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

Heejin Yoo, Joshua R. Widhalm, Yichun Qian, Hiroshi Maeda, Bruce R. Cooper, Amber S. Jannasch, Itay Gonda, Efraim Lewinsohn, David Rhodes and Natalia Dudareva ()
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Heejin Yoo: Purdue University
Joshua R. Widhalm: Purdue University
Yichun Qian: Purdue University
Hiroshi Maeda: Purdue University
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

Nature Communications, 2013, vol. 4, issue 1, 1-11

Abstract: 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.

Date: 2013
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DOI: 10.1038/ncomms3833

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