ArticleChemical science2021
The structure of human dermatan sulfate epimerase 1 emphasizes the importance of C5-epimerization of glucuronic acid in higher organisms.
Article in Chemical science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- Distinct properties of Halobacterium salinarum Agl32, an archaeal D-glucuronyl C5-epimerase involved in N-glycosylation.Glycobiology · 2026Article
- Article
- Identification of the D-glucuronyl C5-epimerase that introduces iduronic acid into N-linked glycans decorating archaeal glycoproteins.Communications biology · 2025Article
- State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025Review
- Review
- Dermatan Sulfate: Structure, Biosynthesis, and Biological Roles.Biomolecules · 2025Review
- Bacterial polysaccharide lyase family 33: Specificity from an evolutionarily conserved binding tunnel.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Inhibitors of dermatan sulfate epimerase 1 decreased accumulation of glycosaminoglycans in mucopolysaccharidosis type I fibroblasts.Glycobiology · 2024Article
- Computational modeling of the molecular basis for the calcium-dependence of the mannuronan C-5 epimerase AvAlgE6 fromComputational and structural biotechnology journal · 2023Article
- Molecular docking analysis of a dermatan sulfate tetra-saccharide to human alpha-L-iduronidase.Bioinformation · 2023Article
- Inhibition of iduronic acid biosynthesis by ebselen reduces glycosaminoglycan accumulation in mucopolysaccharidosis type I fibroblasts.Glycobiology · 2021Article
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 7 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dermatan sulfate epimerase 1 (DS-epi1, EC 5.1.3.19) catalyzes the conversion of d-glucuronic acid to l-iduronic acid on the polymer level, a key step in the biosynthesis of the glycosaminoglycan dermatan sulfate. Here, we present the first crystal structure of the catalytic domains of DS-epi1, solved at 2.4 Å resolution, as well as a model of the full-length luminal protein obtained by a combination of macromolecular crystallography and targeted cross-linking mass spectrometry. Based on docking studies and molecular dynamics simulations of the protein structure and a chondroitin substrate, we suggest a novel mechanism of DS-epi1, involving a His/double-Tyr motif. Our work uncovers detailed information about the domain architecture, active site, metal-coordinating center and pattern of
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Registered trials
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