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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

Teze, David ; Shuoker, Bashar ; Chaberski, Evan Kirk ; Kunstmann, Sonja ; Fredslund, Folmer ; Nordberg Karlsson, Eva LU orcid ; Welner, Ditte Hededam and Abou Hachem, Maher (2019) In ChemRxiv
Abstract
The study describes the first glycoside hydrolase that exhibits comparable levels of activity on α- and β-linked saccharide substrates. This enzyme, assigned into GH109, is encoded by the genome of the human gut symbiont Akkermansia muciniphila that is a model primary degrader of the heavily O-glycosylated mucin glycoprotein that coats the epithelial enterocytes.The elusive catalytic acid/base catalyst in GH109 enzymes is identified as a histidine that is presented by a flexible loop that positions it for catalysis on both α- and β-substrates. This dual activity may be an evolutionary adaptation to extend the range of substrates targeted by a single non-canonical NAD+-dependant GH.
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published
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ChemRxiv
DOI
10.26434/chemrxiv.9989102.v1
language
English
LU publication?
yes
id
95a7dc00-cd12-4bd6-8753-5873b43e7240
date added to LUP
2019-11-15 16:20:47
date last changed
2025-04-04 15:08:06
@misc{95a7dc00-cd12-4bd6-8753-5873b43e7240,
  abstract     = {{The study describes the first glycoside hydrolase that exhibits comparable levels of activity on α- and β-linked saccharide substrates. This enzyme, assigned into GH109, is encoded by the genome of the human gut symbiont Akkermansia muciniphila that is a model primary degrader of the heavily O-glycosylated mucin glycoprotein that coats the epithelial enterocytes.The elusive catalytic acid/base catalyst in GH109 enzymes is identified as a histidine that is presented by a flexible loop that positions it for catalysis on both α- and β-substrates. This dual activity may be an evolutionary adaptation to extend the range of substrates targeted by a single non-canonical NAD+-dependant GH.}},
  author       = {{Teze, David and Shuoker, Bashar and Chaberski, Evan Kirk and Kunstmann, Sonja and Fredslund, Folmer and Nordberg Karlsson, Eva and Welner, Ditte Hededam and Abou Hachem, Maher}},
  language     = {{eng}},
  month        = {{10}},
  series       = {{ChemRxiv}},
  title        = {{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}},
  url          = {{http://dx.doi.org/10.26434/chemrxiv.9989102.v1}},
  doi          = {{10.26434/chemrxiv.9989102.v1}},
  year         = {{2019}},
}