Activities | Families | Sequences | Fold types | References | Help
B6db references: 98442410

type Journal Article
authors Smacchi, E.; Gobbetti, M.
title Purification and characterization of cystathionine gamma-lyase from Lactobacillus fermentum DT41
journal FEMS Microbiol Lett
ui 98442410
year (1998)
volume 166
number 2
pages 197-202.
keywords Amino Acids/analysis
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.
last changed 2008/04/02 19:23

B6db references