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

Couturier, Marie ; Roussel, Alain ; Rosengren, Anna LU ; Leone, Philippe ; Stålbrand, Henrik LU and Berrin, Jean-Guy (2013) In Journal of Biological Chemistry 288(20). p.14624-14635
Abstract
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... (More)
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. (Less)
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
288
issue
20
pages
14624 - 14635
publisher
American Society for Biochemistry and Molecular Biology
external identifiers
  • wos:000319253500062
  • scopus:84877890782
ISSN
1083-351X
DOI
10.1074/jbc.M113.459438
language
English
LU publication?
yes
id
927ac470-ecd8-4cb1-a23e-6a1d45919023 (old id 3931125)
date added to LUP
2016-04-01 10:54:19
date last changed
2022-04-04 22:25:02
@article{927ac470-ecd8-4cb1-a23e-6a1d45919023,
  abstract     = {{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.}},
  author       = {{Couturier, Marie and Roussel, Alain and Rosengren, Anna and Leone, Philippe and Stålbrand, Henrik and Berrin, Jean-Guy}},
  issn         = {{1083-351X}},
  language     = {{eng}},
  number       = {{20}},
  pages        = {{14624--14635}},
  publisher    = {{American Society for Biochemistry and Molecular Biology}},
  series       = {{Journal of Biological Chemistry}},
  title        = {{Structural and Biochemical Analyses of Glycoside Hydrolase Families 5 and 26 beta-(1,4)-Mannanases from Podospora anserina Reveal Differences upon Manno-oligosaccharide Catalysis}},
  url          = {{http://dx.doi.org/10.1074/jbc.M113.459438}},
  doi          = {{10.1074/jbc.M113.459438}},
  volume       = {{288}},
  year         = {{2013}},
}