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A Novel Polyamine Acyltransferase Responsible for the Accumulation of Spermidine Conjugates in Arabidopsis Seed^[W],[OA]

^a Department of Metabolic Biology, John Innes Centre, Colney, Norwich, NR4 7UH, United Kingdom
^b National Key Laboratory of Crop Genetic Improvement, National Center of Plant Gene Research (Wuhan), Huazhong Agricultural University, Wuhan 430070, China
^c Technologies for System Biology, Institute of Food Research, Colney, Norwich, NR4 7UA, United Kingdom
^d Department of Computational Biology, John Innes Centre, Colney, Norwich, NR4 7UH, United Kingdom
^e Department of Biological Chemistry, John Innes Centre, Colney, Norwich, NR4 7UH, United Kingdom

² Address correspondence to cathie.martin{at}bbsrc.ac.uk.

Hydroxycinnamic acid amides are a class of secondary metabolites distributed widely in plants. We have identified two sinapoyl spermidine derivatives, N-((4'-O-glycosyl)-sinapoyl),N'-sinapoylspermidine and N,N'-disinapoylspermidine, which comprise the two major polyamine conjugates that accumulate in Arabidopsis thaliana seed. Using metabolic profiling of knockout mutants to elucidate the functions of members of the BAHD acyltransferase family in Arabidopsis, we have also identified two genes encoding spermidine disinapoyl transferase (SDT) and spermidine dicoumaroyl transferase (SCT) activities. At2g23510, which is expressed mainly in seeds, encodes a spermidine sinapoyl CoA acyltransferase (SDT) that is required for the production of disinapoyl spermidine and its glucoside in Arabidopsis seed. The structurally related BAHD enzyme encoded by At2g25150 is expressed specifically in roots and has spermidine coumaroyl CoA acyltransferase (SCT) activity both in vitro and in vivo.

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