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dc.contributor.authorMunoz, Eva
dc.contributor.authorXu, Ding
dc.contributor.authorKemp, Melissa
dc.contributor.authorZhang, Fuming
dc.contributor.authorLiu, Jian
dc.contributor.authorLinhardt, Robert J.
dc.date2006
dc.date.accessioned2022-06-23T03:56:08Z
dc.date.available2022-06-23T03:56:08Z
dc.date.issued2006-04-25
dc.identifier.citationAffinity, kinetic and structural study of the interaction of 3-O-sulfotransferase isoform 1 with heparan sulfate, E. Mu“oz, D. Xu, J. Liu, R. J. Linhardt, Biochemistry, 45, 5122-5118, 2006.
dc.identifier.issn62960
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5174
dc.identifier.urihttps://doi.org/10.1021/bi052403n
dc.descriptionBiochemistry, 45, 5122-5118
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.abstractThe 3-O-sulfonation of glucosamine residues in heparan sulfate (HS) by 3-O-sulfotransferase (3-OST) is a key substitution that is present in HS sequences of biological importance, in particular HS anticoagulant activity. Six different isoforms of 3-OST have been identified that exhibit different substrate specificity. In this paper the affinity and kinetics of the interaction between 3-O-sulfotransferase isoform 1 (3-OST-1) and HS have been examined using surface plasmon resonance (SPR). 3-OST-1 binds with micomolar affinity to HS (KD = 2.79 μM), and this interaction is apparently independent of the presence of the coenzyme, 3‘-phosphoadenosine 5‘-phosphosulfate (PAPS). A conformational change in the complex has also been detected, supporting data from previous studies. Selected 3-OST-1 mutants have provided valuable information of amino acid residues that participate in 3-OST-1 interaction with HS substrate and its catalytic activity. The results from this study contribute to understanding the substrate specificity among the 3-OST isoforms and in the mechanism of 3-OST-1-catalyzed biosynthesis of anticoagulant HS.
dc.description.sponsorshipNational Heart, Lung, and Blood Institute
dc.languageen_US
dc.language.isoENG
dc.publisherAmerican Chemical Society (ACS)
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofBiochemistry
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleAffinity, kinetic and structural study of the interaction of 3-O-sulfotransferase isoform 1 with heparan sulfate
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1021/bi052403n
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.pages5122-5128
rpi.description.volume45


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