Purification and characterization of benzoate:coenzyme A ligase from Clarkia breweri

Benzoate:CoA ligase (BZL) was partially purified from flowers of the annual California plant Clarkia breweri, BZL catalyzes the formation of benzoyl-CoA and anthraniloyl-CoA. important intermediates for subsequent acyltransferase reactions in plant secondary metabolism. The native enzyme is active as a monomer with a molecular mass of approximate to59-64.5 kDa, and it has K-m values of 45, 95, and 130 muM for benzoic acid, ATP, and CoA, respectively, BZL is most active in the pH range of 7.2-8.4. and its activity is strictly dependent on certain bivalent cations. BZL is an AMP-forming enzyme. Overall, its properties suggest that it is related to the family of CoA ligase enzymes that includes the plant enzyme 4-hydroxycinnamate:CoA ligase. (C) 2002 Elsevier Science (USA). All rights reserved.