{"metadata":{"accession":"PF16332","entry_id":null,"type":"repeat","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR032518","hierarchy":null,"name":{"name":"Dermatan-sulfate epimerase-like, N-terminal","short":"DSE-like_N"},"description":[{"text":"<p>This entry represents the N-terminal of dermatan-sulfate epimerase (DSE) from mammals, and heparin-sulfate lyase (HepB) from bacteria [[cite:PUB00076523]]. DSE converts D-glucuronic acid to L-iduronic acid (IdoUA) residues. It plays an important role in the biosynthesis of the glycosaminoglycan/mucopolysaccharide dermatan sulfate [[cite:PUB00162452],[cite:PUB00109125]]. HepB cleaves both heparin and heparan sulfate glycosaminoglycans through a beta-elimination mechanism. It cleaves heparin at alpha-D-GlcNp2S6S(1->4) alpha-L-IdoAp2S and heparan sulfate at alpha-D-GlcNp2Ac(or 2S)6OH(1->4)beta-D-GlcAp [[cite:PUB00016410]]. This domain is composed of helical hairpins.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00162452":{"PMID":7092807,"ISBN":null,"volume":"201","issue":"3","year":1982,"title":"Biosynthesis of dermatan sulphate. Assay and properties of the uronosyl C-5 epimerase.","URL":null,"raw_pages":"489-93","medline_journal":"Biochem J","ISO_journal":"Biochem J","authors":["Malmstrom A","Aberg L."],"DOI_URL":"https://doi.org/10.1042/bj2010489"},"PUB00016410":{"PMID":8702264,"ISBN":null,"volume":"62","issue":"8","year":1996,"title":"Isolation and expression in Escherichia coli of hepB and hepC, genes coding for the glycosaminoglycan-degrading enzymes heparinase II and heparinase III, respectively, from Flavobacterium heparinum.","URL":null,"raw_pages":"2723-34","medline_journal":"Appl Environ Microbiol","ISO_journal":"Appl. Environ. Microbiol.","authors":["Su H","Blain F","Musil RA","Zimmermann JJ","Gu K","Bennett DC."],"DOI_URL":"http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=8702264&action=stream&blobtype=pdf"},"PUB00076523":{"PMID":20404324,"ISBN":null,"volume":"285","issue":"26","year":2010,"title":"Catalytic mechanism of heparinase II investigated by site-directed mutagenesis and the crystal structure with its substrate.","URL":null,"raw_pages":"20051-61","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Shaya D","Zhao W","Garron ML","Xiao Z","Cui Q","Zhang Z","Sulea T","Linhardt RJ","Cygler M."],"DOI_URL":"http://dx.doi.org/10.1074/jbc.M110.101071"},"PUB00109125":{"PMID":16505484,"ISBN":null,"volume":"281","issue":"17","year":2006,"title":"Biosynthesis of dermatan sulfate: chondroitin-glucuronate C5-epimerase is identical to SART2.","URL":null,"raw_pages":"11560-8","medline_journal":"J Biol Chem","ISO_journal":"J Biol Chem","authors":["Maccarana M","Olander B","Malmstrom J","Tiedemann K","Aebersold R","Lindahl U","Li JP","Malmstrom A."],"DOI_URL":null}},"set_info":{"accession":"CL0059","name":"6_Hairpin"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":101,"interactions":0,"matches":3125,"pathways":0,"proteins":3098,"proteomes":1686,"sets":1,"structural_models":{"alphafold":2372},"structures":14,"taxa":4044},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":8,"alignment:full":2278},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}