ArticleThe Journal of biological chemistry2010
Structural and kinetic analysis of Bacillus subtilis N-acetylglucosaminidase reveals a unique Asp-His dyad mechanism.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 121 citations in OpenAlex.
- Denuded peptidoglycan oligosaccharides enable the biochemical investigation of bacterial cell wall recognition, modification, and degradation.The Journal of biological chemistry · 2026Article
- NagX, a periplasmic β-Antimicrobial agents and chemotherapy · 2026Article
- Ring opening, conformational analysis and NagZ inhibition of a GlcNAc-configured iminosugar-derived aziridine.Carbohydrate research · 2026Article
- N-acetylglucosamine sensing in the filamentous soil fungus Trichoderma reesei.The FEBS journal · 2025Article
- Genome-wide identification and gene expression pattern analysis of the glycoside hydrolase family 1 in Fagopyrum tataricum.BMC plant biology · 2024Article
- An Unusual His/Asp Dyad Operates Catalysis in Agar-Degrading Glycosidases.ACS catalysis · 2024Article
- Crystal structure and activity of a de novo enzyme, ferric enterobactin esterase Syn-F4.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- In Silico Analysis of a GH3 β-Glucosidase fromMicroorganisms · 2023Article
- Crystal structure and identification of amino acid residues for catalysis and binding of GH3 AnBX β-xylosidase from Aspergillus niger.Applied microbiology and biotechnology · 2023Article
- Review
- Functional metagenomic screening identifies an unexpected β-glucuronidase.Nature chemical biology · 2022Article
- The evolutionary advantage of an aromatic clamp in plant family 3 glycoside exo-hydrolases.Nature communications · 2022Article
- NamZ1 and NamZ2 from the Oral Pathogen Tannerella forsythia Are Peptidoglycan Processing Exo-β-Journal of bacteriology · 2022Article
- Enzymatic Preparation of Gentiooligosaccharides by a Thermophilic and Thermostable β-Glucosidase at a High Substrate Concentration.Foods (Basel, Switzerland) · 2022Article
- N-acetylglucosamine Signaling: Transcriptional Dynamics of a Novel Sugar Sensing Cascade in a Model Pathogenic Yeast,Journal of fungi (Basel, Switzerland) · 2021Review
- The bone-degrading enzyme machinery: From multi-component understanding to the treatment of residues from the meat industry.Computational and structural biotechnology journal · 2021Article
- High-Level Extracellular Expression of a New β-N-Acetylglucosaminidase inFrontiers in microbiology · 2021Article
- Characterization and diversity of the complete set of GH family 3 enzymes from Rhodothermus marinus DSM 4253.Scientific reports · 2020Article
- β-Xylosidases: Structural Diversity, Catalytic Mechanism, and Inhibition by Monosaccharides.International journal of molecular sciences · 2019Review
- Microbial Beta Glucosidase Enzymes: Recent Advances in Biomass Conversation for Biofuels Application.Biomolecules · 2019Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Three-dimensional structures of NagZ of Bacillus subtilis, the first structures of a two-domain β-N-acetylglucosaminidase of family 3 of glycosidases, were determined with and without the transition state mimicking inhibitor PUGNAc bound to the active site, at 1.84- and 1.40-Å resolution, respectively. The structures together with kinetic analyses of mutants revealed an Asp-His dyad involved in catalysis: His(234) of BsNagZ acts as general acid/base catalyst and is hydrogen bonded by Asp(232) for proper function. Replacement of both His(234) and Asp(232) with glycine reduced the rate of hydrolysis of the fluorogenic substrate 4'-methylumbelliferyl N-acetyl-β-D-glucosaminide 1900- and 4500-fold, respectively, and rendered activity pH-independent in the alkaline range consistent with a role of these residues in acid/base catalysis. N-Acetylglucosaminyl enzyme intermediate accumulated in the H234G mutant and β-azide product was formed in the presence of sodium azide in both mutants. The Asp-His dyad is conserved within β-N-acetylglucosaminidases but otherwise absent in β-glycosidases of family 3, which instead carry a "classical" glutamate acid/base catalyst. The acid/base glutamate of Hordeum vulgare exoglucanase (Exo1) superimposes with His(234) of the dyad of BsNagZ and, in contrast to the latter, protrudes from a second domain of the enzyme into the active site. This is the first report of an Asp-His catalytic dyad involved in hydrolysis of glycosides resembling in function the Asp-His-Ser triad of serine proteases. Our findings will facilitate the development of mechanism-based inhibitors that selectively target family 3 β-N-acetylglucosaminidases, which are involved in bacterial cell wall turnover, spore germination, and induction of β-lactamase.
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