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
(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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/95a7dc00-cd12-4bd6-8753-5873b43e7240
- author
- Teze, David
; Shuoker, Bashar
; Chaberski, Evan Kirk
; Kunstmann, Sonja
; Fredslund, Folmer
; Nordberg Karlsson, Eva
LU
; Welner, Ditte Hededam and Abou Hachem, Maher
- organization
- publishing date
- 2019-10-21
- type
- Other contribution
- publication status
- published
- subject
- in
- 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
- 2021-02-17 02:31:37
@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}}, }