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Fungal and Plant Phenylalanine Ammonia-lyase

L-Phenylalanine is one of the essential amino acids that cannot be synthesized in mammals in adequate amounts to meet the requirements for protein synthesis. Fungi and plants are able to synthesize phenylalanine via the shikimic acid pathway. L-Phenylalanine, derived from the shikimic acid pathway,...

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Autores principales: Hyun, Min Woo, Yun, Yeo Hong, Kim, Jun Young, Kim, Seong Hwan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Korean Society of Mycology 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3385129/
https://www.ncbi.nlm.nih.gov/pubmed/22783113
http://dx.doi.org/10.5941/MYCO.2011.39.4.257
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author Hyun, Min Woo
Yun, Yeo Hong
Kim, Jun Young
Kim, Seong Hwan
author_facet Hyun, Min Woo
Yun, Yeo Hong
Kim, Jun Young
Kim, Seong Hwan
author_sort Hyun, Min Woo
collection PubMed
description L-Phenylalanine is one of the essential amino acids that cannot be synthesized in mammals in adequate amounts to meet the requirements for protein synthesis. Fungi and plants are able to synthesize phenylalanine via the shikimic acid pathway. L-Phenylalanine, derived from the shikimic acid pathway, is used directly for protein synthesis in plants or metabolized through the phenylpropanoid pathway. This phenylpropanoid metabolism leads to the biosynthesis of a wide array of phenylpropanoid secondary products. The first step in this metabolic sequence involves the action of phenylalanine ammonia-lyase (PAL). The discovery of PAL enzyme in fungi and the detection of (14)CO(2) production from (14)C-ring-labeled phenylalanine and cinnamic acid demonstrated that certain fungi can degrade phenylalanine by a pathway involving an initial deamination to cinnamic acid, as happens in plants. In this review, we provide background information on PAL and a recent update on the presence of PAL genes in fungi.
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spelling pubmed-33851292012-07-10 Fungal and Plant Phenylalanine Ammonia-lyase Hyun, Min Woo Yun, Yeo Hong Kim, Jun Young Kim, Seong Hwan Mycobiology Review Article L-Phenylalanine is one of the essential amino acids that cannot be synthesized in mammals in adequate amounts to meet the requirements for protein synthesis. Fungi and plants are able to synthesize phenylalanine via the shikimic acid pathway. L-Phenylalanine, derived from the shikimic acid pathway, is used directly for protein synthesis in plants or metabolized through the phenylpropanoid pathway. This phenylpropanoid metabolism leads to the biosynthesis of a wide array of phenylpropanoid secondary products. The first step in this metabolic sequence involves the action of phenylalanine ammonia-lyase (PAL). The discovery of PAL enzyme in fungi and the detection of (14)CO(2) production from (14)C-ring-labeled phenylalanine and cinnamic acid demonstrated that certain fungi can degrade phenylalanine by a pathway involving an initial deamination to cinnamic acid, as happens in plants. In this review, we provide background information on PAL and a recent update on the presence of PAL genes in fungi. The Korean Society of Mycology 2011-12 2011-12-07 /pmc/articles/PMC3385129/ /pubmed/22783113 http://dx.doi.org/10.5941/MYCO.2011.39.4.257 Text en © The Korean Society of Mycology http://creativecommons.org/licenses/by-nc/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Hyun, Min Woo
Yun, Yeo Hong
Kim, Jun Young
Kim, Seong Hwan
Fungal and Plant Phenylalanine Ammonia-lyase
title Fungal and Plant Phenylalanine Ammonia-lyase
title_full Fungal and Plant Phenylalanine Ammonia-lyase
title_fullStr Fungal and Plant Phenylalanine Ammonia-lyase
title_full_unstemmed Fungal and Plant Phenylalanine Ammonia-lyase
title_short Fungal and Plant Phenylalanine Ammonia-lyase
title_sort fungal and plant phenylalanine ammonia-lyase
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3385129/
https://www.ncbi.nlm.nih.gov/pubmed/22783113
http://dx.doi.org/10.5941/MYCO.2011.39.4.257
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