ArticleThe Journal of biological chemistry2013
A novel bacterial enzyme with D-glucuronyl C5-epimerase activity.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 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
- Article
- A high effective expression of human D-glucuronyl C5-epimerase with dimer structure inFrontiers in microbiology · 2025Article
- Advances in the preparation and synthesis of heparin and related products.Drug discovery today · 2020Review
- Application-Oriented Marine Isomerases in Biocatalysis.Marine drugs · 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
- Sulfated Alginates as Heparin Analogues: A Review of Chemical and Functional Properties.Molecules (Basel, Switzerland) · 2017Review
- Structural and functional study of D-glucuronyl C5-epimerase.The Journal of biological chemistry · 2015Article
- Enzymatic modifications of exopolysaccharides enhance bacterial persistence.Frontiers in microbiology · 2015Review
- D-glucuronyl C5-epimerase cell type specifically affects angiogenesis pathway in different prostate cancer cells.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycosaminoglycans are biologically active polysaccharides that are found ubiquitously in the animal kingdom. The biosynthesis of these complex polysaccharides involves complicated reactions that turn the simple glycosaminoglycan backbone into highly heterogeneous structures. One of the modification reactions is the epimerization of D-glucuronic acid to its C5-epimer L-iduronic acid, which is essential for the function of heparan sulfate. Although L-iduronic acid residues have been shown to exist in polysaccharides of some prokaryotes, there has been no experimental evidence for the existence of a prokaryotic D-glucuronyl C5-epimerase. This work for the first time reports on the identification of a bacterial enzyme with D-glucuronyl C5-epimerase activity. A gene of the marine bacterium Bermanella marisrubri sp. RED65 encodes a protein (RED65_08024) of 448 amino acids that has an overall 37% homology to the human D-glucuronic acid C5-epimerase. Alignment of this peptide with the human and mouse sequences revealed a 60% similarity at the carboxyl terminus. The recombinant protein expressed in Escherichia coli showed epimerization activity toward substrates generated from heparin and the E. coli K5 capsular polysaccharide, thereby providing the first evidence for bacterial D-glucuronyl C5-epimerase activity. These findings may eventually be used for modification of mammalian glycosaminoglycans.
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