The identification of a variant form of cystathionine beta-synthase in nematodes

Exp Parasitol. 1992 Dec;75(4):415-24. doi: 10.1016/0014-4894(92)90254-8.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Catalysis
  • Cystathionine beta-Synthase / chemistry
  • Cystathionine beta-Synthase / metabolism*
  • Cysteine / metabolism
  • Hydrogen Sulfide / metabolism
  • Isoenzymes / chemistry
  • Isoenzymes / metabolism*
  • Liver / enzymology
  • Mercaptoethanol / pharmacology
  • Molecular Weight
  • Nematoda / enzymology*
  • Nippostrongylus / enzymology
  • Rats
  • Trichostrongyloidea / enzymology

Substances

  • Isoenzymes
  • Mercaptoethanol
  • Cystathionine beta-Synthase
  • Cysteine
  • Hydrogen Sulfide