Document Detail

Cloning and functional characterization of Arabidopsis thaliana D-amino acid aminotransferase--D-aspartate behavior during germination.
MedLine Citation:
PMID:  18318836     Owner:  NLM     Status:  MEDLINE    
The understanding of D-amino acid metabolism in higher plants lags far behind that in mammals, for which the biological functions of these unique amino acids have already been elucidated. In this article, we report on the biochemical behavior of D-amino acids (particularly D-Asp) and relevant metabolic enzymes in Arabidopsis thaliana. During germination and growth of the plant, a transient increase in D-Asp levels was observed, suggesting that D-Asp is synthesized in the plant. Administration of D-Asp suppressed growth, although the inhibitory mechanism responsible for this remains to be clarified. Exogenous D-Asp was efficiently incorporated and metabolized, and was converted to other D-amino acids (D-Glu and D-Ala). We then studied the related metabolic enzymes, and consequently cloned and characterized A. thaliana D-amino acid aminotransferase, which is presumably involved in the metabolism of D-Asp in the plant by catalyzing transamination between D-amino acids. This is the first report of cDNA cloning and functional characterization of a D-amino acid aminotransferase in eukaryotes. The results presented here provide important information for understanding the significance of D-amino acids in the metabolism of higher plants.
Miya Funakoshi; Masae Sekine; Masumi Katane; Takemitsu Furuchi; Masafumi Yohda; Takafumi Yoshikawa; Hiroshi Homma
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The FEBS journal     Volume:  275     ISSN:  1742-464X     ISO Abbreviation:  FEBS J.     Publication Date:  2008 Mar 
Date Detail:
Created Date:  2008-03-05     Completed Date:  2008-05-07     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101229646     Medline TA:  FEBS J     Country:  England    
Other Details:
Languages:  eng     Pagination:  1188-200     Citation Subset:  IM    
School of Pharmaceutical Sciences, Kitasato University, 5-9-1 Shirokane, Minato-ku, Tokyo, Japan.
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MeSH Terms
Amino Acid Sequence
Arabidopsis / drug effects,  enzymology*
Arabidopsis Proteins / genetics,  metabolism*
Bacillus subtilis / enzymology
Cloning, Molecular
Culture Media / chemistry,  metabolism,  pharmacology
D-Aspartic Acid / analysis,  metabolism*,  pharmacology
Molecular Sequence Data
Recombinant Proteins / genetics,  metabolism
Transaminases / genetics,  metabolism*
Reg. No./Substance:
0/Arabidopsis Proteins; 0/Culture Media; 0/Recombinant Proteins; 1783-96-6/D-Aspartic Acid; EC 2.6.1.-/D-amino acid aminotransferase, Arabidopsis thaliana; EC 2.6.1.-/Transaminases

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