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Cysteine conjugate beta-lyase in the gastrointestinal bacterium Eubacterium limosum

GL Larsen and JL Stevens

A cysteine conjugate beta-lyase (beta-lyase) from the gastrointestinal bacterium Eubacterium limosum has been isolated and characterized. This organism has the highest specific activity for cysteine conjugate beta- lyase of the gastrointestinal bacteria studied. The beta-lyase was found to cleave the thioether linkage of S-alkyl- and S-aryl-L-cysteine conjugates. Stoichiometric amounts of 2-mercaptobenzothiazole, pyruvic acid, and ammonia were produced from the beta-lyase cleavage of S-(2- benzothiazolyl)-L-cysteine. The enzyme activity was inhibited by hydroxylamine, iodoacetic acid, or KCN. The enzyme appears to be a 75,000-Da dimer of two 38,000-Da subunits. A natural substrate, cystathionine, was cleaved by this enzyme, indicating that this beta- lyase has beta-cystathionase activity. These data suggest that a beta- cystathionase from E. limosum may be an important enzyme in the metabolism of a wide range of cysteine conjugates of xenobiotics to thiol-containing products.

Volume 29, Issue 1, pp. 97-103, 01/01/1986
Copyright © 1986 by American Society for Pharmacology and Experimental Therapeutics




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Copyright © 1986 by the American Society for Pharmacology and Experimental Therapeutics