Open AccessThe Catalytic Acid–Base in GH109 Resides in a Conserved GGHGG Loop and Allows for Comparable α-Retaining and β-Inverting Activity in an N-Acetylgalactosaminidase from Akkermansia muciniphila
Author(s) -
David Tezé,
Bashar Shuoker,
Evan Kirk Chaberski,
Sonja Kunstmann,
Folmer Fredslund,
Tine Sofie Nielsen,
Emil G. P. Stender,
Günther H. Peters,
Eva Nordberg Karlsson,
Ditte Hededam Welner,
Maher Abou Hachem
Publication year - 2020
Publication title -
acs catalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.898
H-Index - 198
ISSN - 2155-5435
DOI - 10.1021/acscatal.9b04474
Subject(s) - akkermansia muciniphila , glycoside hydrolase , glycosidic bond , stereochemistry , enzyme , glycan , chemistry , active site , hydrolase , biochemistry , biology , computational biology , glycoprotein , gut flora
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