PMID:2013569: Difference between revisions

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<span style = 'font-size: large'> '''Su, H and Newman, EB'''  (1991) A novel L-serine deaminase activity in Escherichia coli K-12.''J. Bacteriol.'' '''173''':2473-80</span>
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!align=left  |Citation
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'''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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!align=left  |Abstract
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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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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2013569 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC207810 PMC207810]


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|{{TableHeadingColor}} |'''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.
!align=left  |Keywords
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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
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2013569 PubMed]
 
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Latest revision as of 04:36, 15 September 2013

Citation

Su, H and Newman, EB (1991) A novel L-serine deaminase activity in Escherichia coli K-12. J. Bacteriol. 173:2473-80

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.

Links

PubMed PMC207810

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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