L-serine degradation in Escherichia coli K-12: cloning and sequencing of the sdaA gene.
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.
Su
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HS
Department of Biology, Concordia University, Montreal, Canada.
Lang
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BF
Newman
E B
EB
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*
D012694:Serine; D012695:L-Serine Dehydratase