title: L-serine degradation in Escherichia coli K-12: cloning and sequencing of the sdaA gene.
abstract: A new mutant of Escherichia coli K-12 unable to grow with L-serine, glycine, and L-leucine has been isolated by lambda plac Mu insertion and shown to be deficient in L-serine deaminase activity. The corresponding gene, sdaA, has been cloned from a prototrophic strain, and the clone has been characterized and sequenced. The evidence is consistent with the hypothesis that sdaA is the structural gene for L-serine deaminase. However, other possibilities are also considered. No significant homology with previously reported DNA or protein sequences was detected.
authors.affiliation: Department of Biology, Concordia University, Montreal, Canada.
authors.forename: H S
authors.initials: HS
authors.lastname: Su
authors.forename: B F
authors.initials: BF
authors.lastname: Lang
authors.forename: E B
authors.initials: EB
authors.lastname: Newman
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D003090:Coliphages / Q000235:genetics; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D005796:Genes; D005798:Genes, Bacterial; D012695:L-Serine Dehydratase / Q000235:genetics*; D008969:Molecular Sequence Data; D010957:Plasmids; D015183:Restriction Mapping; D012694:Serine / Q000378:metabolism*
chemical_list: D012694:Serine; D012695:L-Serine Dehydratase