ArticleThe Journal of biological chemistry2015
Structural and functional study of D-glucuronyl C5-epimerase.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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Who cites it
24 citing papers in PubMed, 50 citations in OpenAlex.
- Distinct properties of Halobacterium salinarum Agl32, an archaeal D-glucuronyl C5-epimerase involved in N-glycosylation.Glycobiology · 2026Article
- Synthetic biology for heparin biomanufacturing.Bioresources and bioprocessing · 2026Review
- Identification of the D-glucuronyl C5-epimerase that introduces iduronic acid into N-linked glycans decorating archaeal glycoproteins.Communications biology · 2025Article
- D-glucuronyl C5-Epimerase Binds to EGFR to Suppress Kidney Fibrosis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Comprehensive Integrated Analyses of Proteins and Metabolites in Equine Seminal Plasma (Horses and Donkeys).Proteomes · 2025Article
- Involvement of GTPases and vesicle adapter proteins in Heparan sulfate biosynthesis: role of Rab1A, Rab2A and GOLPH3.The FEBS journal · 2025Article
- A high effective expression of human D-glucuronyl C5-epimerase with dimer structure inFrontiers in microbiology · 2025Article
- Identification and Verification of Biomarkers Related to Polyamine Metabolism in Diabetic Nephropathy.Journal of diabetes research · 2025Article
- Cell-surface d-glucuronyl C5-epimerase binds to porcine deltacoronavirus spike protein facilitating viral entry.Journal of virology · 2024Article
- Exploring Heparan Sulfate Proteoglycans as Mediators of Human Mesenchymal Stem Cell Neurogenesis.Cellular and molecular neurobiology · 2024Review
- Prognostic value ofHeliyon · 2023Article
- Mechanism and influencing factors of crystal-cell interaction in the formation of calcium oxalate stones.Zhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences · 2022Article
- The construction of a dual-functional strain that produces both polysaccharides and sulfotransferases.Biotechnology letters · 2021Article
- The structure of human dermatan sulfate epimerase 1 emphasizes the importance of C5-epimerization of glucuronic acid in higher organisms.Chemical science · 2021Article
- Elucidating the unusual reaction kinetics of D-glucuronyl C5-epimerase.Glycobiology · 2020Article
- Heparan Sulfate Proteoglycans Biosynthesis and Post Synthesis Mechanisms Combine Few Enzymes and Few Core Proteins to Generate Extensive Structural and Functional Diversity.Molecules (Basel, Switzerland) · 2020Review
- Substrate binding mode and catalytic mechanism of human heparan sulfate d-glucuronyl C5 epimerase.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Glycosaminoglycan-Protein Interactions by Nuclear Magnetic Resonance (NMR) Spectroscopy.Molecules (Basel, Switzerland) · 2018Review
- The "in and out" of glucosamine 6-O-sulfation: the 6th sense of heparan sulfate.Glycoconjugate journal · 2017Review
- Structure Based Substrate Specificity Analysis of Heparan Sulfate 6-O-Sulfotransferases.ACS chemical biology · 2017Article
Corrections and comments
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Authors and funding
15 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heparan sulfate (HS) is a glycosaminoglycan present on the cell surface and in the extracellular matrix, which interacts with diverse signal molecules and is essential for many physiological processes including embryonic development, cell growth, inflammation, and blood coagulation. D-glucuronyl C5-epimerase (Glce) is a crucial enzyme in HS synthesis, converting D-glucuronic acid to L-iduronic acid to increase HS flexibility. This modification of HS is important for protein ligand recognition. We have determined the crystal structures of Glce in apo-form (unliganded) and in complex with heparin hexasaccharide (product of Glce following O-sulfation), both in a stable dimer conformation. A Glce dimer contains two catalytic sites, each at a positively charged cleft in C-terminal α-helical domains binding one negatively charged hexasaccharide. Based on the structural and mutagenesis studies, three tyrosine residues, Tyr(468), Tyr(528), and Tyr(546), in the active site were found to be crucial for the enzymatic activity. The complex structure also reveals the mechanism of product inhibition (i.e. 2-O- and 6-O-sulfation of HS keeps the C5 carbon of L-iduronic acid away from the active-site tyrosine residues). Our structural and functional data advance understanding of the key modification in HS biosynthesis.
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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.