Cystathionine beta-synthase and gamma-cystathionase in helminths.
The activities of gamma-cystathionase and cystathionine beta-synthase were investigated in a range of gastrointestinal, free-living and entomophagous nematodes. Although nematode gamma-cystathionase used the same range of substrates as the mammalian hepatic enzyme, its activity was extremely low and there were significant interspecies variations with respect to the relative order of active substrates. Like the mammalian liver enzyme, nematode cystathionine beta-synthase showed activity in the directions of both cystathionine synthesis and the forward and reverse "L-serine sulphhydrase" reactions. However, the most important feature of the survey was the widespread ability of nematode cystathionine beta-synthase to catalyse the non-mammalian "activated L-serine sulphhydrase" reaction (L-cysteine + R-SH----cysteine thioether + H2S). Additional survey work revealed that the ability to catalyse the activated L-serine sulphhydrase reaction was almost universal amongst nematodes. Activated L-serine sulphhydrase activity was also demonstrated in the acanthocephalan Pomphorhynchus laevis but was absent from cestodes and digeneans.
Walker
J
J
Department of Biological Sciences, University College of Wales, Aberystwyth, Dyfed, UK.
Barrett
J
J
D000049:Acanthocephala / Q000201:enzymology; D000818:Animals; D002589:Cestoda / Q000201:enzymology; D003541:Cystathionine beta-Synthase / Q000378:metabolism*; D003542:Cystathionine gamma-Lyase / Q000378:metabolism*; D009348:Nematoda / Q000201:enzymology*; D014200:Trematoda / Q000201:enzymology
D003541:Cystathionine beta-Synthase; D003542:Cystathionine gamma-Lyase