Structural and electronic determinants of lytic polysaccharide monooxygenase reactivity on polysaccharide substrates

T. J. Simmons, K. E. H. Frandsen, L. Ciano, T. Tryfona, N. Lenfant, J. C. Poulsen, L. F. L. Wilson, T. Tandrup, M. Tovborg, K. Schnorr, K. S. Johansen, B. Henrissat, P. H. Walton, L Lo Leggio () and P. Dupree ()
Additional contact information
T. J. Simmons: University of Cambridge
K. E. H. Frandsen: UMR 1163 BBF (Biodiversité et Biotechnologie Fongiques)
L. Ciano: University of York
T. Tryfona: University of Cambridge
N. Lenfant: CNRS, Aix-Marseille Université
J. C. Poulsen: University of Copenhagen
L. F. L. Wilson: University of Cambridge
T. Tandrup: University of Copenhagen
M. Tovborg: Novozymes A/S
K. Schnorr: Novozymes A/S
K. S. Johansen: Copenhagen University
B. Henrissat: CNRS, Aix-Marseille Université
P. H. Walton: University of York
L Lo Leggio: University of Copenhagen
P. Dupree: University of Cambridge

Nature Communications, 2017, vol. 8, issue 1, 1-12

Abstract: Abstract Lytic polysaccharide monooxygenases (LPMOs) are industrially important copper-dependent enzymes that oxidatively cleave polysaccharides. Here we present a functional and structural characterization of two closely related AA9-family LPMOs from Lentinus similis (LsAA9A) and Collariella virescens (CvAA9A). LsAA9A and CvAA9A cleave a range of polysaccharides, including cellulose, xyloglucan, mixed-linkage glucan and glucomannan. LsAA9A additionally cleaves isolated xylan substrates. The structures of CvAA9A and of LsAA9A bound to cellulosic and non-cellulosic oligosaccharides provide insight into the molecular determinants of their specificity. Spectroscopic measurements reveal differences in copper co-ordination upon the binding of xylan and glucans. LsAA9A activity is less sensitive to the reducing agent potential when cleaving xylan, suggesting that distinct catalytic mechanisms exist for xylan and glucan cleavage. Overall, these data show that AA9 LPMOs can display different apparent substrate specificities dependent upon both productive protein–carbohydrate interactions across a binding surface and also electronic considerations at the copper active site.

Date: 2017
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-017-01247-3 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-01247-3

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-017-01247-3

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().