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-Reference-Cited by-同舟云学术

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

Published:2020-02-11 Issue:6 Volume:10 Page:3809-3819
ISSN:2155-5435
Container-title:ACS Catalysis
language:en
Short-container-title:ACS Catal.

Author:

Teze David¹²^ORCID,Shuoker Bashar¹³,Chaberski Evan Kirk²,Kunstmann Sonja¹,Fredslund Folmer²^ORCID,Nielsen Tine Sofie¹,Stender Emil G. P.¹,Peters Günther H. J.⁴^ORCID,Karlsson Eva Nordberg³^ORCID,Welner Ditte Hededam²^ORCID,Hachem Maher Abou¹^ORCID

Affiliation:

1. Department of Biotechnology and Biomedicine, Technical University of Denmark, DK-2800 Lyngby, Denmark

2. Enzyme Engineering and Structural Biology, The Novo Nordisk Center for Biosustainability, Kemitorvet, Building 220, DK-2800 Lyngby, Denmark

3. Biotechnology, Department of Chemistry (KILU), Lund University, Post Office Box 124, 221 00 Lund, Sweden

4. Department of Chemistry, Technical University of Denmark, DK-2800 Lyngby, Denmark

Funder

Novo Nordisk Fonden

H2020 Marie Sklodowska-Curie Actions

Ministry of Higher Education and Scientific Research

Publisher

American Chemical Society (ACS)

Subject