Vibrio campbellii strain ATCC BAA-1116.Acta crystallographica. Section D, Structural biology · 2021Article
- Review on Structures of Pesticide Targets.International journal of molecular sciences · 2020Review
- The beta-1, 4-N-acetylglucosaminidase 1 gene, selected by domestication and breeding, is involved in cocoon construction of Bombyx mori.PLoS genetics · 2020Article
- Examining the molecular characteristics of glycoside hydrolase family 20 β-N-acetylglucosaminidases with high activity.Bioengineered · 2019Article
- Knockdown ofInsects · 2019Article
- Complex N-glycan breakdown by gut Bacteroides involves an extensive enzymatic apparatus encoded by multiple co-regulated genetic loci.Nature microbiology · 2019Article
- Computational Study for the Unbinding Routes of β-International journal of molecular sciences · 2019Article
- Characterization ofInternational journal of molecular sciences · 2019Article
- Modification of the Thioglycosyl-Naphthalimides as Potent and Selective Human O-GlcNAcase Inhibitors.ACS medicinal chemistry letters · 2018Article
- Glycoside hydrolase family 18 and 20 enzymes are novel targets of the traditional medicine berberine.The Journal of biological chemistry · 2018Article
- A Shinella β-N-acetylglucosaminidase of glycoside hydrolase family 20 displays novel biochemical and molecular characteristics.Extremophiles : life under extreme conditions · 2017Article
- Distinctive molecular and biochemical characteristics of a glycoside hydrolase family 20 β-N-acetylglucosaminidase and salt tolerance.BMC biotechnology · 2017Article
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
β-N-acetyl-D-hexosaminidase has been postulated to have a specialized function. However, the structural basis of this specialization is not yet established. OfHex1, the enzyme from the Asian corn borer Ostrinia furnacalis (one of the most destructive pests) has previously been reported to function merely in chitin degradation. Here the vital role of OfHex1 during the pupation of O. furnacalis was revealed by RNA interference, and the crystal structures of OfHex1 and OfHex1 complexed with TMG-chitotriomycin were determined at 2.1 Å. The mechanism of selective inhibition by TMG-chitotriomycin was related to the existence of the +1 subsite at the active pocket of OfHex1 and a key residue, Trp(490), at this site. Mutation of Trp(490) to Ala led to a 2,277-fold decrease in sensitivity toward TMG-chitotriomycin as well as an 18-fold decrease in binding affinity for the substrate (GlcNAc)(2). Although the overall topology of the catalytic domain of OfHex1 shows a high similarity with the human and bacterial enzymes, OfHex1 is distinguished from these enzymes by large conformational changes linked to an "open-close" mechanism at the entrance of the active site, which is characterized by the "lid" residue, Trp(448). Mutation of Trp(448) to Ala or Phe resulted in a more than 1,000-fold loss in enzyme activity, due mainly to the effect on k(cat). The current work has increased our understanding of the structure-function relationship of OfHex1, shedding light on the structural basis that accounts for the specialized function of β-N-acetyl-D-hexosaminidase as well as making the development of species-specific pesticides a likely reality.
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