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Endohexosaminidase M: Exploring and Exploiting Enzyme Substrate Specificity
Author(s) -
Rising Thomas W. D. F.,
Claridge Timothy D. W.,
Moir James W. B.,
Fairbanks Antony J.
Publication year - 2006
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.200600183
Subject(s) - glycosylation , oxazoline , glycosyl , chemistry , mannose , glycosyl donor , substrate (aquarium) , enzyme , hydrolysis , biochemistry , glycosyltransferase , stereochemistry , combinatorial chemistry , catalysis , biology , ecology
Oxazoline saccharides have been synthesised and tested as glycosyl donors for endohexosaminidase M (Endo M)‐catalysed glycosylation of a GlcNAcAsn glycosyl amino acid. Endo M‐catalysed glycosylation is not limited to donors containing the Manβ(1‐4)GlcNAc linkage, and replacement of the core mannose unit by glucose promotes irreversible glycosylation. In this case, use of a modified oxazoline donor as a transition‐state mimic allows enzyme‐catalysed synthesis, but precludes product hydrolysis.