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L-Glutamate-l-carboxylase in Intestinal Parasites

Abstract

GLUTAMATE decarboxylase, an enzyme widely found in animals, plants and micro-organisms, has been searched for in intestinal parasites. We have found activity in the four species examined: Ascaridia galli, Ascaris lumbricoides, Taenia solium and Moniezia expansa. Cavier and Savel1 discovered several amino-acid decarboxylases in Ascaris lumbricoides but glutamate decarboxylase was not reported. Campbell2 identified 4-aminobutyrate, product of the reaction, in the free amino-acid fraction of several cestodes, and Monteoliva3 found it in the whole homogenate of Ascaridia galli. The direct relation of 4-aminobutyrate with the tricarboxylic acid cycle—through transamination with 2-oxoglutarate–has been found in brain4, in micro-organisms5 and in plant seeds and tubers6. Impaired respiration mutants of Saccharomyces cerevisiae show increased activity while in normal yeast strains glutamate decarboxylase activity increases as oxygen supply decreases7. As in Ascaris8, succinic acid accumulates in both cases9. The metabolism of intestinal parasites being predominantly anaerobic10, the investigation of a Krebs cycle by-pass system seems worth while.

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MONTEOLIVA, M., RASERO, F., GORGÉ, J. et al. L-Glutamate-l-carboxylase in Intestinal Parasites. Nature 205, 1111–1112 (1965). https://doi.org/10.1038/2051111a0

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