Phylogenetic and experimental characterization of an acyl-ACP thioesterase family reveals significant diversity in enzymatic specificity and activity

Acyl-acyl carrier protein thioesterases (acyl-ACP TEs) 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 i...

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Veröffentlicht in:	BMC biochemistry 2011-08, Vol.12 (1), p.44-44, Article 44
Hauptverfasser:	Jing, Fuyuan, Cantu, David C, Tvaruzkova, Jarmila, Chipman, Jay P, Nikolau, Basil J, Yandeau-Nelson, Marna D, Reilly, Peter J
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Biocatalysis Biosynthesis Chemicals Cluster Analysis Databases, Protein E coli Esterases Fatty acids Fatty Acids, Unsaturated - biosynthesis Fatty Acids, Volatile - biosynthesis Identification and classification Models, Molecular Molecular Sequence Data Phylogeny Physiological aspects Plant introductions Plants - enzymology Protein Conformation Seeds Sequence Analysis, DNA Studies Substrate Specificity Thiolester Hydrolases - chemistry Thiolester Hydrolases - classification Thiolester Hydrolases - metabolism Trees
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