Asparagine 405 of heparin lyase II prevents the cleavage of glycosidic linkages proximate to a 3-O-sulfo glucosamine residue

Authors
Zhao, W.
Garron, M.L.
Yang, B.
Xiao, Z.
Esko, J.D.
Cygler, M
Linhardt, Robert J.
ORCID
https://orcid.org/0000-0003-2219-5833
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Issue Date
2011
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
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Full Citation
Asparagine 405 of heparin lyase II prevents the cleavage of glycosidic linkages proximate to a 3-O-sulfo glucosamine residue, W. Zhao, M.-L. Garron, B. Yang, Z. Xiao, J. D. Esko, M, Cygler, R. J. Linhardt, Febs Letters, 585, 2461–2466, 2011.
Abstract
Heparin and heparan sulfate contain a rare 3-O-sulfoglucosamine residue critical for anticoagulation and virus recognition, respectively. The glycosidic linkage proximate to this 3-O-sulfoglucosamine is resistant to cleavage by all heparin lyases. Heparin lyase II has a broad specificity. The crystal structure of the wild type heparin lyase II identified its active site and showed a close spatial proximity between Asn405 and the 3-OH group of the bound glucosamine residue. In this study, we mutated Asn405 to the less sterically demanding Ala405 or Gly405, which broadened the substrate specificity of heparin lyase II and caused it to cleave the resistant linkage proximate to the 3-O-sulfoglucosamine residue.
Description
Febs Letters, 585, 2461–2466
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Department
The Linhardt Research Labs.
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
Publisher
FEBS Press
Relationships
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
https://harc.rpi.edu/
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