title: Two families of acyl-CoA thioesterases in Arabidopsis.
abstract: We have identified two families of acyl-CoA thioesterase (ACHs) in Arabidopsis thaliana. One family, consisting of AtACH1 and AtACH2, appears to be peroxisomal, as they have type-1 peroxisomal targeting sequences. The other family, consisting of AtACH4 and AtACH5, resides in the endoplasmic reticulum, as shown by green fluorescent protein studies. AtACH2 has been overexpressed in Escherichia coli and shows high levels of acyl-CoA thioesterase activity against both 16:0-CoA and 18:1-CoA. AtACH5 has also been overexpressed in E. coli, and shows thioesterase activity as well. ACHs have been characterized in other many other organisms and in various subcellular locations, but their true physiological role is not yet understood. Indeed, atach5 gene knockout mutants have no observable phenotype.
authors.affiliation: Institute of Biological Chemistry, Washington State University, Pullman, WA 99163, USA.
authors.forename: G
authors.initials: G
authors.lastname: Tilton
authors.forename: J
authors.initials: J
authors.lastname: Shockey
authors.forename: J
authors.initials: J
authors.lastname: Browse
mesh_terms: D017360:Arabidopsis / Q000201:enzymology*; D003001:Cloning, Molecular; D004721:Endoplasmic Reticulum / Q000201:enzymology; D004926:Escherichia coli; D017930:Genes, Reporter; D049452:Green Fluorescent Proteins; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism; D008055:Lipids / Q000096:biosynthesis; D008164:Luminescent Proteins / Q000032:analysis / Q000235:genetics; D010170:Palmitoyl-CoA Hydrolase / Q000235:genetics / Q000378:metabolism*; D020675:Peroxisomes / Q000201:enzymology; D030821:Plants, Genetically Modified; D011993:Recombinant Fusion Proteins / Q000378:metabolism
chemical_list: D007527:Isoenzymes; D008055:Lipids; D008164:Luminescent Proteins; D011993:Recombinant Fusion Proteins; D049452:Green Fluorescent Proteins; D010170:Palmitoyl-CoA Hydrolase