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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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Detalles Bibliográficos
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
Descripción
Sumario: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.