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Identification of β-phenylalanine as a non-protein amino acid in cultivated rice, Oryza sativa

Non-protein amino acids, often analogs of the standard 20 protein amino acids, have been discovered in many plant species. Recent research with cultivated rice (Oryza sativa) identified (3R)-β-tyrosine, as well as a tyrosine amino mutase that synthesizes (3R)-β-tyrosine from the protein amino acid (...

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Autores principales: Yokoo, Takayuki, Takata, Ryo, Yan, Jian, Matsumoto, Fuka, Teraishi, Masayoshi, Okumoto, Yutaka, Jander, Georg, Mori, Naoki
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4802750/
https://www.ncbi.nlm.nih.gov/pubmed/27066169
http://dx.doi.org/10.1080/19420889.2015.1086045
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author Yokoo, Takayuki
Takata, Ryo
Yan, Jian
Matsumoto, Fuka
Teraishi, Masayoshi
Okumoto, Yutaka
Jander, Georg
Mori, Naoki
author_facet Yokoo, Takayuki
Takata, Ryo
Yan, Jian
Matsumoto, Fuka
Teraishi, Masayoshi
Okumoto, Yutaka
Jander, Georg
Mori, Naoki
author_sort Yokoo, Takayuki
collection PubMed
description Non-protein amino acids, often analogs of the standard 20 protein amino acids, have been discovered in many plant species. Recent research with cultivated rice (Oryza sativa) identified (3R)-β-tyrosine, as well as a tyrosine amino mutase that synthesizes (3R)-β-tyrosine from the protein amino acid (2S)-α-tyrosine. Gas chromatography-mass spectrometry (GC-MS) assays and comparison to an authentic standard showed that β-phenylalanine is also a relatively abundant non-protein amino acid in rice leaves and that its biosynthesis occurs independently from that of β-tyrosine.
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spelling pubmed-48027502016-04-08 Identification of β-phenylalanine as a non-protein amino acid in cultivated rice, Oryza sativa Yokoo, Takayuki Takata, Ryo Yan, Jian Matsumoto, Fuka Teraishi, Masayoshi Okumoto, Yutaka Jander, Georg Mori, Naoki Commun Integr Biol Article Addendum Non-protein amino acids, often analogs of the standard 20 protein amino acids, have been discovered in many plant species. Recent research with cultivated rice (Oryza sativa) identified (3R)-β-tyrosine, as well as a tyrosine amino mutase that synthesizes (3R)-β-tyrosine from the protein amino acid (2S)-α-tyrosine. Gas chromatography-mass spectrometry (GC-MS) assays and comparison to an authentic standard showed that β-phenylalanine is also a relatively abundant non-protein amino acid in rice leaves and that its biosynthesis occurs independently from that of β-tyrosine. Taylor & Francis 2015-09-25 /pmc/articles/PMC4802750/ /pubmed/27066169 http://dx.doi.org/10.1080/19420889.2015.1086045 Text en © 2015 The Author(s). Published with license by Taylor & Francis Group, LLC 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. The moral rights of the named author(s) have been asserted.
spellingShingle Article Addendum
Yokoo, Takayuki
Takata, Ryo
Yan, Jian
Matsumoto, Fuka
Teraishi, Masayoshi
Okumoto, Yutaka
Jander, Georg
Mori, Naoki
Identification of β-phenylalanine as a non-protein amino acid in cultivated rice, Oryza sativa
title Identification of β-phenylalanine as a non-protein amino acid in cultivated rice, Oryza sativa
title_full Identification of β-phenylalanine as a non-protein amino acid in cultivated rice, Oryza sativa
title_fullStr Identification of β-phenylalanine as a non-protein amino acid in cultivated rice, Oryza sativa
title_full_unstemmed Identification of β-phenylalanine as a non-protein amino acid in cultivated rice, Oryza sativa
title_short Identification of β-phenylalanine as a non-protein amino acid in cultivated rice, Oryza sativa
title_sort identification of β-phenylalanine as a non-protein amino acid in cultivated rice, oryza sativa
topic Article Addendum
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4802750/
https://www.ncbi.nlm.nih.gov/pubmed/27066169
http://dx.doi.org/10.1080/19420889.2015.1086045
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