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Cysteine metabolism in the cestode Hymenolepis diminuta

Published online by Cambridge University Press:  06 April 2009

M. Gomez-Bautista  and
J. Barrett
M. Gomez-Bautista
Affiliation:
Departamento de Parasitologia, Facultad de Farmacia, Universidad de Salamanca, Salamanca, Spain
J. Barrett*
Affiliation:
Department of Zoology, University College of Wales, Aberystwyth, U.K.
*
Reprint requests to: Professor J. Barrett, Department of Zoology, University College of Wales, Aberystwyth, Dyfed SY23 3DA.
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Summary

The major pathways for cysteine catabolism in Hymenolepis diminuta have been investigated. The parasite has an active cystathionine-β-synthase and, as in other tissues, this enzyme has a wide substrate specificity. However, the enzyme from H. diminuta differs significantly from the mammalian enzyme in showing a high serine sulphydrase activity and a high serine lyase activity. There was only low γ-cystathionase activity in H. diminuta and again the enzyme showed a range of substrate specificities. Cysteine aminotransferase activity was readily demonstrated in the tapeworm, but there was no evidence for 3-mercaptopyruvate sulphotransferase activity. An oxidative pathway for cysteine catabolism in H. diminuta was shown by the presence of cysteine dioxygenase and cysteine sulphinate transaminase. The properties of the helminth cysteine dioxygenase were very similar to those of rat liver. H. diminuta was able to reduce cystine to cysteine via a glutathione-cysteine transhydrogenase system.

Type
Research Article
Information
Parasitology , Volume 97 , Issue 1 , August 1988 , pp. 149 - 159
Copyright
Copyright © Cambridge University Press 1988

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