The 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

David Teze, Bashar Shuoker, Evan Kirk Chaberski, Sonja Kunstmann, Folmer Fredslund, Tine Sofie Nielsen, Emil G. P. Stender, Günther H.J. Peters, Eva Nordberg Karlsson, Ditte Hededam Welner, Maher Abou Hachem*

*Corresponding author for this work

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