Structural snapshots of heparin depolymerization by heparin lyase I
Author
Han, 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, MiroslawOther Contributors
Date Issued
2009-12-04Subject
Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineeringDegree
Terms of Use
CC 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.; Attribution 3.0 United StatesFull Citation
Structural 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.Metadata
Show full item recordAbstract
Heparin 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.;Description
Journal 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.Department
The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);Publisher
ElsevierRelationships
The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Journal of Biological Chemistry; https://harc.rpi.edu/;Access
Open Access; A full text version is available in DSpace@RPI; A full text version is available in DSpace@RPI;Collections
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