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Catabolism of Branched Chain Amino Acids Supports Respiration but Not Volatile Synthesis in Tomato Fruits.
MedLine Citation:
PMID:  22199237     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
The branched-chain amino acid transaminases (BCATs) have a crucial role in metabolism of the branched-chain amino acids leucine, isoleucine, and valine. These enzymes catalyze the last step of synthesis and the initial step of degradation of these amino acids. Although the biosynthetic pathways of branched chain amino acids in plants have been extensively investigated and a number of genes have been characterized, their catabolism in plants is not yet completely understood. We previously characterized the branched chain amino acid transaminase gene family in tomato, revealing both the subcellular localization and kinetic properties of the enzymes encoded by six genes. Here, we examined possible functions of the enzymes during fruit development. We further characterized transgenic plants differing in the expression of branched chain amino acid transaminases 1 and 3, evaluating the rates of respiration in fruits deficient in BCAT1 and the levels of volatiles in lines overexpressing either BCAT1 or BCAT3. We quantitatively tested, via precursor and isotope feeding experiments, the importance of the branched chain amino acids and their corresponding keto acids in the formation of fruit volatiles. Our results not only demonstrate for the first time the importance of branched chain amino acids in fruit respiration, but also reveal that keto acids, rather than amino acids, are the likely precursors for the branched chain flavor volatiles.
Authors:
Andrej Kochevenko; Wagner L Araújo; Gregory S Maloney; Denise M Tieman; Phuc Thi Do; Mark G Taylor; Harry J Klee; Alisdair R Fernie
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-12-22
Journal Detail:
Title:  Molecular plant     Volume:  -     ISSN:  1752-9867     ISO Abbreviation:  -     Publication Date:  2011 Dec 
Date Detail:
Created Date:  2011-12-26     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101465514     Medline TA:  Mol Plant     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Max Planck Institute of Molecular Plant Physiology, 14476 Potsdam-Golm, Germany.
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