ArticleThe Journal of biological chemistry2012
Remarkable transglycosylation activity of glycosynthase mutants of endo-D, an endo-β-N-acetylglucosaminidase from Streptococcus pneumoniae.
Article in The Journal of biological chemistry, 2012. 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 42 papers.
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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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Who cites it
42 citing papers in PubMed, 78 citations in OpenAlex.
- Glycan Remodeling Technologies for Enhancing Antibody Function.Advances in experimental medicine and biology · 2026Review
- Glycan Remodeling Technologies for Enhancing Antibody Function.Advances in experimental medicine and biology · 2026Review
- Site-directed mutagenesis leads to the optimized transglycosylation activity of endo-beta-N-acetylglucosaminidase from Trypanosoma brucei.Glycoconjugate journal · 2024Article
- Article
- One-step synthesis of site-specific antibody-drug conjugates by reprograming IgG glycoengineering with LacNAc-based substrates.Acta pharmaceutica Sinica. B · 2022Article
- Recent Advances Toward Engineering Glycoproteins Using Modified Yeast Display Platforms.Methods in molecular biology (Clifton, N.J.) · 2022Review
- General and Robust Chemoenzymatic Method for Glycan-Mediated Site-Specific Labeling and Conjugation of Antibodies: Facile Synthesis of Homogeneous Antibody-Drug Conjugates.ACS chemical biology · 2021Article
- Proteomic response inJournal of oral microbiology · 2021Article
- Importance and Monitoring of Therapeutic Immunoglobulin G Glycosylation.Experientia supplementum (2012) · 2021Review
- Innovative Preparation of Biopharmaceuticals Using Transglycosylation Activity of Microbial Endoglycosidases.Journal of applied glycoscience · 2021Article
- Structural insights into the mechanisms and specificities of IgG-active endoglycosidases.Glycobiology · 2020Review
- On enzymatic remodeling of IgG glycosylation; unique tools with broad applications.Glycobiology · 2020Review
- Cell-Free Synthetic Glycobiology: Designing and Engineering Glycomolecules Outside of Living Cells.Frontiers in chemistry · 2020Review
- Structural basis for the specific cleavage of core-fucosylatedThe Journal of biological chemistry · 2019Article
- Glycoengineering of Antibodies for Modulating Functions.Annual review of biochemistry · 2019Review
- Chemoenzymatic Methods for the Synthesis of Glycoproteins.Chemical reviews · 2018Review
- Stable isotope labeling approaches for NMR characterization of glycoproteins using eukaryotic expression systems.Journal of biomolecular NMR · 2018Article
- Site-specific immobilization of endoglycosidases for streamlined chemoenzymatic glycan remodeling of antibodies.Carbohydrate research · 2018Article
- Characterization of novel endo-β-N-acetylglucosaminidases from Sphingobacterium species, Beauveria bassiana and Cordyceps militaris that specifically hydrolyze fucose-containing oligosaccharides and human IgG.Scientific reports · 2018Article
- Glycosylation engineering of therapeutic IgG antibodies: challenges for the safety, functionality and efficacy.Protein & cell · 2018Review
Corrections and comments
- Erratum issued
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Endo-β-N-acetylglucosaminidase from Streptococcus pneumoniae (Endo-D) is an endoglycosidase capable of hydrolyzing the Fc N-glycan of intact IgG antibodies after sequential removal of the sialic acid, galactose, and internal GlcNAc residues in the N-glycan. Endo-D also possesses transglycosylation activity with sugar oxazoline as the donor substrate, but the transglycosylation yield is low due to enzymatic hydrolysis of the donor substrate and the product. We report here our study on the hydrolytic and transglycosylation activity of recombinant Endo-D and its selected mutants. We found that Endo-D preferred core-fucosylated N-glycan for hydrolysis but favored nonfucosylated GlcNAc acceptor for transglycosylation. Several mutants showed significantly enhanced transglycosylation efficiency over the wild type enzyme. Two mutants (N322Q and N322A) were identified as typical glycosynthases that demonstrated remarkable transglycosylation activity with only marginal or no product hydrolysis activity. Kinetic studies revealed that the N322Q [corrected]and N322A glycosynthases had much higher catalytic efficiency for glycosylating the nonfucosylated GlcNAc acceptor. In comparison, the N322Q was much more efficient than N322A for transglycosylation. However, N322Q and N322A [corrected] could not take more complex N-glycan oxazoline as substrate for transglycosylation, indicating their strict substrate specificity. The usefulness of the N322Q glycosynthase was exemplified by its application for efficient glycosylation remodeling of IgG-Fc domain.
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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.