On the roles of AA15 lytic polysaccharide monooxygenases derived from the termite Coptotermes gestroi.

Animals Copper / chemistry Insect Proteins / chemistry Isoptera / enzymology Mixed Function Oxygenases / chemistry Models, Molecular
AA15 CAZymes Chitin Chitinases LPMOs Termites

Journal

Journal of inorganic biochemistry
ISSN: 1873-3344
Titre abrégé: J Inorg Biochem
Pays: United States
ID NLM: 7905788

Informations de publication

Date de publication:
03 2021
Historique:
received: 29 07 2020
revised: 18 11 2020
accepted: 18 11 2020
pubmed: 10 1 2021
medline: 1 10 2021
entrez: 9 1 2021
Statut: ppublish

Résumé

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. Using ascorbate and O

Identifiants

DOI: 10.1016/j.jinorgbio.2020.111316 PMID: 33421883
pubmed: 33421883
pii: S0162-0134(20)30344-5
doi: 10.1016/j.jinorgbio.2020.111316
pii:
doi:

Substances chimiques

Insect Proteins 0
Copper 789U1901C5
Mixed Function Oxygenases EC 1.-

Types de publication

Journal Article Research Support, Non-U.S. Gov't Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

111316

Informations de copyright

Copyright © 2020. Published by Elsevier Inc.

Auteurs

João Paulo L Franco Cairo (JPL)

Department of Biochemistry and Tissue Biology, Institute of Biology, University of Campinas, Campinas, SP, Brazil; Department of Chemistry, University of York, Heslington, York, United Kingdom; Programa de Processos Tecnológicos e Ambientais, Universidade de Sorocaba - UNISO, Sorocaba, SP, Brazil.

David Cannella (D)

PhotoBioCatalysis Unit, Crop Production and Biocatalysis - CPBL, Biomass Transformation lab - BTL, Interfaculty School of Bioengineers, Université Libre de Bruxelles, Belgium.

Leandro C Oliveira (LC)

Department of Physics - Institute of Biosciences, Humanities and Exact Sciences, São Paulo State University (UNESP), São José do Rio Preto, SP, Brazil.

Thiago A Gonçalves (TA)

Department of Biochemistry and Tissue Biology, Institute of Biology, University of Campinas, Campinas, SP, Brazil; Programa de Processos Tecnológicos e Ambientais, Universidade de Sorocaba - UNISO, Sorocaba, SP, Brazil.

Marcelo V Rubio (MV)

Department of Biochemistry and Tissue Biology, Institute of Biology, University of Campinas, Campinas, SP, Brazil.

Cesar R F Terrasan (CRF)

Department of Biochemistry and Tissue Biology, Institute of Biology, University of Campinas, Campinas, SP, Brazil.

Robson Tramontina (R)

Programa de Processos Tecnológicos e Ambientais, Universidade de Sorocaba - UNISO, Sorocaba, SP, Brazil.

Luciana S Mofatto (LS)

Department of Genetic, Evolution and Bioagents, Institute of Biology, University of Campinas, Campinas, SP, Brazil.

Marcelo F Carazzolle (MF)

Department of Genetic, Evolution and Bioagents, Institute of Biology, University of Campinas, Campinas, SP, Brazil.

Wanius Garcia (W)

Centro de Ciências Naturais e Humanas, Universidade Federal do ABC (UFABC), Santo André, SP, Brazil.

Claus Felby (C)

Department of Geosciences and Natural Resource Management, Faculty of Science, University of Copenhagen, Frederiksberg C, Denmark.

André Damasio (A)

Department of Biochemistry and Tissue Biology, Institute of Biology, University of Campinas, Campinas, SP, Brazil; São Paulo Fungal Group, Brazil.

Paul H Walton (PH)

Department of Chemistry, University of York, Heslington, York, United Kingdom. Electronic address: paul.walton@york.ac.uk.

Fabio Squina (F)

Programa de Processos Tecnológicos e Ambientais, Universidade de Sorocaba - UNISO, Sorocaba, SP, Brazil. Electronic address: fabio.squina@gmail.com.

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Classifications MeSH

questionsmedicales.fr › Eucaryotes › Animaux › On the roles of AA15 lytic polysaccharide...
questionsmedicales.fr › Produits chimiques inorganiques › Métaux › Métaux lourds › Cuivre › On the roles of AA15 lytic polysaccharide...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines d'arthropode › Protéines d'insecte › On the roles of AA15 lytic polysaccharide...
questionsmedicales.fr › Eucaryotes › Animaux › Invertébrés › Arthropodes › Insectes › Isoptera › On the roles of AA15 lytic polysaccharide...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Oxidoreductases › Oxygénases › Mixed function oxygenases › On the roles of AA15 lytic polysaccharide...
questionsmedicales.fr › Techniques d'investigation › Modèles théoriques › Modèles moléculaires › On the roles of AA15 lytic polysaccharide...