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dc.rights.licenseOpen Access
dc.rights.licenseA full text version is available in DSpace@RPI
dc.contributor.authorHan, Young Hyun
dc.contributor.authorGarron, Marie Line
dc.contributor.authorKim, Hye Yeon
dc.contributor.authorKim, Wan Seok
dc.contributor.authorZhang, Zhenqing
dc.contributor.authorRyu, Kyeong Seok
dc.contributor.authorShaya, David
dc.contributor.authorXiao, Zhongping
dc.contributor.authorCheong, Chaejoon
dc.contributor.authorKim, Yeong Shik
dc.contributor.authorLinhardt, R. J.
dc.contributor.authorJeon, Young Ho
dc.contributor.authorCygler, Miroslaw
dc.date2009
dc.date.accessioned2022-06-23T01:34:58Z
dc.date.available2022-06-23T01:34:58Z
dc.date.issued2009-12-04
dc.identifier.citationStructural snapshots of heparin depolymerization by heparin lyase I, Y.-H. Han, M.-L. Garron, H.-Y. Kim, W.-S. Kim, Z. Zhang, K.-S. Ryu, D. Shaya, Z. Xiao, C. Cheong, Y.-S. Kim, R. J. Linhardt, Y. H. Jeon, M. Cygler, Journal of Biological Chemistry, 284, 34019–34027, 2009.
dc.identifier.issn1083351X
dc.identifier.issn219258
dc.identifier.urihttps://doi.org/10.1074/jbc.M109.025338
dc.descriptionJournal of Biological Chemistry, 284, 34019–34027
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.abstractHeparin lyase I (heparinase I) specifically depolymerizes heparin, cleaving the glycosidic linkage next to iduronic acid. Here, we show the crystal structures of heparinase I from Bacteroides thetaiotaomicron at various stages of the reaction with heparin oligosaccharides before and just after cleavage and product disaccharide. The heparinase I structure is comprised of a beta-jellyroll domain harboring a long and deep substrate binding groove and an unusual thumb-resembling extension. This thumb, decorated with many basic residues, is of particular importance in activity especially on short heparin oligosaccharides. Unexpected structural similarity of the active site to that of heparinase II with an (alpha/alpha)(6) fold is observed. Mutational studies and kinetic analysis of this enzyme provide insights into the catalytic mechanism, the substrate recognition, and processivity.
dc.description.sponsorshipNational Heart, Lung, and Blood Institute
dc.languageENG
dc.language.isoen_US
dc.publisherElsevier
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofJournal of Biological Chemistry
dc.relation.urihttps://harc.rpi.edu/
dc.rightsAttribution 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/us/*
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleStructural snapshots of heparin depolymerization by heparin lyase Ien_US
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1074/jbc.M109.025338
dc.rights.holderCC BY : this license allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use. Credit must be given to the authors and the original work must be properly cited.
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.pages34019-34027
rpi.description.volume284


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