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  • Teze, DavidTechnical University of Denmark (author)

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

  • Article/chapterEnglish2020

Publisher, publication year, extent ...

  • 2020-02-11
  • American Chemical Society (ACS),2020
  • 11 s.

Numbers

  • LIBRIS-ID:oai:lup.lub.lu.se:bd29e90b-6378-4e06-86fc-09b423b3602b
  • https://lup.lub.lu.se/record/bd29e90b-6378-4e06-86fc-09b423b3602bURI
  • https://doi.org/10.1021/acscatal.9b04474DOI

Supplementary language notes

  • Language:English
  • Summary in:English

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  • Subject category:art swepub-publicationtype
  • Subject category:ref swepub-contenttype

Notes

  • 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 and genre

Added entries (persons, corporate bodies, meetings, titles ...)

  • Shuoker, BasharLund University,Technical University of Denmark (author)
  • Chaberski, Evan KirkTechnical University of Denmark (author)
  • Kunstmann, SonjaTechnical University of Denmark (author)
  • Fredslund, FolmerTechnical University of Denmark(Swepub:lu)maxl-ffl (author)
  • Nielsen, Tine SofieTechnical University of Denmark (author)
  • Stender, Emil G.P.Technical University of Denmark (author)
  • Peters, Günther H.J.Technical University of Denmark (author)
  • Karlsson, Eva NordbergLund 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(Swepub:lu)biot-eno (author)
  • Welner, Ditte HededamTechnical University of Denmark (author)
  • Hachem, Maher AbouTechnical University of Denmark(Swepub:lu)biot-mah (author)
  • Technical University of DenmarkLund University (creator_code:org_t)

Related titles

  • In:ACS Catalysis: American Chemical Society (ACS)10:6, s. 3809-38192155-5435

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