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The influence of ortho- and para-diphenoloxidase substrates on pigment formation in black yeast-like fungi

Dothideaceous black yeast-like fungi (BYF) are known to synthesise DHN-melanin that is inhibited by the systemic fungicide tricyclazole. The final step of the DHN melanin pathway is the conjoining of 1,8-DHN molecules to form the melanin polymer. There are several candidate enzymes for this step, in...

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Autores principales: Yurlova, N.A., de Hoog, G.S., Fedorova, L.G.
Formato: Texto
Lenguaje:English
Publicado: CBS Fungal Biodiversity Centre 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2610312/
https://www.ncbi.nlm.nih.gov/pubmed/19287525
http://dx.doi.org/10.3114/sim.2008.61.03
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author Yurlova, N.A.
de Hoog, G.S.
Fedorova, L.G.
author_facet Yurlova, N.A.
de Hoog, G.S.
Fedorova, L.G.
author_sort Yurlova, N.A.
collection PubMed
description Dothideaceous black yeast-like fungi (BYF) are known to synthesise DHN-melanin that is inhibited by the systemic fungicide tricyclazole. The final step of the DHN melanin pathway is the conjoining of 1,8-DHN molecules to form the melanin polymer. There are several candidate enzymes for this step, including phenoloxidases such as tyrosinase and laccases, peroxidases, and perhaps also catalases. We analysed the type polyphenoloxidases that are involved in biosynthesis of BYF melanins. For that purpose we used substrates of o-diphenoloxidases (EC 1.10.3.1.): 4-hydroxyphenyl-pyruvic acid, L-β-phenyllactic acid, tyrosine, pyrocatechol, 3,4-dihydroxyphenylalanine and homogentisic acid, as well as substrates of p-diphenoloxidases (EC 1.10.3.2.): syringaldazine, resorcinol, p-phenylenediamine, phloroglucinol, guaiacol and pyrogallic acid. Fourteen strains of black yeasts originating from different natural biotopes were investigated. The tested strains could be divided into four groups based on their ability to produce dark pigments when cultivated on aromatic substrates of o- and on p-diphenoloxidases. It was established that syringaldazine, pyrogallic acid and 4-hydrophenyl-pyruvic acid, β-phenyllactic acid optimally promote melanin biosynthesis. Average intensity of pigmentation of all strains studied was minimal when guaiacol was used as a substrate. The present investigation indicates that the melanisation process may involve more enzymes and more substrates than those commonly recognised. Black yeasts are likely to contain a multipotent polyphenoloxidase.
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spelling pubmed-26103122009-03-13 The influence of ortho- and para-diphenoloxidase substrates on pigment formation in black yeast-like fungi Yurlova, N.A. de Hoog, G.S. Fedorova, L.G. Stud Mycol Articles Dothideaceous black yeast-like fungi (BYF) are known to synthesise DHN-melanin that is inhibited by the systemic fungicide tricyclazole. The final step of the DHN melanin pathway is the conjoining of 1,8-DHN molecules to form the melanin polymer. There are several candidate enzymes for this step, including phenoloxidases such as tyrosinase and laccases, peroxidases, and perhaps also catalases. We analysed the type polyphenoloxidases that are involved in biosynthesis of BYF melanins. For that purpose we used substrates of o-diphenoloxidases (EC 1.10.3.1.): 4-hydroxyphenyl-pyruvic acid, L-β-phenyllactic acid, tyrosine, pyrocatechol, 3,4-dihydroxyphenylalanine and homogentisic acid, as well as substrates of p-diphenoloxidases (EC 1.10.3.2.): syringaldazine, resorcinol, p-phenylenediamine, phloroglucinol, guaiacol and pyrogallic acid. Fourteen strains of black yeasts originating from different natural biotopes were investigated. The tested strains could be divided into four groups based on their ability to produce dark pigments when cultivated on aromatic substrates of o- and on p-diphenoloxidases. It was established that syringaldazine, pyrogallic acid and 4-hydrophenyl-pyruvic acid, β-phenyllactic acid optimally promote melanin biosynthesis. Average intensity of pigmentation of all strains studied was minimal when guaiacol was used as a substrate. The present investigation indicates that the melanisation process may involve more enzymes and more substrates than those commonly recognised. Black yeasts are likely to contain a multipotent polyphenoloxidase. CBS Fungal Biodiversity Centre 2008 /pmc/articles/PMC2610312/ /pubmed/19287525 http://dx.doi.org/10.3114/sim.2008.61.03 Text en Copyright © Copyright 2008 CBS Fungal Biodiversity Centre You are free to share - to copy, distribute and transmit the work, under the following conditions: Attribution:  You must attribute the work in the manner specified by the author or licensor (but not in any way that suggests that they endorse you or your use of the work). Non-commercial:  You may not use this work for commercial purposes. No derivative works:  You may not alter, transform, or build upon this work. For any reuse or distribution, you must make clear to others the license terms of this work, which can be found at http://creativecommons.org/licenses/by-nc-nd/3.0/legalcode. (http://creativecommons.org/licenses/by-nc-nd/3.0/legalcode) Any of the above conditions can be waived if you get permission from the copyright holder. Nothing in this license impairs or restricts the author's moral rights.
spellingShingle Articles
Yurlova, N.A.
de Hoog, G.S.
Fedorova, L.G.
The influence of ortho- and para-diphenoloxidase substrates on pigment formation in black yeast-like fungi
title The influence of ortho- and para-diphenoloxidase substrates on pigment formation in black yeast-like fungi
title_full The influence of ortho- and para-diphenoloxidase substrates on pigment formation in black yeast-like fungi
title_fullStr The influence of ortho- and para-diphenoloxidase substrates on pigment formation in black yeast-like fungi
title_full_unstemmed The influence of ortho- and para-diphenoloxidase substrates on pigment formation in black yeast-like fungi
title_short The influence of ortho- and para-diphenoloxidase substrates on pigment formation in black yeast-like fungi
title_sort influence of ortho- and para-diphenoloxidase substrates on pigment formation in black yeast-like fungi
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2610312/
https://www.ncbi.nlm.nih.gov/pubmed/19287525
http://dx.doi.org/10.3114/sim.2008.61.03
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