Glycosynthase mutants of endoglycosidase S2 show potent transglycosylation activity and remarkably relaxed substrate specificity for antibody glycosylation remodeling

Journal of Biological Chemistry

Volumn 291, Issue 32, 2016, Pages 16508-16518

  Li, Tiezheng ^a   Tong, Xin ^a   Yang, Qiang ^a   Giddens, John P ^a   Wang, Lai Xi ^a  

^a Bldg 142   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HYDROLYSIS; MONOCLONAL ANTIBODIES; POLYSACCHARIDES;

BIOLOGICAL FUNCTIONS; COMPARATIVE STUDIES; HYDROLYSIS ACTIVITY; SITE DIRECTED MUTAGENESIS; STREPTOCOCCUS PYOGENES; SUBSTRATE SPECIFICITY; THERAPEUTIC MONOCLONAL ANTIBODIES; TRANS GLYCOSYLATION ACTIVITY;

GLYCOSYLATION;

ENDOGLYCOSIDASE S2; GLYCAN; GLYCOSIDASE; MUTANT PROTEIN; RITUXIMAB; TRASTUZUMAB; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; NDOS PROTEIN, STREPTOCOCCUS PYOGENES;

ANTIBODY GLYCOSYLATION; ARTICLE; COMPARATIVE STUDY; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; GLYCOSYLATION; HYDROLYSIS; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; SITE DIRECTED MUTAGENESIS; STREPTOCOCCUS PYOGENES; WILD TYPE; CHEMISTRY; ENZYMOLOGY; GENETICS; MUTATION;

BACTERIAL PROTEINS; GLYCOSIDE HYDROLASES; GLYCOSYLATION; HYDROLYSIS; MUTATION; RITUXIMAB; STREPTOCOCCUS PYOGENES; SUBSTRATE SPECIFICITY; TRASTUZUMAB;

EID: 84982803694     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M116.738765     Document Type: Article

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