PMID:6986356: Difference between revisions

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<span style = 'font-size: large'> '''Clark, D and Cronan, JE'''  (1980) Escherichia coli mutants with altered control of alcohol dehydrogenase and nitrate reductase.''J. Bacteriol.'' '''141''':177-83</span>
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!align=left  |Citation
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'''Clark, D and Cronan, JE Jr'''  (1980) Escherichia coli mutants with altered control of alcohol dehydrogenase and nitrate reductase. ''J. Bacteriol.'' '''141''':177-83
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!align=left  |Abstract
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Mutants of Escherichia coli which overproduce alcohol dehydrogenase were obtained by selection for the ability to use ethanol as an acetate source in a strain auxotrophic for acetate. A mutant having a 20-fold overproduction of alcohol dehydrogenase was able to use ethanol only to fulfill its acetate requirement, whereas two mutants with a 60-fold overproduction were able to use ethanol as a sole carbon source. The latter two mutants produced only 25% of the wild-type level of nitrate reductase, when grown under anaerobic conditions. Alcohol dehydrogenase production was largely unaffected by catabolite repression but was repressed by nitrate under both aerobic and anaerobic conditions. The genetic locus responsible for alcohol dehydrogenase overproduction was located at min 27 on the E. coli genetic map; the gene order, as determined by transduction, was trp tonB adh chlC hemA. The possible relationship of alcohol dehydrogenase to anaerobic redox systems such as formate-nitrate reductase is discussed.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6986356 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC293557 PMC293557]


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|{{TableHeadingColor}} |'''Abstract''' || Mutants of Escherichia coli which overproduce alcohol dehydrogenase were obtained by selection for the ability to use ethanol as an acetate source in a strain auxotrophic for acetate. A mutant having a 20-fold overproduction of alcohol dehydrogenase was able to use ethanol only to fulfill its acetate requirement, whereas two mutants with a 60-fold overproduction were able to use ethanol as a sole carbon source. The latter two mutants produced only 25% of the wild-type level of nitrate reductase, when grown under anaerobic conditions. Alcohol dehydrogenase production was largely unaffected by catabolite repression but was repressed by nitrate under both aerobic and anaerobic conditions. The genetic locus responsible for alcohol dehydrogenase overproduction was located at min 27 on the E. coli genetic map; the gene order, as determined by transduction, was trp tonB adh chlC hemA. The possible relationship of alcohol dehydrogenase to anaerobic redox systems such as formate-nitrate reductase is discussed.
!align=left  |Keywords
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Alcohol Oxidoreductases/biosynthesis; Anaerobiosis; Chromosome Mapping; Chromosomes, Bacterial; Escherichia coli/enzymology; Escherichia coli/genetics; Ethanol/metabolism; Genes, Regulator; Mutation; Nitrate Reductases/biosynthesis; Nitrates/pharmacology; Oxidoreductases/metabolism; Propylene Glycols/metabolism
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6986356 PubMed]
 
[http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=6986356 Full text]
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Latest revision as of 04:49, 15 September 2013

Citation

Clark, D and Cronan, JE Jr (1980) Escherichia coli mutants with altered control of alcohol dehydrogenase and nitrate reductase. J. Bacteriol. 141:177-83

Abstract

Mutants of Escherichia coli which overproduce alcohol dehydrogenase were obtained by selection for the ability to use ethanol as an acetate source in a strain auxotrophic for acetate. A mutant having a 20-fold overproduction of alcohol dehydrogenase was able to use ethanol only to fulfill its acetate requirement, whereas two mutants with a 60-fold overproduction were able to use ethanol as a sole carbon source. The latter two mutants produced only 25% of the wild-type level of nitrate reductase, when grown under anaerobic conditions. Alcohol dehydrogenase production was largely unaffected by catabolite repression but was repressed by nitrate under both aerobic and anaerobic conditions. The genetic locus responsible for alcohol dehydrogenase overproduction was located at min 27 on the E. coli genetic map; the gene order, as determined by transduction, was trp tonB adh chlC hemA. The possible relationship of alcohol dehydrogenase to anaerobic redox systems such as formate-nitrate reductase is discussed.

Links

PubMed PMC293557

Keywords

Alcohol Oxidoreductases/biosynthesis; Anaerobiosis; Chromosome Mapping; Chromosomes, Bacterial; Escherichia coli/enzymology; Escherichia coli/genetics; Ethanol/metabolism; Genes, Regulator; Mutation; Nitrate Reductases/biosynthesis; Nitrates/pharmacology; Oxidoreductases/metabolism; Propylene Glycols/metabolism

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