TY - JOUR
T1 - Discovery of fungal oligosaccharide-oxidising flavo-enzymes with previously unknown substrates, redox-activity profiles and interplay with LPMOs
AU - Haddad Momeni, Majid
AU - Fredslund, Folmer
AU - Bissaro, Bastien
AU - Raji, Olanrewaju
AU - Vuong, Thu V.
AU - Meier, Sebastian
AU - Nielsen, Tine Sofie
AU - Lombard, Vincent
AU - Guigliarelli, Bruno
AU - Biaso, Frédéric
AU - Haon, Mireille
AU - Grisel, Sacha
AU - Henrissat, Bernard
AU - Welner, Ditte Hededam
AU - Master, Emma R.
AU - Berrin, Jean Guy
AU - Abou Hachem, Maher
N1 - Funding Information:
This study was supported by a Novo Nordisk Foundation Post-doc grant within the Biotechnology Based Synthesis and Production Research Programme to MHM (NNF17OC0025642). F.F. and D.H.W. were funded by The Novo Nordisk Foundation Grant No. NNF10CC1016517. NMR spectra were acquired at the NMR center DTU supported by the Villum and Carlsberg Foundations. J.G.B., B.G. (Bruno G) and F.B. (Frédéric B) thank IM2B (Institut de Microbiologie, Bioénergies et Biotechnologie). The DSC instrument is funded by the Carlsberg Foundation Grant (2013-01-0112) to M.A.H. The authors are also grateful to the EPR facilities available at the French EPR network (IR CNRS 3443) and the Aix-Marseille University EPR center. Prof. Peter Westh and Dr. Jeppi Kari are acknowledged for discussion on the redox-activities of AA7.
Publisher Copyright:
© 2021, The Author(s).
Copyright:
Copyright 2021 Elsevier B.V., All rights reserved.
PY - 2021/4/9
Y1 - 2021/4/9
N2 - Oxidative plant cell-wall processing enzymes are of great importance in biology and biotechnology. Yet, our insight into the functional interplay amongst such oxidative enzymes remains limited. Here, a phylogenetic analysis of the auxiliary activity 7 family (AA7), currently harbouring oligosaccharide flavo-oxidases, reveals a striking abundance of AA7-genes in phytopathogenic fungi and Oomycetes. Expression of five fungal enzymes, including three from unexplored clades, expands the AA7-substrate range and unveils a cellooligosaccharide dehydrogenase activity, previously unknown within AA7. Sequence and structural analyses identify unique signatures distinguishing the strict dehydrogenase clade from canonical AA7 oxidases. The discovered dehydrogenase directly is able to transfer electrons to an AA9 lytic polysaccharide monooxygenase (LPMO) and fuel cellulose degradation by LPMOs without exogenous reductants. The expansion of redox-profiles and substrate range highlights the functional diversity within AA7 and sets the stage for harnessing AA7 dehydrogenases to fine-tune LPMO activity in biotechnological conversion of plant feedstocks.
AB - Oxidative plant cell-wall processing enzymes are of great importance in biology and biotechnology. Yet, our insight into the functional interplay amongst such oxidative enzymes remains limited. Here, a phylogenetic analysis of the auxiliary activity 7 family (AA7), currently harbouring oligosaccharide flavo-oxidases, reveals a striking abundance of AA7-genes in phytopathogenic fungi and Oomycetes. Expression of five fungal enzymes, including three from unexplored clades, expands the AA7-substrate range and unveils a cellooligosaccharide dehydrogenase activity, previously unknown within AA7. Sequence and structural analyses identify unique signatures distinguishing the strict dehydrogenase clade from canonical AA7 oxidases. The discovered dehydrogenase directly is able to transfer electrons to an AA9 lytic polysaccharide monooxygenase (LPMO) and fuel cellulose degradation by LPMOs without exogenous reductants. The expansion of redox-profiles and substrate range highlights the functional diversity within AA7 and sets the stage for harnessing AA7 dehydrogenases to fine-tune LPMO activity in biotechnological conversion of plant feedstocks.
UR - http://www.scopus.com/inward/record.url?scp=85104136135&partnerID=8YFLogxK
U2 - 10.1038/s41467-021-22372-0
DO - 10.1038/s41467-021-22372-0
M3 - Article
C2 - 33837197
AN - SCOPUS:85104136135
SN - 2041-1723
VL - 12
JO - Nature Communications
JF - Nature Communications
IS - 1
M1 - 2132
ER -