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B6db references: lenovcostchi

type Journal Article
authors Watanabe, M.; Kusano, M.; Oikawa, A.; Fukushima, A.; Noji, M.; Saito, K.
title Physiological roles of beta-substituted alanine synthase gene (Bsas) family in Arabidopsis thaliana
journal Plant Physiol
sel unselected
ui lenovcostchi
year (2008)
volume 146
pages 310-20
keywords Arabidopsis/*enzymology/genetics
abstract The beta-substituted alanine synthase (Bsas) family in the large super family of pyridoxal 5'-phosphate-dependent enzymes comprises cysteine (Cys) synthase (CSase) [O-acetylserine (thiol) lyase] and beta-cyanoalanine synthase (CASase) in plants. Nine genomic sequences encode putative Bsas proteins in Arabidopsis thaliana. The physiological roles of these Bsas isoforms in vivo were investigated by the characterization of T-DNA insertion mutants. The analyses of gene expression, activities of CSase and CASase, and levels of Cys and glutathione in the bsas mutants indicated that cytosolic Bsas1;1, plastidic Bsas2;1, and mitochondrial Bsas2;2 play major roles in Cys biosynthesis. Cytosolic Bsas1;1 has the most dominant contribution both in leaf and root, and mitochondrial Bsas2;2 plays a significant role in root. Mitochondrial Bsas3;1 is a genuine CASase. Non-targeted metabolome analyses of knockout mutants were carried out by a combination of gas chromatography time-of-flight mass spectrometry and capillary electrophoresis time-of-flight mass spectrometry. The level of -glutamyl--cyanoalanine decreased in the mutant bsas3;1, indicating the crucial role of Bsas3;1 in -cyanoalanine metabolism in vivo.
last changed 2008/04/01 15:48

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