Acetyl-coenzyme A carboxylase from the developing endosperm of Ricinus communis. I. Isolation and characterization

Arch Biochem Biophys. 1983 Sep;225(2):576-85. doi: 10.1016/0003-9861(83)90069-3.


Acetyl-coenzyme A carboxylase has been purified from the plastids of developing castor oil seeds. High concentrations of the enzyme are required for stability as well as the presence of dithiothreitol, glycerol, bicarbonate, Triton X-100, and polyvinyl-pyrrolidone. It has a molecular weight of approximately 528,000 and appears to be membrane associated. Acetyl-CoA carboxylase is active over a wide pH range with an optimum at 8.0. Arrhenius plots are biphasic. The enzyme displays normal Michaelis-Menten kinetics with limiting Michaelis constants of KATP, 0.1 mM; KHCO-3, 3.0 mM; and Kacetyl-CoA, 0.05 mM. Monovalent cations, such as K+ and Cs+, exert a small activating effect on the enzyme while a divalent cation, Mn2+ or Mg2+, is essential for activity. The enzyme does not appear to be highly regulated by cellular metabolites.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetyl-CoA Carboxylase / isolation & purification*
  • Acetyl-CoA Carboxylase / metabolism
  • Castor Bean / enzymology*
  • Cations, Divalent
  • Cations, Monovalent
  • Drug Stability
  • Hydrogen-Ion Concentration
  • Kinetics
  • Ligases / isolation & purification*
  • Molecular Weight
  • Plants, Toxic*
  • Ribulose-Bisphosphate Carboxylase / metabolism
  • Ricinus / enzymology*
  • Seeds / enzymology*
  • Thermodynamics


  • Cations, Divalent
  • Cations, Monovalent
  • Ribulose-Bisphosphate Carboxylase
  • Ligases
  • Acetyl-CoA Carboxylase