The identification of a variant form of cystathionine beta-synthase in nematodes.
Characterization of the physical and catalytic properties of the enzyme responsible for nematode "activated L-serine sulfhydrase" activity (L-cysteine + R-SH-->cysteine thioether + H2S) has led to its identification as a novel, variant form (allelozyme) of cystathionine beta-synthase that is distinct from a mammalian-type synthase also present in nematodes. Additional work has demonstrated the ability of live Panagrellus redivivus to produce H2[35S] from exogenous L-[35S]cysteine and 2-mercaptoethanol, thus providing preliminary evidence for the in vivo operation of the activated L-serine sulfhydrase reaction in nematodes.
Walker
J
J
Department of Biological Sciences, University College of Wales, Aberystwyth, Dyfed, U.K.
Barrett
J
J
Thong
K W
KW
D000818:Animals; D002384:Catalysis; D003541:Cystathionine beta-Synthase / Q000737:chemistry / Q000378:metabolism*; D003545:Cysteine / Q000378:metabolism; D006862:Hydrogen Sulfide / Q000378:metabolism; D007527:Isoenzymes / Q000737:chemistry / Q000378:metabolism*; D008099:Liver / Q000201:enzymology; D008623:Mercaptoethanol / Q000494:pharmacology; D008970:Molecular Weight; D009348:Nematoda / Q000201:enzymology*; D009559:Nippostrongylus / Q000201:enzymology; D051381:Rats; D014251:Trichostrongyloidea / Q000201:enzymology
D007527:Isoenzymes; D008623:Mercaptoethanol; D003541:Cystathionine beta-Synthase; D003545:Cysteine; D006862:Hydrogen Sulfide