Further Studies on the Properties of Liver Propionyl Coenzyme A Holocarboxylase Synthetase and the Specificity of Holocarboxylase Formation

Abstract

Several lines of evidence reported previously indicated that the reactions shown below are catalyzed by a synthetase purified from rabbit liver, but the predicted biotin-dependent 32P-labeled pyrophosphate-adenosine triphosphate exchange was found to be very slow.Mg++ ATP + d-biotin \ d-biotinyl S-adenylate + PPi (1) d-Biotinyl5'-adenylate + propionyl coenzyme A .