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פותח על ידי קלירמאש פתרונות בע"מ -
An alternative pathway contributes to phenylalanine biosynthesis in plants via a cytosolic tyrosine:phenylpyruvate aminotransferase
Year:
2013
Source of publication :
Nature Communications
Authors :
גונדה, איתי
;
.
לוינסון, אפרים
;
.
Volume :
4
Co-Authors:
Yoo, H., Department of Horticulture and Landscape Architecture, Purdue University, 625 Agriculture Mall Dr, West Lafayette, IN, United States
Widhalm, J.R., Department of Horticulture and Landscape Architecture, Purdue University, 625 Agriculture Mall Dr, West Lafayette, IN, United States
Qian, Y., Department of Horticulture and Landscape Architecture, Purdue University, 625 Agriculture Mall Dr, West Lafayette, IN, United States
Maeda, H., Department of Horticulture and Landscape Architecture, Purdue University, 625 Agriculture Mall Dr, West Lafayette, IN, United States, Department of Botany, University of Wisconsin-Madison, 430 Lincoln Drive, Madison, WI, United States
Cooper, B.R., Bindley Bioscience Center, Metabolite Profiling Facility, Purdue University, West Lafayette, IN, United States
Jannasch, A.S., Bindley Bioscience Center, Metabolite Profiling Facility, Purdue University, West Lafayette, IN, United States
Gonda, I., Institute of Plant Sciences, Newe ya'Ar Research Center, Agricultural Research Organization, PO Box 1021, Ramat Yishay, Israel
Lewinsohn, E., Institute of Plant Sciences, Newe ya'Ar Research Center, Agricultural Research Organization, PO Box 1021, Ramat Yishay, Israel
Rhodes, D., Department of Horticulture and Landscape Architecture, Purdue University, 625 Agriculture Mall Dr, West Lafayette, IN, United States
Dudareva, N., Department of Horticulture and Landscape Architecture, Purdue University, 625 Agriculture Mall Dr, West Lafayette, IN, United States, Department of Biochemistry, Purdue University, West Lafayette, IN, United States
Facilitators :
From page:
To page:
(
Total pages:
1
)
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. © 2013 Macmillan Publishers Limited. All rights reserved.
Note:
Related Files :
arabidopsis
biosynthesis
cellular distribution
Genetics
metabolism
Petunia
Phenylalanine
עוד תגיות
תוכן קשור
More details
DOI :
10.1038/ncomms3833
Article number:
2833
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
24723
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:09
Scientific Publication
An alternative pathway contributes to phenylalanine biosynthesis in plants via a cytosolic tyrosine:phenylpyruvate aminotransferase
4
Yoo, H., Department of Horticulture and Landscape Architecture, Purdue University, 625 Agriculture Mall Dr, West Lafayette, IN, United States
Widhalm, J.R., Department of Horticulture and Landscape Architecture, Purdue University, 625 Agriculture Mall Dr, West Lafayette, IN, United States
Qian, Y., Department of Horticulture and Landscape Architecture, Purdue University, 625 Agriculture Mall Dr, West Lafayette, IN, United States
Maeda, H., Department of Horticulture and Landscape Architecture, Purdue University, 625 Agriculture Mall Dr, West Lafayette, IN, United States, Department of Botany, University of Wisconsin-Madison, 430 Lincoln Drive, Madison, WI, United States
Cooper, B.R., Bindley Bioscience Center, Metabolite Profiling Facility, Purdue University, West Lafayette, IN, United States
Jannasch, A.S., Bindley Bioscience Center, Metabolite Profiling Facility, Purdue University, West Lafayette, IN, United States
Gonda, I., Institute of Plant Sciences, Newe ya'Ar Research Center, Agricultural Research Organization, PO Box 1021, Ramat Yishay, Israel
Lewinsohn, E., Institute of Plant Sciences, Newe ya'Ar Research Center, Agricultural Research Organization, PO Box 1021, Ramat Yishay, Israel
Rhodes, D., Department of Horticulture and Landscape Architecture, Purdue University, 625 Agriculture Mall Dr, West Lafayette, IN, United States
Dudareva, N., Department of Horticulture and Landscape Architecture, Purdue University, 625 Agriculture Mall Dr, West Lafayette, IN, United States, Department of Biochemistry, Purdue University, West Lafayette, IN, United States
An alternative pathway contributes to phenylalanine biosynthesis in plants via a cytosolic tyrosine:phenylpyruvate aminotransferase
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. © 2013 Macmillan Publishers Limited. All rights reserved.
Scientific Publication
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