Abstract
A medium-chain fatty acid:CoA ligase (AMP) which activates salicylate has been purified approximately 30-fold from bovine liver "mitochondria." The new enzyme is not completely free of a medium-chain fatty acid:CoA ligase (AMP) (EC 6.2.1.2) of the type first described by Mahler, Wakil, and Bock [J. Biol. Chem. 204, 453 (1953)], but the two enzymes can be distinguished readily from each other. The enzyme with salicyl-CoA synthetase activity is more easily inactivated, migrates more slowly toward the anode during disc gel electrophoresis, and utilizes a wider spectrum of aromatic acid substrates than the enzyme described earlier. Evidence was obtained that both enzymes could catalyze the activation of hexanoate, benzoate, o-methoxybenzoate, and anthranilate, but only the "salicylate" enzyme displayed activity with salicylate and p-aminosalicylate.
ACKNOWLEDGMENT The authors wish to thank Dr. Sung Ling Yuan for his valuable technical assistance.
- Copyright © 1971 by Academic Press, Inc.
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