|
type |
Journal Article |
authors |
Smacchi, E.; Gobbetti, M. |
title |
Purification and characterization of cystathionine gamma-lyase from Lactobacillus fermentum DT41 |
journal |
FEMS Microbiol Lett |
Activity |
4.4.1.1 |
Family |
4.4.1.1 |
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 |
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