Partial Purification and Characterization of Acetyl-CoA Synthetase from Mature Spinach Leaves
Acetyl-CoA synthetase (ACS) catalyzes the conversion of acetate to acetyl-CoA. In photosynthetic tissue, this enzyme is localized in the chloroplast (1) where it potentially provides a key source of acetyl-CoA for fatty acid, isoprenoid, and branch-chain amino acid biosynthesis. Acetyl-CoA synthetase’s contribution to chloroplast acetyl-CoA is presently controversial because of the identification of alternative sources of acetyl-CoA (i. e. pyruvate dehydrogenase complex (2, 3), and carnitine acyltransferase (4)), in the chloroplast. To further elucidate the role of ACS in chloroplast acetyl-CoA metabolism we have partially purified and characterized ACS from mature spinach leaves.
KeywordsCaproic Acid Pyruvate Dehydrogenase Complex Photosynthetic Tissue Spinach Leave Bovine Mammary Gland
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