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Partial Purification and Characterization of Acetyl-CoA Synthetase from Mature Spinach Leaves

  • C. A. Zeiher
  • D. D. Randall

Abstract

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.

Keywords

Caproic Acid Pyruvate Dehydrogenase Complex Photosynthetic Tissue Spinach Leave Bovine Mammary Gland 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • C. A. Zeiher
    • 1
  • D. D. Randall
    • 1
  1. 1.Dept. of BiochemistryUniversity of Missouri-ColumbiaColumbiaUSA

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