Abstract
Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes which catalyze the oxidative cleavage of polysaccharides. LPMOs belonging to family 15 in the Auxiliary Activity (AA) class from the Carbohydrate-Active Enzyme database are found widespread across the Tree of Life, including viruses, algae, oomycetes and animals. Recently, two AA15s from the firebrat Thermobia domestica were reported to have oxidative activity, one towards cellulose or chitin and the other towards chitin, signalling that AA15 LPMOs from insects potentially have different biochemical functions. Herein, we report the identification and characterization of two family AA15 members from the lower termite Coptotermes gestroi. Addition of Cu(II) to CgAA15a or CgAA15b had a thermostabilizing effect on both.
Original language | English |
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Article number | 111316 |
Number of pages | 12 |
Journal | JOURNAL OF INORGANIC BIOCHEMISTRY |
Volume | 216 |
Early online date | 23 Nov 2020 |
DOIs | |
Publication status | Published - 6 Jan 2021 |
Bibliographical note
Funding Information:We would like to acknowledge professors Luisa Ciano and Gideon Davies as well as Dr. Alessandro Paradisi for supporting on experiments and for comments on the manuscript. We also would like to acknowledge Dr. Magdalena Calusinska for kindly provide the sequences of LPMOs AA15 from termites Cortaritermes sp. and Macrotermes natalensis. This research was supported by grants from Funda??o de Amparo ? Pesquisa do Estado de S?o Paulo - FAPESP (FMS 2015/50590?4; JPLFC 2016/09950?0; 2017/11952?3; WG 2017/17275?3; TAG 2017/16089?1; AD 2015/50612?8 and 2017/22669?0) and Conselho Nacional de Desenvolvimento Cient?fico e Tecnol?gico - CNPq. (FMS 428527/2018?3 and 305740/2017?2; WG 422132/2018?7; LCO 442352/2014?0; AD 404654/2018?5 and 304816/2017?5). We would like to acknowledge the MASS facility from Brazilian Biosciences National Laboratory (LNBio ? CNPEM) Campinas, SP, Brazil; the Analytic Center from the Institute of Chemistry from the State University of Campinas, Campinas, SP, Brazil; and the Technology Facility, Department of Biology, University of York, York, United Kingdom. The molecular dynamics simulations were performed at the Center for Scientific Computing (NCC/GridUNESP) of the S?o Paulo State University (UNESP) and CENAPAD-SP (Centro Nacional de Processamento de Alto Desempenho em S?o Paulo), project UNICAMP/FINEP-MCTII.
Funding Information:
We would like to acknowledge professors Luisa Ciano and Gideon Davies as well as Dr. Alessandro Paradisi for supporting on experiments and for comments on the manuscript. We also would like to acknowledge Dr. Magdalena Calusinska for kindly provide the sequences of LPMOs AA15 from termites Cortaritermes sp. and Macrotermes natalensis. This research was supported by grants from Fundação de Amparo à Pesquisa do Estado de São Paulo - FAPESP ( FMS 2015/50590–4 ; JPLFC 2016/09950–0 ; 2017/11952–3 ; WG 2017/17275–3 ; TAG 2017/16089–1 ; AD 2015/50612–8 and 2017/22669–0 ) and Conselho Nacional de Desenvolvimento Científico e Tecnológico - CNPq. ( FMS 428527/2018–3 and 305740/2017–2 ; WG 422132/2018–7 ; LCO 442352/2014–0 ; AD 404654/2018–5 and 304816/2017–5 ). We would like to acknowledge the MASS facility from Brazilian Biosciences National Laboratory (LNBio – CNPEM) Campinas, SP, Brazil; the Analytic Center from the Institute of Chemistry from the State University of Campinas, Campinas, SP, Brazil; and the Technology Facility, Department of Biology, University of York, York, United Kingdom. The molecular dynamics simulations were performed at the Center for Scientific Computing (NCC/GridUNESP) of the São Paulo State University (UNESP) and CENAPAD-SP (Centro Nacional de Processamento de Alto Desempenho em São Paulo), project UNICAMP/FINEP-MCTII.
Publisher Copyright:
© 2020
Copyright:
Copyright 2021 Elsevier B.V., All rights reserved.
Keywords
- AA15
- CAZymes
- Chitin
- Chitinases
- LPMOs
- Termites