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

FEBS Letters

Volumn 585, Issue 15, 2011, Pages 2461-2466

  Zhao, Wenjing ^a   Garron, Marie Line ^b   Yang, Bo ^c   Xiao, Zhongping ^c   Esko, Jeffrey D ^d   Cygler, Miroslaw ^a,b   Linhardt, Robert J ^a,c  

^a RENSSELAER POLYTECHNIC INSTITUTE   (United States)

^b MCGILL UNIVERSITY   (Canada)

^c Research Rensselaer Polytechnic Institute   (United States)

^d UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

3 O Sulfoglucosamine; Heparin; Heparin lyase II; Heparinase; Protein engineering; Site directed mutagenesis; Substrate specificity

Indexed keywords

3 O SULFOGLUCOSAMINE; ASPARAGINE; ASPARAGINE 405; GLUCOSAMINE DERIVATIVE; GLYCINE; HEPARIN LYASE; HEPARIN LYASE 2; UNCLASSIFIED DRUG;

ANALYTIC METHOD; ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; MUTANT; PRIORITY JOURNAL; PROTEIN CLEAVAGE; SITE DIRECTED MUTAGENESIS; WILD TYPE;

ANTICOAGULANTS; ASPARAGINE; BACTERIAL PROTEINS; CARBOHYDRATE SEQUENCE; GLUCOSAMINE; HEPARIN; HEPARIN LYASE; HEPARITIN SULFATE; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; POLYSACCHARIDES; SUBSTRATE SPECIFICITY;

EID: 79960903117     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2011.06.023     Document Type: Article

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