Search: onr:"swepub:oai:lup.lub.lu.se:bd29e90b-6378-4e06-86fc-09b423b3602b" >
The Catalytic Acid-...
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 (author)
- Technical University of Denmark
-
- Shuoker, Bashar (author)
- Lund University,Technical University of Denmark
-
- Chaberski, Evan Kirk (author)
- Technical University of Denmark
-
show more...
-
- Kunstmann, Sonja (author)
- Technical University of Denmark
-
- Fredslund, Folmer (author)
- Technical University of Denmark
-
- Nielsen, Tine Sofie (author)
- Technical University of Denmark
-
- Stender, Emil G.P. (author)
- Technical University of Denmark
-
- Peters, Günther H.J. (author)
- Technical University of Denmark
-
- Karlsson, Eva Nordberg (author)
- Lund University,Lunds universitet,Bioteknik,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biotechnology,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
-
- Welner, Ditte Hededam (author)
- Technical University of Denmark
-
- Hachem, Maher Abou (author)
- Technical University of Denmark
-
show less...
-
(creator_code:org_t)
- 2020-02-11
- 2020
- English 11 s.
-
In: ACS Catalysis. - : American Chemical Society (ACS). - 2155-5435. ; 10:6, s. 3809-3819
- Related links:
-
http://dx.doi.org/10...
-
show more...
-
https://backend.orbi...
-
https://lup.lub.lu.s...
-
https://doi.org/10.1...
-
show less...
Abstract
Subject headings
Close
- Enzymes active on glycosidic bonds are defined according to the stereochemistry of both substrates and products of the reactions they catalyze. The CAZy classification further assigns these enzymes into sequence-based families sharing a common stereochemistry for substrates (either α- or β-) and products (i.e., inverting or retaining mechanism). Here we describe the N-acetylgalactosaminidases AmGH109A and AmGH109B (i.e., GH109: glycoside hydrolase family 109) from the human gut symbiont Akkermansia muciniphila. Notably, AmGH109A displays α-retaining and β-inverting N-acetylgalactosaminidase activities with comparable efficiencies on natural disaccharides. This dual specificity could provide an advantage in targeting a broader range of host-derived glycans. We rationalize this discovery through bioinformatics, structural, mutational, and computational studies, unveiling a histidine residing in a conserved GGHGG motif as the elusive catalytic acid-base of the GH109 family.
Subject headings
- TEKNIK OCH TEKNOLOGIER -- Industriell bioteknik -- Biokatalys och enzymteknik (hsv//swe)
- ENGINEERING AND TECHNOLOGY -- Industrial Biotechnology -- Biocatalysis and Enzyme Technology (hsv//eng)
Keyword
- GH4
- glycoside hydrolase
- human gut microbiota
- inverting
- MD simulations
- mechanism
- mucin
- retaining
Publication and Content Type
- art (subject category)
- ref (subject category)
Find in a library
To the university's database
- By the author/editor
-
Teze, David
-
Shuoker, Bashar
-
Chaberski, Evan ...
-
Kunstmann, Sonja
-
Fredslund, Folme ...
-
Nielsen, Tine So ...
-
show more...
-
Stender, Emil G. ...
-
Peters, Günther ...
-
Karlsson, Eva No ...
-
Welner, Ditte He ...
-
Hachem, Maher Ab ...
-
show less...
- About the subject
-
- ENGINEERING AND TECHNOLOGY
-
ENGINEERING AND ...
-
and Industrial Biote ...
-
and Biocatalysis and ...
- Articles in the publication
-
ACS Catalysis
- By the university
-
Lund University