First evidence of cholinesterase-like activity in Basidiomycota.


Journal

PloS one
ISSN: 1932-6203
Titre abrégé: PLoS One
Pays: United States
ID NLM: 101285081

Informations de publication

Date de publication:
2019
Historique:
received: 26 02 2019
accepted: 13 04 2019
entrez: 1 5 2019
pubmed: 1 5 2019
medline: 9 1 2020
Statut: epublish

Résumé

Cholinesterases (ChE), the enzymes whose primary function is the hydrolysis of choline esters, are widely expressed throughout the nature. Although they have already been found in plants and microorganisms, including ascomycete fungi, this study is the first report of ChE-like activity in fungi of the phylum Basidiomycota. This activity was detected in almost a quarter of the 45 tested aqueous fungal extracts. The ability of these extracts to hydrolyse acetylthiocholine was about ten times stronger than the hydrolytic activity towards butyrylthiocholine and propionylthiocholine. In-gel detection of ChE-like activity with acetylthiocholine indicated a great variability in the characteristics of these enzymes which are not characterized as vertebrate-like based on (i) differences in inhibition by excess substrate, (ii) susceptibility to different vertebrate acetylcholinesterase and butyrylcholinesterase inhibitors, and (iii) a lack of orthologs using phylogenetic analysis. Limited inhibition by single inhibitors and multiple activity bands using in-gel detection indicate the presence of several ChE-like enzymes in these aqueous extracts. We also observed inhibitory activity of the same aqueous mushroom extracts against insect acetylcholinesterase in 10 of the 45 samples tested; activity was independent of the presence of ChE-like activity in extracts. Both ChE-like activities with different substrates and the ability of extracts to inhibit insect acetylcholinesterase were not restricted to any fungal family but were rather present across all included Basidiomycota families. This study can serve as a platform for further research regarding ChE activity in mushrooms.

Identifiants

pubmed: 31039204
doi: 10.1371/journal.pone.0216077
pii: PONE-D-19-05648
pmc: PMC6490906
doi:

Substances chimiques

Cholinesterase Inhibitors 0
Lipase EC 3.1.1.3
Cholinesterases EC 3.1.1.8

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

e0216077

Déclaration de conflit d'intérêts

The authors have declared that no competing interests exist.

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Auteurs

Kristina Sepčić (K)

Department of Biology, Biotechnical Faculty, University of Ljubljana, Ljubljana, Slovenia.

Jerica Sabotič (J)

Department of Biotechnology, Jožef Stefan Institute, Ljubljana, Slovenia.

Robin A Ohm (R)

Department of Biology, Faculty of Science, Utrecht University, Padualaan, Utrecht, The Netherlands.

Damjana Drobne (D)

Department of Biology, Biotechnical Faculty, University of Ljubljana, Ljubljana, Slovenia.

Anita Jemec Kokalj (A)

Department of Biology, Biotechnical Faculty, University of Ljubljana, Ljubljana, Slovenia.

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Classifications MeSH