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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
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- Teze, David (författare)
- Technical University of Denmark
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- Shuoker, Bashar (författare)
- Lund University,Technical University of Denmark
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- Chaberski, Evan Kirk (författare)
- Technical University of Denmark
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- Kunstmann, Sonja (författare)
- Technical University of Denmark
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- Fredslund, Folmer (författare)
- Technical University of Denmark
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- Nielsen, Tine Sofie (författare)
- Technical University of Denmark
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- Stender, Emil G.P. (författare)
- Technical University of Denmark
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- Peters, Günther H.J. (författare)
- Technical University of Denmark
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- Karlsson, Eva Nordberg (författare)
- 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
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- Welner, Ditte Hededam (författare)
- Technical University of Denmark
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- Hachem, Maher Abou (författare)
- Technical University of Denmark
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(creator_code:org_t)
- 2020-02-11
- 2020
- Engelska 11 s.
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Ingår i: ACS Catalysis. - : American Chemical Society (ACS). - 2155-5435. ; 10:6, s. 3809-3819
- Relaterad länk:
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http://dx.doi.org/10...
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https://backend.orbi...
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https://lup.lub.lu.s...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- TEKNIK OCH TEKNOLOGIER -- Industriell bioteknik -- Biokatalys och enzymteknik (hsv//swe)
- ENGINEERING AND TECHNOLOGY -- Industrial Biotechnology -- Biocatalysis and Enzyme Technology (hsv//eng)
Nyckelord
- GH4
- glycoside hydrolase
- human gut microbiota
- inverting
- MD simulations
- mechanism
- mucin
- retaining
Publikations- och innehållstyp
- art (ämneskategori)
- ref (ämneskategori)
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Teze, David
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Shuoker, Bashar
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Chaberski, Evan ...
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Kunstmann, Sonja
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Fredslund, Folme ...
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Nielsen, Tine So ...
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Stender, Emil G. ...
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Peters, Günther ...
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Karlsson, Eva No ...
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Welner, Ditte He ...
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Hachem, Maher Ab ...
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