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                  <mods:namePart>El-Azaz-Ciudad, Jorge</mods:namePart>
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                  <mods:namePart>Cánovas-Ramos, Francisco Miguel</mods:namePart>
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                  <mods:namePart>De-la-Torre-Fazio, Fernando Nicolás</mods:namePart>
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                  <mods:namePart>Ávila-Sáez, Concepción</mods:namePart>
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                  <mods:dateAccessioned encoding="iso8601">2014-06-19T12:45:42Z</mods:dateAccessioned>
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               <mods:abstract>In plants, arogenate dehydratase activity (ADT, EC 4.2.1.91) is responsible for&#xd;
the last step in the main pathway for phenylalanine biosynthesis, known as the&#xd;
arogenate pathway, which consist in two steps: the conversion of prephenate to&#xd;
arogenate in a reaction catalyzed by the enzyme prephenate aminotransferase (PAT, EC&#xd;
2.6.1.78) and the decarboxylation of arogenate to render phenylalanine catalyzed by&#xd;
ADT. The arogenate pathway results of particular interest according to the important&#xd;
role of phenylalanine in plant metabolism, acting as the main gate of entry to&#xd;
phenylpropanoids biosynthesis, that constitute up to 30 to 45% of plant organic matter&#xd;
(Razal et al., 1996). This is particularly relevant in perennial woody plants, in which&#xd;
lignification process and resultant biomass acumulation through plant life cycle are&#xd;
notably important.&#xd;
Despite of the high importance of phenylalanine biosynthesis and derived&#xd;
phenylpropanoids in plants biology, the arogenate pathway still remains poorly&#xd;
characterized, particularly in woody plants. Very recently, two independent publications&#xd;
reported physiological evidences suggesting an alternative arogenate-independent&#xd;
pathway for phenylalanine biosynthesis in plants (Yoo et al., 2013; De la Torre et al.,&#xd;
2014), as described previously in fungi and bacteria. This pathway is dependent of a&#xd;
prephenate dehydratase enzyme (PDT, EC 4.2.1.51) catalyzing the conversion of&#xd;
prephenate to phenylpyruvate, being subsequently converted into phenylalanine through&#xd;
a transamination reaction. It has been reported that ADT and PDT activities are housed&#xd;
in the same proteins in plants (Cho et al., 2007).&#xd;
Here we present preliminary results focused on the characterization of the&#xd;
ADT/PDT gene family in maritime pine (Pinus pinaster Ait.), a conifer tree of&#xd;
ecological and commercial interest. Our results demonstrate the existence of at least 9&#xd;
ADT-like genes in the P. pinaster transcriptome, showing organ- and developmentspecific&#xd;
mRNA and protein expression profiles. Moreover, 3 of those 9 candidate genes&#xd;
present a distinctive phylogenetic clustering, forming a conifer-characteristic group of&#xd;
ADT-like genes differenced from the remaining ADT sequences. These findings&#xd;
highlights the potential importance of ADT/PDT activities in conifer metabolism,&#xd;
suggesting the existence of a singular and highly-specialized prephenate-related&#xd;
metabolism in conifers.&#xd;
Cho MH, Corea OR, Yang H, Bedgar DL, Laskar DD, Anterola AM, Moog-Anterola FA, Hood RL,&#xd;
Kohalmi SE, Bernards MA, Kang C, Davin LB and Lewis NG. (2007) Phenylalanine biosynthesis in&#xd;
Arabidopsis thaliana. Identification and characterization of arogenate dehydratases. J Biol Chem.&#xd;
282(42):30827-35.</mods:abstract>
               <mods:language>
                  <mods:languageTerm authority="rfc3066">eng</mods:languageTerm>
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               <mods:subject>
                  <mods:topic>Fenilalanina</mods:topic>
               </mods:subject>
               <mods:titleInfo>
                  <mods:title>Phenylalanine biosynthesis: the role and evolution of arogenate dehydratase gene family in c</mods:title>
               </mods:titleInfo>
               <mods:genre>conference output</mods:genre>
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