Open AccessAn endo‐β‐ N ‐acetylglucosaminidase from E nterococcus faecalis V 583 responsible for the hydrolysis of high‐mannose and hybrid‐type N ‐linked glycans
Author(s) -
Bøhle Liv Anette,
Mathiesen Geir,
VaajeKolstad Gustav,
Eijsink Vincent G.H.
Publication year - 2011
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2011.02419.x
Subject(s) - endoglycosidase , glycan , glycosidic bond , glycoside hydrolase , mannose , biochemistry , enzyme , biology , glycoprotein , microbiology and biotechnology , chemistry
It has been demonstrated previously that E nterococcus faecalis produces secreted endoglycosidases that enable the bacteria to remove N ‐linked glycans from glycoproteins. One enzyme potentially responsible for this activity is EF 0114, comprising a typical GH 18 endoglycosidase domain and a GH 20 domain. We have analyzed the other candidate, EF 2863, and show that this predicted single domain GH 18 protein is an endo‐β‐ N ‐acetylglucosaminidase. EF 2863 hydrolyzes the glycosidic bond between two N ‐acetylglucosamines ( G lc NA c) in N ‐linked glycans of the high‐mannose and hybrid type, releasing the glycan and leaving one G lc NA c attached to the protein. The activity of EF 2863 is similar to that of the well known deglycosylating enzyme E ndo H from S treptomyces plicatus . According to the CAZ y nomenclature, the enzyme is designated E f E ndo18 A .