The Presence and Possible Function of Methylmalonyl CoA Mutase and Propionyl CoA Carboxylase in Spirometra mansonoides

Both spargana and adult forms of Spirometra mansonoides were shown to accumulate lactate, succinate, acetate, and propionate upon in vitro incubation. Adults differed markedly from the spargana in that quantitatively the most significant products of the former were acetate and propionate while the l...

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Bibliographic Details
Published in:The Journal of parasitology 1977-10, Vol.63 (5), p.769-774
Main Authors: Tkachuck, Richard D., Saz, Howard J., Weinstein, Paul P., Finnegan, Kevin, Mueller, Justus F.
Format: Article
Language:English
Subjects:
Acetates
Acetates - metabolism
Adenosine Triphosphate - biosynthesis
Adult animals
Animals
Carboxy-Lyases - metabolism
Cestoda - enzymology
Cobamides - metabolism
Enzymes
Fermentation
Isomerases - metabolism
Lactates
Lactates - biosynthesis
Larva - enzymology
Methylmalonyl-CoA Mutase - metabolism
Parasites
Propionates
Propionates - metabolism
Radioactive decay
Sazes
Sparganum - enzymology
Sparganum - metabolism
Succinates - biosynthesis
Vitamin B12
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Summary:Both spargana and adult forms of Spirometra mansonoides were shown to accumulate lactate, succinate, acetate, and propionate upon in vitro incubation. Adults differed markedly from the spargana in that quantitatively the most significant products of the former were acetate and propionate while the latter formed primarily acetate and lactate. The adults accumulated approximately 32 times more propionate than the spargana per gram of tissue. In accord with this propionate formation, propionyl CoA carboxylase and methylmalonyl CoA mutase have been found to be present in both stages of the parasite. As might be predicted, however, the activities of the carboxylase and mutase were 100-fold and 10-fold higher, respectively, in the adults as compared to the larvae. A possible physiological relationship between propionate formation and energy generation is suggested. Accordingly, inorganic 32P was incorporated into ATP upon incubation of methylmalonyl CoA with a homogenate obtained from adult S. mansonoides. Since methylmalonyl CoA mutase requires vitamin B12 coenzyme, a relationship between vitamin B12 content and propionate formation in helminths is suggested.
ISSN:0022-3395
1937-2345
DOI:10.2307/3279876