ArticleThe Journal of biological chemistry2012
Uncovering biphasic catalytic mode of C5-epimerase in heparan sulfate biosynthesis.
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. Cited by 37 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
37 citing papers in PubMed, 64 citations in OpenAlex.
- Advances in chemoenzymatic synthesis of glycosaminoglycans and proteoglycans.Current opinion in chemical biology · 2026Review
- Synthetic biology for heparin biomanufacturing.Bioresources and bioprocessing · 2026Review
- Editor's Choice Development of a method to measure the activity of heparan sulfate 6-endosulfatase for biological research.Glycobiology · 2025Article
- Genetic variability in proteoglycan biosynthetic genes reveals new facets of heparan sulfate diversity.Essays in biochemistry · 2024Review
- Biosynthetic production of anticoagulant heparin polysaccharides through metabolic and sulfotransferases engineering strategies.Nature communications · 2024Article
- Heparan Sulfate Biosynthesis and Sulfation Profiles as Modulators of Cancer Signalling and Progression.Frontiers in oncology · 2021Review
- Progress and challenges in the synthesis of sequence controlled polysaccharides.Beilstein journal of organic chemistry · 2021Review
- Advances in the preparation and synthesis of heparin and related products.Drug discovery today · 2020Review
- 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
- Evaluation of non-reducing end pathologic glycosaminoglycan detection method for monitoring therapeutic response to enzyme replacement therapy in human mucopolysaccharidosis I.Molecular genetics and metabolism · 2020Article
- 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
- Controlled Chemoenzymatic Synthesis of Heparan Sulfate Oligosaccharides.Angewandte Chemie (International ed. in English) · 2018Article
- Chemoenzymatic synthesis of heparan sulfate and heparin oligosaccharides and NMR analysis: paving the way to a diverse library for glycobiologists.Chemical science · 2017Article
- Epigenetic Regulation of the Biosynthesis & Enzymatic Modification of Heparan Sulfate Proteoglycans: Implications for Tumorigenesis and Cancer Biomarkers.International journal of molecular sciences · 2017Review
- Engineered heparins as new anticoagulant drugs.Bioengineering & translational medicine · 2017Review
- Heparan Sulfate Domains Required for Fibroblast Growth Factor 1 and 2 Signaling through Fibroblast Growth Factor Receptor 1c.The Journal of biological chemistry · 2017Article
- Biosynthesis of glycosaminoglycans: associated disorders and biochemical tests.Journal of inherited metabolic disease · 2016Review
- Uncovering the Catalytic Direction of Chondroitin AC Exolyase: FROM THE REDUCING END TOWARDS THE NON-REDUCING END.The Journal of biological chemistry · 2016Article
- Bioengineered heparins and heparan sulfates.Advanced drug delivery reviews · 2016Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Heparan sulfate (HS), a highly sulfated polysaccharide, is biosynthesized through a pathway involving several enzymes. C(5)-epimerase (C(5)-epi) is a key enzyme in this pathway. C(5)-epi is known for being a two-way catalytic enzyme, displaying a "reversible" catalytic mode by converting a glucuronic acid to an iduronic acid residue, and vice versa. Here, we discovered that C(5)-epi can also serve as a one-way catalyst to convert a glucuronic acid to an iduronic acid residue, displaying an "irreversible" catalytic mode. Our data indicated that the reversible or irreversible catalytic mode strictly depends on the saccharide substrate structures. The biphasic mode of C(5)-epi offers a novel mechanism to regulate the biosynthesis of HS with the desired biological functions.
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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.