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Strategies to Better Target Fungal Squalene Monooxygenase

Fungal pathogens present a challenge in medicine and agriculture. They also harm ecosystems and threaten biodiversity. The allylamine class of antimycotics targets the enzyme squalene monooxygenase. This enzyme occupies a key position in the sterol biosynthesis pathway in eukaryotes, catalyzing the...

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Autor principal: Sagatova, Alia A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7828399/
https://www.ncbi.nlm.nih.gov/pubmed/33450973
http://dx.doi.org/10.3390/jof7010049
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author Sagatova, Alia A.
author_facet Sagatova, Alia A.
author_sort Sagatova, Alia A.
collection PubMed
description Fungal pathogens present a challenge in medicine and agriculture. They also harm ecosystems and threaten biodiversity. The allylamine class of antimycotics targets the enzyme squalene monooxygenase. This enzyme occupies a key position in the sterol biosynthesis pathway in eukaryotes, catalyzing the rate-limiting reaction by introducing an oxygen atom to the squalene substrate converting it to 2,3-oxidosqualene. Currently, terbinafine—the most widely used allylamine—is mostly used for treating superficial fungal infections. The ability to better target this enzyme will have significant implications for human health in the treatment of fungal infections. The human orthologue can also be targeted for cholesterol-lowering therapeutics and in cancer therapies. This review will focus on the structural basis for improving the current therapeutics for fungal squalene monooxygenase.
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spelling pubmed-78283992021-01-25 Strategies to Better Target Fungal Squalene Monooxygenase Sagatova, Alia A. J Fungi (Basel) Review Fungal pathogens present a challenge in medicine and agriculture. They also harm ecosystems and threaten biodiversity. The allylamine class of antimycotics targets the enzyme squalene monooxygenase. This enzyme occupies a key position in the sterol biosynthesis pathway in eukaryotes, catalyzing the rate-limiting reaction by introducing an oxygen atom to the squalene substrate converting it to 2,3-oxidosqualene. Currently, terbinafine—the most widely used allylamine—is mostly used for treating superficial fungal infections. The ability to better target this enzyme will have significant implications for human health in the treatment of fungal infections. The human orthologue can also be targeted for cholesterol-lowering therapeutics and in cancer therapies. This review will focus on the structural basis for improving the current therapeutics for fungal squalene monooxygenase. MDPI 2021-01-13 /pmc/articles/PMC7828399/ /pubmed/33450973 http://dx.doi.org/10.3390/jof7010049 Text en © 2021 by the author. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Sagatova, Alia A.
Strategies to Better Target Fungal Squalene Monooxygenase
title Strategies to Better Target Fungal Squalene Monooxygenase
title_full Strategies to Better Target Fungal Squalene Monooxygenase
title_fullStr Strategies to Better Target Fungal Squalene Monooxygenase
title_full_unstemmed Strategies to Better Target Fungal Squalene Monooxygenase
title_short Strategies to Better Target Fungal Squalene Monooxygenase
title_sort strategies to better target fungal squalene monooxygenase
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7828399/
https://www.ncbi.nlm.nih.gov/pubmed/33450973
http://dx.doi.org/10.3390/jof7010049
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