Revisiting the AA14 family of lytic polysaccharide monooxygenases and their catalytic activity - INRAE - Institut national de recherche pour l’agriculture, l’alimentation et l’environnement
Article Dans Une Revue FEBS Letters Année : 2023

Revisiting the AA14 family of lytic polysaccharide monooxygenases and their catalytic activity

Tina Tuveng
Heidi Østby
  • Fonction : Auteur
Ketty Tamburrini
  • Fonction : Auteur
Bastien Bissaro
Olav Hegnar
  • Fonction : Auteur
Anton Stepnov
Anikó Várnai
Jean‐guy Berrin
  • Fonction : Auteur
Vincent Eijsink

Résumé

Lytic polysaccharide monooxygenases (LPMOs) belonging to the AA14 family are believed to contribute to the enzymatic degradation of lignocellulosic biomass by specifically acting on xylan in recalcitrant cellulose-xylan complexes. Functional characterization of an AA14 LPMO from Trichoderma reesei, TrAA14A, and a re-evaluation of the properties of the previously described AA14 from Pycnoporus coccineus, PcoAA14A, showed that these proteins have oxidase and peroxidase activities that are common for LPMOs. However, we were not able to detect activity on cellulose-associated xylan or any other tested polysaccharide substrate, meaning that the substrate of these enzymes remains unknown. Next to raising questions regarding the true nature of AA14 LPMOs, the present data illustrate possible pitfalls in the functional characterization of these intriguing enzymes.

Dates et versions

hal-04164881 , version 1 (18-07-2023)

Identifiants

Citer

Tina Tuveng, Heidi Østby, Ketty Tamburrini, Bastien Bissaro, Olav Hegnar, et al.. Revisiting the AA14 family of lytic polysaccharide monooxygenases and their catalytic activity. FEBS Letters, 2023, ⟨10.1002/1873-3468.14694⟩. ⟨hal-04164881⟩
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