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dc.contributor.authorDesai, Umesh R.
dc.contributor.authorWang, Hui Ming
dc.contributor.authorLinhardt, Robert J.
dc.date1993
dc.date.accessioned2022-06-27T17:14:38Z
dc.date.available2022-06-27T17:14:38Z
dc.date.issued1993-01-01
dc.identifier.citationSubstrate Specificity of the Heparin Lyases from Flavobacterium heparinum, U.R. Desai, H.M. Wang, R.J. Linhardt, Archives of Biochemistry and Biophysics, 306, 461-468 (1993).
dc.identifier.issn39861
dc.identifier.urihttps://doi.org/10.1006/abbi.1993.1538
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5974
dc.descriptionArchives of Biochemistry and Biophysics, 306, 461-468
dc.descriptionNote : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
dc.description.abstractA detailed knowledge about the substrate specificities of the heparin lyases is necessary when using these enzymes as tools for elucidating the sequence of heparin and heparan sulfate. The substrate specificity of heparin lyases I, II, and III have been profiled with structurally defined, heparin-derived oligosaccharides. The primary substrate specificities of heparin lyases I and III require the presence of 2-O-sulfated alpha-L-idopyranosyluronic acid and beta-D-glucopyranosyluronic acid residues, respectively, at the linkages being cleaved. Heparin lyase II demonstrates an intriguingly broad primary specificity for oligosaccharides, acting at linkages containing alpha-L-idopyranosyluronic and beta-D-glucopyranosyluronic acid as well as at linkages containing alpha-L-galactopyranosyluronic acid residues. In addition to their primary specificities, each lyase also demonstrates secondary specificities under forcing conditions. Differences in the sulfation pattern within uronic acid residues and sulfation of adjacent residues has profound impact on the ease of lyase cleavage of a glycosidic linkage. Specifically, heparin lyases I and III exhibit secondary specificity for oligosaccharides containing an unsulfated alpha-L-idopyranosyluronic acid residue. The lack of sulfation on residues adjacent to the linkage undergoing cleavage increases the action of heparin lyase III on a glycosidic linkage. In contrast, reduced sulfation on adjacent residues make glycosidic linkage resistant to heparin lyase I. The primary and secondary specificity can be rationalized on the basis of most favorable solution conformation of the uronic acid residues.
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1006/abbi.1993.1538
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofArchives of Biochemistry and Biophysics
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleSubstrate Specificity of the Heparin Lyases from Flavobacterium heparinum
dc.typeArticle
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dcterms.isVersionOfhttps://doi.org/10.1006/abbi.1993.1538
dc.rights.holderIn Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
rpi.description.pages461-468
rpi.description.volume306


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