STUDIES ON THE ADENOSINE TRIPHOSPHATE-PROPIONATE REACTION IN EXTRACTS OF AN UNIDENTIFIED BACTERIUM,

Abstract

An adenosine triphosphate-linked propionate activation is de scribed with apractically coenzyme A-free bacterial extract which yields pyrophosphate without addition of coenzyme A or hydroxylamine. No accumulation of a hydroxylamine-reactive compound was observed. The reaction is stimulated by coenzyme A and hydroxylamine. The preparation catalyzes the reactions: (a) propionyl adenylate + pyro phosphate[long dash][forward arrow] propionate + adenosine triphosphate, and (b) propionyl adeny late + coenzyme A[forward arrow] propionyl coenzyme A + adenylate. The prepara tion contains an active hydrolase for propionyl adenylate. It is assumed that pyrophosphate formation from adenosine triphosphate + propionate is due to propionyl adenylate formation and its rapid removal by hydrol ysis. A convenient method for the preparation of acyl adenylates is described.