Cysteine conjugate lyase in the gastrointestinal bacterium fusobacterium necrophorum

G. L. Larsen, J. D. Larson, J. A. Gustafsson

Research output: Contribution to journalArticlepeer-review

28 Scopus citations


1. A cysteine conjugate β-lyase from the anaerobic gastrointestinal bacterium Fusobacterium necrophorum was purified 51-fold by heat treatment, ammonium sulphate fractionation, gel-filtration chromatography, and anion-exchange chromatography. 2. This enzyme catalyses the cleavage of the thioether linkage in cysteine conjugates of the following S-alkyl- or S-aryl-linked compounds: cysteine conjugate of propachlor (2-S-cysteinyl-N-isopropylacetanilide); 1,2-dihydro-1-hydroxy-2-S-cysteinylnaphthalene and S-(2-benzothiazolyl)cysteine. 3. 2-Mercapto-N-isopropylacetanilide, pyruvic acid and ammonia were produced from the β-lyase cleavage of the cysteine conjugate of propachlor in equimolar ratios. 4. the apparent K(m) values for the cysteine conjugate of propachlor and S-(benzothiazolyl)cysteine were 1.1 and 1.0 mM, respectively. 5. Pyridoxal phosphate was required for enzymic activity. Ammonium ion activated enzymic activity, while hydroxylamine completely inhibited the enzyme. Dithiothreitol and bovine serum albumin had no effect on enzymic activity.

Original languageEnglish (US)
Pages (from-to)689-700
Number of pages12
Issue number11
StatePublished - 1983

ASJC Scopus subject areas

  • Biochemistry
  • Toxicology
  • Pharmacology
  • Health, Toxicology and Mutagenesis


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