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The anaerobic formation of propionic acid in the mitochondria of the lugwormArenicola marina

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Summary

The anaerobic transformation of malate and succinate into propionate was demonstrated in homogenates and mitochondria isolated from the body wall musculature ofArenicola marina, a facultative anaerobic polychaete. Synthesis of propionate from succinate was enhanced by the addition of malate and ADP. In the presence of malate, acetate was formed in addition to propionate. Maximal quantities of both fatty acids were produced by mitochondria incubated with malate, succinate, and ADP. Since the rate of propionate production in this case was about the same as in homogenates when related to fresh weight, it is concluded that the enzymatic system involved is localized exclusively in the mitochondria. The rate of propionate production is correlated with the concentration of succinate, saturation being reached at about 5 mM. In tracer experiments using (methyl-14C)-malonyl-CoA, 2,3-14C-succinate, and 1-14C-propionate as precursors, the pathway of the transformation of succinate into propionate was examined. The results indicate that methylmalonyl-CoA is an intermediary product. It was shown that the synthesis of propionate from succinate is coupled to the formation of ATP. The ratio ATP/propionate was 0.76. Dinitrophenol had only a slight effect on this ratio, although the utilization of succinate was inhibited considerably. It is concluded that in vivo substrate level phosphorylation occurs equimolar to the formation of propionate from succinate.

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Abbreviations

Ap 5 A :

P1,P5-di(adenosine-5′-)pentaphosphate

DNP :

2,4-dinitrophenol

mma :

methylmalonic acid

mm-CoA :

methylmalonyl-CoA

EC 6.2.1.1:

Acetate thiokinase (AMP)

EC 3.6.1.3:

actomyosin ATPase

EC 2.7.4.3:

adenylate kinase

EC 2.8.3.1:

CoA transferase

EC 2.7.1.1:

hexokinase

EC 2.1.3.1:

methylmalonyl-CoA carboxyltransferase

EC 5.4.99.1:

methylmalonyl-CoA isomerase

EC 5.1.99.1:

methylmalonyl-CoA racemase

EC 6.4.1.3:

propionyl-CoA carboxylase

EC 1.2.4.1:

pyruvate dehydrogenase

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Supported by Deutsche Forschungsgemeinschaft Gr 456/6

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Schroff, G., Zebe, E. The anaerobic formation of propionic acid in the mitochondria of the lugwormArenicola marina . J Comp Physiol B 138, 35–41 (1980). https://doi.org/10.1007/BF00688733

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