Open AccessAcetate Binding of Spinach Chloroplasts as a Facet of Fatty Acid Synthesis
Author(s) -
Kenneth A. Devor,
J.B. Mudd
Publication year - 1968
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.43.6.853
Subject(s) - spinach , chemistry , acetyl coa , cofactor , biochemistry , chloroplast , fatty acid synthesis , citrate synthase , substrate (aquarium) , binding site , coenzyme a , fatty acid , enzyme , biology , ecology , reductase , gene
A particulate fraction of spinach chloroplasts is the major site of binding when either acetate or acetyl-CoA is used as substrate. The acetate is linked covalently, and the binding is inhibited by reagents which react with sulfhydryl groups. The amount of acetate bound is lowered by both citrate and oxaloacetate; however, the binding is not reversed by oxaloacetate. Reversal of binding is also not brought about by the addition of unlabeled acetyl-CoA. If cofactors for fatty acid synthesis and cold acetyl-CoA are added, the binding of labeled acetate is reversed. Acyl carrier protein from E. coli increases the binding of labeled acetate.