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  • Title: Purification and characterization of cystathionine gamma-lyase from Lactobacillus fermentum DT41.
    Author: Smacchi E, Gobbetti M.
    Journal: FEMS Microbiol Lett; 1998 Sep 15; 166(2):197-202. PubMed ID: 9770274.
    Abstract:
    A homo-tetrameric ca. 140-kDa cystathionine gamma-lyase was purified to homogeneity from Lactobacillus fermentum DT41 by four chromatographic steps. This was the first enzyme responsible for amino acid catabolism purified from lactobacilli. The activity is pyridoxal-5'-phosphate dependent and the enzyme catalyzes the alpha,gamma-elimination reaction of L-cystathionine producing L-cysteine, ammonia and alpha-ketobutyrate. The cystathionine gamma-lyase produced a free thiol group, a keto acid component and ammonia from several amino acids, including L-cysteine and methionine, and amino acid derivatives. L-Cystine was the best substrate. The enzyme was stable in the conditions of cheese ripening and may contribute to the biosynthesis of sulfur-containing compounds.
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