Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.

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

Autor: Teze, David, Shuoker, Bashar, Chaberski, Evan Kirk, Kunstmann, Sonja, Fredslund, Folmer, Nielsen, Tine Sofie, Stender, Emil G. P., Peters, Günther H.J., Nordberg Karlsson, Eva, Welner, Ditte Hededam, Abou Hachem, Maher

Publikováno v: Teze, D, Shuoker, B, Chaberski, E K, Kunstmann, S, Fredslund, F, Nielsen, T S, Stender, E G P, Peters, G H J, Nordberg Karlsson, E, Welner, D H & Abou Hachem, M 2020, ' 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 ', A C S Catalysis, vol. 10, pp. 3809-3819 . https://doi.org/10.26434/chemrxiv.9989102.v1, https://doi.org/10.1021/acscatal.9b04474

Enzymes active on glycosidic bonds are defined according to the stereochemistry of both substrates and products of the reactions they catalyse. The CAZy classification further assigns these enzymes into sequence-based families sharing a common stereo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::953d669b7728f68b73038a8edc71c16c
https://orbit.dtu.dk/en/publications/2e1d692d-29a2-445b-b45d-c201cf19f764

Discovery of fungal oligosaccharide-oxidising flavo-enzymes with previously unknown substrates, redox-activity profiles and interplay with LPMOs.

Autor: Haddad Momeni, Majid, Fredslund, Folmer, Bissaro, Bastien, Raji, Olanrewaju, Vuong, Thu V., Meier, Sebastian, Nielsen, Tine Sofie, Lombard, Vincent, Guigliarelli, Bruno, Biaso, Frédéric, Haon, Mireille, Grisel, Sacha, Henrissat, Bernard, Welner, Ditte Hededam, Master, Emma R., Berrin, Jean-Guy, Abou Hachem, Maher

Publikováno v: Nature Communications; 4/9/2021, Vol. 12 Issue 1, p1-13, 13p

Akkermansia muciniphila exoglycosidases target extended blood group antigens to generate ABO-universal blood.

Autor: Jensen M; Department of Biotechnology & Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark., Stenfelt L; Department of Biotechnology & Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark.; Division of Hematology and Transfusion Medicine, Department of Laboratory Medicine, Lund University, Lund, Sweden., Ricci Hagman J; Division of Hematology and Transfusion Medicine, Department of Laboratory Medicine, Lund University, Lund, Sweden.; Department of Clinical Immunology and Transfusion Medicine, Office for Medical Services, Region Skåne, Sweden., Pichler MJ; Department of Biotechnology & Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark., Weikum J; Department of Biotechnology & Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark., Nielsen TS; Department of Biotechnology & Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark., Hult A; Department of Clinical Immunology and Transfusion Medicine, Office for Medical Services, Region Skåne, Sweden., Morth JP; Department of Biotechnology & Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark., Olsson ML; Division of Hematology and Transfusion Medicine, Department of Laboratory Medicine, Lund University, Lund, Sweden. martin_l.olsson@med.lu.se.; Department of Clinical Immunology and Transfusion Medicine, Office for Medical Services, Region Skåne, Sweden. martin_l.olsson@med.lu.se., Abou Hachem M; Department of Biotechnology & Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark. maha@bio.dtu.dk.

Publikováno v: Nature microbiology [Nat Microbiol] 2024 May; Vol. 9 (5), pp. 1176-1188. Date of Electronic Publication: 2024 Apr 29.