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Cloning and Characterization of Two Lactobacillus casei Genes Encoding a Cystathionine Lyase▿

By Stefan Irmler, Sylvie Raboud, Beata Beisert, Doris Rauhut and Hélène Berthoud

Abstract

Volatile sulfur compounds are key flavor compounds in several cheese types. To better understand the metabolism of sulfur-containing amino acids, which certainly plays a key role in the release of volatile sulfur compounds, we searched the genome database of Lactobacillus casei ATCC 334 for genes encoding putative homologs of enzymes known to degrade cysteine, cystathionine, and methionine. The search revealed that L. casei possesses two genes that putatively encode a cystathionine β-lyase (CBL; EC 4.4.1.8). The enzyme has been implicated in the degradation of not only cystathionine but also cysteine and methionine. Recombinant CBL proteins catalyzed the degradation of l-cystathionine, O-succinyl-l-homoserine, l-cysteine, l-serine, and l-methionine to form α-keto acid, hydrogen sulfide, or methanethiol. The two enzymes showed notable differences in substrate specificity and pH optimum

Topics: Genetics and Molecular Biology
Publisher: American Society for Microbiology (ASM)
OAI identifier: oai:pubmedcentral.nih.gov:2223195
Provided by: PubMed Central
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