ArticleBioMed research international2014
A novel laccase with potent antiproliferative and HIV-1 reverse transcriptase inhibitory activities from mycelia of mushroom Coprinus comatus.
Article in BioMed research international, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 43 citations in OpenAlex.
- Harnessing the Nutritional Value, Therapeutic Applications, and Environmental Impact of Mushrooms.Food science & nutrition · 2025Review
- Unlocking the Power: New Insights into the Anti-Aging Properties of Mushrooms.Journal of fungi (Basel, Switzerland) · 2024Review
- Transcriptome analysis of genes associated with autolysis of Coprinus comatus.Scientific reports · 2022Article
- Narrative Review: Bioactive Potential of Various Mushrooms as the Treasure of Versatile Therapeutic Natural Product.Journal of fungi (Basel, Switzerland) · 2021Review
- Natural Products with Inhibitory Activity against Human Immunodeficiency Virus Type 1.Advances in virology · 2021Review
- The two faces of Coprinus comatus-Functional properties and potential hazards.Phytotherapy research : PTR · 2020Review
- The antioxidant activities of alkalic-extractable polysaccharides from Coprinus comatus on alcohol-induced liver injury in mice.Scientific reports · 2018Article
- A comparative overview of antioxidative properties and phenolic profiles of different fungal origins: fruiting bodies and submerged cultures ofJournal of food science and technology · 2017Article
- Purification and Characterization of a White Laccase with Pronounced Dye Decolorizing Ability and HIV-1 Reverse Transcriptase Inhibitory Activity from Lepista nuda.Molecules (Basel, Switzerland) · 2016Article
- How to enjoy laccases.Cellular and molecular life sciences : CMLS · 2015Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A novel laccase was isolated and purified from fermentation mycelia of mushroom Coprinus comatus with an isolation procedure including three ion-exchange chromatography steps on DEAE-cellulose, CM-cellulose, and Q-Sepharose and one gel-filtration step by fast protein liquid chromatography on Superdex 75. The purified enzyme was a monomeric protein with a molecular weight of 64 kDa. It possessed a unique N-terminal amino acid sequence of AIGPVADLKV, which has considerably high sequence similarity with that of other fungal laccases, but is different from that of C. comatus laccases reported. The enzyme manifested an optimal pH value of 2.0 and an optimal temperature of 60°C using 2,2'-azinobis(3-ethylbenzothiazolone-6-sulfonic acid) diammonium salt (ABTS) as the substrate. The laccase displayed, at pH 2.0 and 37°C, K(m) values of 1.59 mM towards ABTS. It potently suppressed proliferation of tumor cell lines HepG2 and MCF7, and inhibited human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) with an IC50 value of 3.46 μM, 4.95 μM, and 5.85 μM, respectively, signifying that it is an antipathogenic protein.
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