Structural dissection of two redox proteins from the shipworm symbiont Teredinibacter turnerae

Autor: Badri S. Rajagopal, Nick Yates, Jake Smith, Alessandro Paradisi, Catherine Tétard-Jones, William G. T. Willats, Susan Marcus, J. Paul Knox, Mohd Firdaus-Raih, Bernard Henrissat, Gideon J. Davies, Paul H. Walton, Alison Parkin, Glyn R. Hemsworth

Publikováno v: IUCrJ, Vol 11, Iss 2, Pp 260-274 (2024)

The discovery of lytic polysaccharide monooxygenases (LPMOs), a family of copper-dependent enzymes that play a major role in polysaccharide degradation, has revealed the importance of oxidoreductases in the biological utilization of biomass. In fungi

Externí odkaz: https://doaj.org/article/5416359705ac4bb7868e9c0558924d6d

Deletion of AA9 Lytic Polysaccharide Monooxygenases Impacts A. nidulans Secretome and Growth on Lignocellulose

Autor: César Rafael Fanchini Terrasan, Marcelo Ventura Rubio, Jaqueline Aline Gerhardt, João Paulo Franco Cairo, Fabiano Jares Contesini, Mariane Paludetti Zubieta, Fernanda Lopes de Figueiredo, Fernanda Lima Valadares, Thamy Lívia Ribeiro Corrêa, Mario Tyago Murakami, Telma Teixeira Franco, Gideon J. Davies, Paul H. Walton, Andre Damasio

Publikováno v: Microbiology Spectrum, Vol 10, Iss 3 (2022)

ABSTRACT Lytic polysaccharide monooxygenases (LPMOs) are oxidative enzymes found in viruses, archaea, and bacteria as well as eukaryotes, such as fungi, algae and insects, actively contributing to the degradation of different polysaccharides. In Aspe

Externí odkaz: https://doaj.org/article/1194f219026e4fe2afc2b9e41095ea91

The histidine brace: nature's copper alternative to haem?

Autor: Paul H. Walton, Gideon J. Davies, Daniel E. Diaz, João P. Franco‐Cairo

Publikováno v: FEBS Letters. 597:485-494

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::00b3796dbc21014ff090311a22ac94c6
https://doi.org/10.1002/1873-3468.14579

Structural perturbations of substrate binding and oxidation state changes in a lytic polysaccharide monooxygenase

Autor: Paul H, Walton, Gideon J, Davies

Publikováno v: JBIC Journal of Biological Inorganic Chemistry. 27:705-713

LPMOs are enzymes which catalyse the oxidation of a C-H bond within polysaccharides, leading to their oxidative cleavage. To achieve this, LPMOs employ highly reactive oxidising intermediates, the generation of which is likely coupled to substrate bi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8fdb1c9b71ec8055d58c13aa5fc00f36
https://doi.org/10.1007/s00775-022-01966-z

Oxidative cleavage of polysaccharides by a termite-derived superoxide dismutase boosts the degradation of biomass by glycoside hydrolases

Autor: João Paulo L. Franco Cairo, Fernanda Mandelli, Robson Tramontina, David Cannella, Alessandro Paradisi, Luisa Ciano, Marcel R. Ferreira, Marcelo V. Liberato, Lívia B. Brenelli, Thiago A. Gonçalves, Gisele N. Rodrigues, Thabata M. Alvarez, Luciana S. Mofatto, Marcelo F. Carazzolle, José G. C. Pradella, Adriana F. Paes Leme, Ana M. Costa-Leonardo, Mário Oliveira-Neto, André Damasio, Gideon J. Davies, Claus Felby, Paul H. Walton, Fabio M. Squina

Publikováno v: Franco Cairo, J P L, Mandelli, F, Tramontina, R, Cannella, D, Paradisi, A, Ciano, L, Ferreira, M R, Liberato, M V, Brenelli, L B, Goncalves, T A, Rodrigues, G N, Alvarez, T M, Mofatto, L S, Carazzolle, M F, Pradella, J G C, Leme, A F P, Costa-Leonardo, A M, Oliveira-Neto, M, Damasio, A, Davies, G J, Felby, C, Walton, P H & Squina, F M 2022, ' Oxidative cleavage of polysaccharides by a termite-derived superoxide dismutase boosts the degradation of biomass by glycoside hydrolases ', Green Chemistry, vol. 24, no. 12, pp. 4845-4858 . https://doi.org/10.1039/d1gc04519a

Wood-feeding termites effectively degrade plant biomass through enzymatic degradation. Despite their high efficiencies, however, individual glycoside hydrolases isolated from termites and their symbionts exhibit anomalously low effectiveness in ligno

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6bec8f2b4a169d8b8859cf96836695d
https://doi.org/10.1039/d1gc04519a