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Prephenate aminotransferase directs plant phenylalanine biosynthesis via arogenate

Nature Chemical Biology volume 7, pages 19–21 (2011)Cite this article

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Abstract

The aromatic amino acids L-phenylalanine and L-tyrosine and their plant-derived natural products are essential in human and plant metabolism and physiology. Here we identified Petunia hybrida and Arabidopsis thaliana genes encoding prephenate aminotransferases (PPA-ATs), thus completing the identification of the genes involved in phenylalanine and tyrosine biosyntheses. Biochemical and genetic characterization of enzymes showed that PPA-AT directs carbon flux from prephenate toward arogenate, making the arogenate pathway predominant in plant phenylalanine biosynthesis.

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Figure 1: Effects of PPA-AT downregulation on the shikimate, phenylalanine and tyrosine pathways.
Figure 2: PPA-AT converts prephenate to arogenate.

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Change history

  • 10 December 2010

    In the version of this article initially published, the word “prephenate” was inadvertently switched to “phenylalanine” in the eighth paragraph. The error has been corrected in the HTML and PDF versions of the article.

References

  1. Boerjan, W., Ralph, J. & Baucher, M. Annu. Rev. Plant Biol. 54, 519–546 (2003).

    Article  CAS  Google Scholar 

  2. Kutchan, T.M. in The Alkaloids, Vol. 50 (ed. Cordell, G.) 257–316 (Academic Press, San Diego, 1998).

  3. Bramley, P.M. et al. J. Sci. Food Agric. 80, 913–938 (2000).

    Article  CAS  Google Scholar 

  4. Siehl, D.L. in Plant Amino Acids: Biochemistry and Biotechnology (ed. Singh, B.) 171–204 (CRC Press, 1999).

  5. Rippert, P. & Matringe, M. Eur. J. Biochem. 269, 4753–4761 (2002).

    Article  CAS  Google Scholar 

  6. Cho, M.H. et al. J. Biol. Chem. 282, 30827–30835 (2007).

    Article  CAS  Google Scholar 

  7. Maeda, H. et al. Plant Cell 22, 832–849 (2010).

    Article  CAS  Google Scholar 

  8. Yamada, T. et al. Plant Cell 20, 1316–1329 (2008).

    Article  CAS  Google Scholar 

  9. Rubin, J.L. & Jensen, R.A. Plant Physiol. 64, 727–734 (1979).

    Article  CAS  Google Scholar 

  10. Siehl, D.L., Singh, B.K. & Conn, E.E. Plant Physiol. 81, 711–713 (1986).

    Article  CAS  Google Scholar 

  11. Bonner, C.A. & Jensen, R.A. Arch. Biochem. Biophys. 238, 237–246 (1985).

    Article  CAS  Google Scholar 

  12. Redkina, T.V., Uspenska, Z. & Kretovic, V. Biochemistry (Mosc.) 34, 247–256 (1969).

    Google Scholar 

  13. Siehl, D.L., Connelly, J.A. & Conn, E.E. Z. Naturfo. C. 41, 79–86 (1986).

    Article  CAS  Google Scholar 

  14. De-Eknamkul, W. & Ellis, B.E. Arch. Biochem. Biophys. 267, 87–94 (1988).

    Article  CAS  Google Scholar 

  15. Wightman, F. & Forest, J.C. Phytochemistry 17, 1455–1471 (1978).

    Article  CAS  Google Scholar 

  16. Obayashi, T., Hayashi, S., Saeki, M., Ohta, H. & Kinoshita, K. Nucleic Acids Res. 37, D987–D991 (2009).

    Article  CAS  Google Scholar 

  17. Görlach, J. et al. Proc. Natl. Acad. Sci. USA 92, 3166–3170 (1995).

    Article  Google Scholar 

  18. de la Torre, F., De Santis, L., Suarez, M.F., Crespillo, R. & Canovas, F.M. Plant J. 46, 414–425 (2006).

    Article  CAS  Google Scholar 

  19. Nobe, Y. et al. J. Biol. Chem. 273, 29554–29564 (1998).

    Article  CAS  Google Scholar 

  20. Verdonk, J.C. et al. Phytochemistry 62, 997–1008 (2003).

    Article  CAS  Google Scholar 

  21. Bickel, H. & Schultz, G. Phytochemistry 18, 498–499 (1979).

    Article  CAS  Google Scholar 

  22. Nakai, T. et al. Biochemistry 38, 2413–2424 (1999).

    Article  CAS  Google Scholar 

  23. Zamir, L., Tiberio, R. & Jensen, R. Tetrahedr. Lett. 24, 2815–2818 (1983).

    Article  CAS  Google Scholar 

  24. Marino, G. et al. J. Biol. Chem. 263, 12305–12309 (1988).

    CAS  PubMed  Google Scholar 

  25. Fazel, A.M. & Jensen, R.A. J. Bacteriol. 138, 805–815 (1979).

    CAS  PubMed  PubMed Central  Google Scholar 

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Acknowledgements

We thank J. Zheng and C.M. Kish (Purdue University) for technical assistance in the quantitative real-time PCR experiments, G. Taguchi and E. Pichersky (University of Michigan) for the pLISG vector and N. Bonawitz, D. Rhodes (Purdue University) and members of Dudareva laboratory for critical reading of the manuscript. This work was supported by the US Agriculture and Food Research Initiative competitive grant no. 2010-65115-20385 from US Department of Agriculture National Institute of Food and Agriculture and by grant MCB-0615700 from the US National Science Foundation to N.D. H.M. was supported in part by the Japan Society for the Promotion of Science Postdoctoral Fellowship for Research Abroad.

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  1. Department of Horticulture and Landscape Architecture, Purdue University, West Lafayette, Indiana, USA

    Hiroshi Maeda, Heejin Yoo & Natalia Dudareva

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  1. Hiroshi Maeda
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  2. Heejin Yoo
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  3. Natalia Dudareva
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Contributions

H.M. and N.D. designed research; H.M. and H.Y. performed experiments; H.M., H.Y. and N.D. analyzed data; H.M. and N.D. wrote the paper. All authors read and edited the manuscript.

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Correspondence to Natalia Dudareva.

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The authors declare no competing financial interests.

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Supplementary Methods, Supplementary Figures 1–9 and Supplementary Tables 1 & 2 (PDF 1032 kb)

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Supplementary Data Set (TXT 40 kb)

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Maeda, H., Yoo, H. & Dudareva, N. Prephenate aminotransferase directs plant phenylalanine biosynthesis via arogenate. Nat Chem Biol 7, 19–21 (2011). https://doi.org/10.1038/nchembio.485

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