Structural and Biochemical Analyses of Glycoside Hydrolase Families 5 and 26 beta-(1,4)-Mannanases from Podospora anserina Reveal Differences upon Manno-oligosaccharide Catalysis

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift


The microbial deconstruction of the plant cell wall is a key biological process that is of increasing importance with the development of a sustainable biofuel industry. The glycoside hydrolase families GH5 (PaMan5A) and GH26 (PaMan26A) endo-beta-1,4-mannanases from the coprophilic ascomycete Podospora anserina contribute to the enzymatic degradation of lignocellulosic biomass. In this study, P. anserina mannanases were further subjected to detailed comparative analysis of their substrate specificities, active site organization, and transglycosylation capacity. Although PaMan5A displays a classical mode of action, PaMan26A revealed an atypical hydrolysis pattern with the release of mannotetraose and mannose from mannopentaose resulting from a predominant binding mode involving the -4 subsite. The crystal structures of PaMan5A and PaMan26A were solved at 1.4 and 2.85 angstrom resolution, respectively. Analysis of the PaMan26A structure supported strong interaction with substrate at the -4 subsite mediated by two aromatic residues Trp-244 and Trp-245. The PaMan26A structure appended to its family 35 carbohydrate binding module revealed a short and proline-rich rigid linker that anchored together the catalytic and the binding modules.


  • Marie Couturier
  • Alain Roussel
  • Anna Rosengren
  • Philippe Leone
  • Henrik Stålbrand
  • Jean-Guy Berrin
Enheter & grupper

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Biologiska vetenskaper
Sidor (från-till)14624-14635
TidskriftJournal of Biological Chemistry
Utgåva nummer20
StatusPublished - 2013
Peer review utfördJa

Relaterad forskningsoutput

Anna Rosengren, 2014, Department of Chemistry, Lund University. 180 s.

Forskningsoutput: AvhandlingDoktorsavhandling (sammanläggning)

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