Abstract
Extracts from M. lwoffi oxidize propionate but at a low rate when compared with whole cells. This oxidative activity requires the formation of propionyl-CoA. Enzymes catalyzing the formation of propionyl phosphate and propionyl-CoA are present. The presence of a propionyl-CoA hydrolase is probably an artifact but partly responsible for the low rates of oxidation. Enzymes catalyzing the reduction of NAD+ and the formation of pyruvate with propionyl-CoA as substrate are present. That the only pathway for the metabolism of propionate in extracts is a direct one to acetate via pyruvate was confirmed by the use of 14c-labelled materials. A possible sequence of enzyme-catalyzed reactions that account for the observations is described.

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