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Enhanced Glycosylation with Mutants of Endohexosaminidase A (Endo A)
Author(s) -
Heidecke Christoph D.,
Ling Zhenlian,
Bruce Neil C.,
Moir James W. B.,
Parsons Thomas B.,
Fairbanks Antony J.
Publication year - 2008
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200800214
Subject(s) - histidine , glycosylation , mutant , chemistry , glutamine , residue (chemistry) , biochemistry , enzyme , ribonuclease , glycosyl , acceptor , hydrolysis , stereochemistry , amino acid , rna , physics , gene , condensed matter physics
The big make over : Replacement of the key Glu173 residue of Endo A by either glutamine or histidine produces mutant enzymes for which hydrolytic activity has either been eliminated, or significantly curtailed, yet which still effect transglycosylation of acceptor substrates by the use of oxazolines as glycosyl donors. The E173H histidine mutant was demonstrated to be more effective than wild‐type Endo A for the production of a single homogenous glycoform of ribonuclease B (see scheme).