The Presence and Possible Function of Methylmalonyl CoA Mutase and Propionyl CoA Carboxylase in Spirometra mansonoides
- 1 October 1977
- journal article
- research article
- Published by JSTOR in Journal of Parasitology
- Vol. 63 (5) , 769-774
- https://doi.org/10.2307/3279876
Abstract
Both spargana and adult forms of S. mansonoides accumulated lactate, succinate, acetate and propionate on 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 about 32 times more propionate than the spargana per gram of tissue. In accord with this propionate formation, propionyl CoA carboxylase and methylmalonyl CoA mutase were present in both stages of the parasite. As might be predicted, the activities of the carboxylase and mutase were 100-fold and 10-fold higher, respectively, in adults as compared to larvae. A possible physiological relationship between propionate formation and energy generation is suggested. 32Pi was incorporated into ATP on 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.This publication has 1 reference indexed in Scilit:
- Succinic and Reduced Diphosphopyridine Nucleotide Oxidase Systems of Ascaris MuscleJournal of Biological Chemistry, 1961