Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 15658847Journal NLM ID: 9716531Publisher: Washington, DC: American Chemical Society
Correspondence: ulf.lindahl
imbim.uu.se
Institutions: Department of Medical Biochemistry and Microbiology, Uppsala University, Box 582, SE-751 23 Uppsala, Sweden
Heparin remains a major drug in prevention of thromboembolic disease. Concerns related to its animal source have prompted search for heparin analogues. The anticoagulant activity of heparin depends on a specific pentasaccharide sequence that binds antithrombin. We report the generation of a product with antithrombin-binding, anticoagulant, and antithrombotic properties similar to those of heparin, through combined chemical and enzymatic modification of a bacterial (E. coli K5) polysaccharide. The process is readily applicable to large-scale production.
capsular polysaccharide, Escherichia coli, heparin, chemical synthesis, anticoagulant activity, enzymatic modification
Structure type: polymer chemical repeating unit
Location inside paper: p.349
Trivial name: K5 polysaccharide, K-antigen, N-acetyl heparosan, heparosan (N-acetylheparosan), heparosan, heparosan (glycosaminoglycan GAG), K5 CPS, heparosan (K5-antigen), N-acetylheparosan
Compound class: EPS, K-antigen, CPS, polysaccharide
Contained glycoepitopes: IEDB_115136,IEDB_140630,IEDB_141807,IEDB_151531,IEDB_153764,IEDB_423153
Methods: biological assays, biosynthetic modifications, chemoenzymatic modifications
Related record ID(s): 10798
NCBI Taxonomy refs (TaxIDs): 562Reference(s) to other database(s): GTC:G26089XS, GlycomeDB:
656
Show glycosyltransferases
There is only one chemically distinct structure:
Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 ]
NCBI PubMed ID: 15658847Journal NLM ID: 9716531Publisher: Washington, DC: American Chemical Society
Correspondence: ulf.lindahl
imbim.uu.se
Institutions: Department of Medical Biochemistry and Microbiology, Uppsala University, Box 582, SE-751 23 Uppsala, Sweden
Heparin remains a major drug in prevention of thromboembolic disease. Concerns related to its animal source have prompted search for heparin analogues. The anticoagulant activity of heparin depends on a specific pentasaccharide sequence that binds antithrombin. We report the generation of a product with antithrombin-binding, anticoagulant, and antithrombotic properties similar to those of heparin, through combined chemical and enzymatic modification of a bacterial (E. coli K5) polysaccharide. The process is readily applicable to large-scale production.
capsular polysaccharide, Escherichia coli, heparin, chemical synthesis, anticoagulant activity, enzymatic modification
Structure type: polymer chemical repeating unit
Location inside paper: p.350, Fig. 1
Contained glycoepitopes: IEDB_115136,IEDB_140630,IEDB_141807,IEDB_142354,IEDB_151531,IEDB_241120,IEDB_241121,IEDB_423153
Methods: biological assays, biosynthetic modifications, chemoenzymatic modifications
Biological activity: antithrombin-binding, anticoagulant activities, antithrombotic activities
Comments, role: modified capsular polysaccharide
Related record ID(s): 10573
NCBI Taxonomy refs (TaxIDs): 562Reference(s) to other database(s): GTC:G01715ML, GlycomeDB:
27829
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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