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Cloning and functional characterization of an acyl-ACP thioesterase (CvFatB) from Cuphea viscosissima in Arabidopsis
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- URLhttps://db.koreascholar.com/Article/Detail/302520
Acyl-acyl carrier protein (ACP) thioesterase (TE) catalyze the hydrolysis of the thioester bond that links the acyl chain to the sulfhydryl group of the phosphopantetheine prosthetic group of ACP. This reaction terminates acyl chain elongation of fatty acid biosynthesis, and in plant seeds it is the biochemical determinant of the fatty acid compositions of storage lipids. A full-length cDNA of an acyl-ACP thioesterase, named CvFatB, was isolated from oil plant Cuphea viscosissima accumulating up to 90% caprylate (8:0) and caprate (10:0) in its seed oil. This cDNA contains a 1,245-bp open reading frame that encodes a protein of 415 amino acids. The deduced sequence also contains two essential residues (H317 and C352) for TE catalytic activity and a putative chloroplast transit peptide at the N-terminal. Overexpression of the CvFatB cDNA in Arabidopsis resulted in increased levels of saturated fatty acid, especially palmitate, and reduced levels of unsaturated fatty acids. The findings suggest that CvFatB from oil plant C. viscosissima can function as a saturated acyl-ACP TE and can potentially be used to diversify the fatty acid biosynthesis pathway to produce novel fatty acids.
