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An alternative pathway contributes to phenylalanine biosynthesis in plants via a cytosolic tyrosine:phenylpyruvate aminotransferase

Author

Listed:
  • Heejin Yoo

    (Purdue University)

  • Joshua R. Widhalm

    (Purdue University)

  • Yichun Qian

    (Purdue University)

  • Hiroshi Maeda

    (Purdue University
    Present address: Department of Botany, University of Wisconsin-Madison, 430 Lincoln Drive, Madison, Wisconsin 53706, USA)

  • Bruce R. Cooper

    (Bindley Bioscience Center, Metabolite Profiling Facility, Purdue University)

  • Amber S. Jannasch

    (Bindley Bioscience Center, Metabolite Profiling Facility, Purdue University)

  • Itay Gonda

    (Institute of Plant Sciences, Newe Ya’ar Research Center, Agricultural Research Organization)

  • Efraim Lewinsohn

    (Institute of Plant Sciences, Newe Ya’ar Research Center, Agricultural Research Organization)

  • David Rhodes

    (Purdue University)

  • Natalia Dudareva

    (Purdue University
    Purdue University)

Abstract

Phenylalanine is a vital component of proteins in all living organisms, and in plants is a precursor for thousands of additional metabolites. Animals are incapable of synthesizing phenylalanine and must primarily obtain it directly or indirectly from plants. Although plants can synthesize phenylalanine in plastids through arogenate, the contribution of an alternative pathway via phenylpyruvate, as occurs in most microbes, has not been demonstrated. Here we show that plants also utilize a microbial-like phenylpyruvate pathway to produce phenylalanine, and flux through this route is increased when the entry point to the arogenate pathway is limiting. Unexpectedly, we find the plant phenylpyruvate pathway utilizes a cytosolic aminotransferase that links the coordinated catabolism of tyrosine to serve as the amino donor, thus interconnecting the extra-plastidial metabolism of these amino acids. This discovery uncovers another level of complexity in the plant aromatic amino acid regulatory network, unveiling new targets for metabolic engineering.

Suggested Citation

  • Heejin Yoo & Joshua R. Widhalm & Yichun Qian & Hiroshi Maeda & Bruce R. Cooper & Amber S. Jannasch & Itay Gonda & Efraim Lewinsohn & David Rhodes & Natalia Dudareva, 2013. "An alternative pathway contributes to phenylalanine biosynthesis in plants via a cytosolic tyrosine:phenylpyruvate aminotransferase," Nature Communications, Nature, vol. 4(1), pages 1-11, December.
  • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3833
    DOI: 10.1038/ncomms3833
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    Cited by:

    1. Xing-Qi Huang & Renqiuguo Li & Jianxin Fu & Natalia Dudareva, 2022. "A peroxisomal heterodimeric enzyme is involved in benzaldehyde synthesis in plants," Nature Communications, Nature, vol. 13(1), pages 1-15, December.

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