Journal of bacteriology, 174(10), 3339-3347 (1992-05-01)
A DNA fragment containing the Saccharomyces cerevisiae CYS3 (CYI1) gene was cloned. The clone had a single open reading frame of 1,182 bp (394 amino acid residues). By comparison of the deduced amino acid sequence with the N-terminal amino acid
Cystathionine gamma-synthase catalyzes a pyridoxal phosphate dependent synthesis of cystathionine from O-succinyl-L-homoserine (OSHS) and L-cysteine via a gamma-replacement reaction. In the absence of L-cysteine, OSHS undergoes an enzyme-catalyzed, gamma-elimination reaction to form succinate, alpha-ketobutyrate, and ammonia. Since elimination of the
Journal of biochemistry, 143(1), 59-68 (2007-11-06)
Cystathionine gamma-synthase (CGS) catalyses the first step of the transsulfuration pathway that converts l-cysteine to l-homocysteine in bacteria, whereas this pathway is absent in human. In this report, we identified a new metB gene from Helicobacter pylori strain SS1, and
Applied and environmental microbiology, 74(1), 99-106 (2007-11-13)
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
Journal of bacteriology, 153(1), 558-561 (1983-01-01)
Mutations were found which enable Escherichia coli K-12 to form homocysteine in the absence of cystathionase. The formation of homocysteine in the mutant strains required cystathionine gamma-synthetase, the metB gene product, but bypassed the normal intermediate cystathionine. It is concluded
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