Structural snapshots of heparin depolymerization by heparin lyase I
AuthorHan, Young Hyun; Garron, Marie Line; Kim, Hye Yeon; Kim, Wan Seok; Zhang, Zhenqing; Ryu, Kyeong Seok; Shaya, David; Xiao, Zhongping; Cheong, Chaejoon; Kim, Yeong Shik; Linhardt, R. J.; Jeon, Young Ho; Cygler, Miroslaw
SubjectBiology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
Full 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.
MetadataShow full item record
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.;
DescriptionJournal of Biological Chemistry, 284, 34019–34027; Note : 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.
DepartmentThe Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
RelationshipsThe Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Journal of Biological Chemistry; https://harc.rpi.edu/;
AccessOpen Access; A full text version is available in DSpace@RPI; A full text version is available in DSpace@RPI;
The following license files are associated with this item: