PMID:2013569
| Citation |
Su, H and Newman, EB (1991) A novel L-serine deaminase activity in Escherichia coli K-12. J. Bacteriol. 173:2473-80 |
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| Abstract |
We demonstrate here that Escherichia coli K-12 synthesizes two different L-serine deaminases (L-SD) catalyzing the nonoxidative deamination of L-serine to pyruvate, one coded for by the previously described sdaA gene and a second, hitherto undescribed enzyme which we call L-SD2. A strain carrying a null mutation in sdaA made no detectable L-SD in minimal medium, but had activity in Luria broth. We describe a mutation, sdaX, which affects the regulation of L-SD2 and permits its expression in minimal medium, and an insertion mutation, sdaB, which abolishes L-SD2 activity completely. Both mutations lie near 60.5 min on the E. coli genetic map. The two L-SD enzymes have similar enzyme parameters, and both require posttranslational activation. |
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| Keywords |
Chromosome Mapping; Cloning, Molecular; Conjugation, Genetic; Dithiothreitol/pharmacology; Escherichia coli/metabolism; Iron/pharmacology; L-Serine Dehydratase/biosynthesis; L-Serine Dehydratase/genetics; Nucleic Acid Hybridization; Plasmids; Transduction, Genetic |
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