Identification of a plant gene encoding glutamate/aspartate-prephenate aminotransferase: The last homeless enzyme of aromatic amino acids biosynthesis

被引:54
作者
Graindorge, Matthieu [2 ,5 ]
Giustini, Cecile [2 ,4 ]
Jacomin, Anne Claire [5 ]
Kraut, Alexandra [3 ]
Curien, Gilles [1 ,2 ]
Matringe, Michel [2 ,4 ]
机构
[1] CNRS, Lab Physiol Cellulaire Vegetale, iRTSV, UMR 5168, F-38054 Grenoble, France
[2] CEA, Lab Physiol Cellulaire Vegetale, iRTSV, DSV, F-38054 Grenoble, France
[3] INSERM, Lab Etud Dynam Proteomes, U880, F-38054 Grenoble, France
[4] INRA, UMR 1200, F-38054 Grenoble, France
[5] Univ Grenoble 1, F-38054 Grenoble, France
关键词
Aspartate aminotransferase; Aromatic amino acid; Enzymology; Metabolism; Plant; Prephenate aminotransferase; AROGENATE DEHYDROGENASE; L-TYROSINE; CYCLOHEXADIENYL DEHYDROGENASE; ASPARTATE-AMINOTRANSFERASE; ARABIDOPSIS-THALIANA; SHIKIMATE PATHWAY; L-PHENYLALANINE; PROTEIN FAMILY; CELL-CULTURES; PURIFICATION;
D O I
10.1016/j.febslet.2010.09.037
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In all organisms synthesising phenylalanine and/or tyrosine via arogenate, a prephenate aminotransferase is required for the transamination of prephenate into arogenate. The identity of the gene encoding this enzyme in the organisms where this activity occurs is still unknown. Glutamate/aspartate-prephenate aminotransferase (PAT) is thus the last homeless enzyme in the aromatic amino acids pathway. We report on the purification, mass spectrometry identification and biochemical characterization of Arabidopsis thaliana prephenate aminotransferase. Our data revealed that this activity is housed by the prokaryotic-type plastidic aspartate aminotransferase (At2g22250). This represents the first identification of a gene encoding PAT. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:4357 / 4360
页数:4
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