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<span style = 'font-size: large'> '''Ely, B and Pittard, J'''  (1979) Aromatic amino acid biosynthesis: regulation of shikimate kinase in Escherichia coli K-12.''J. Bacteriol.'' '''138''':933-43</span>
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'''Ely, B and Pittard, J'''  (1979) Aromatic amino acid biosynthesis: regulation of shikimate kinase in Escherichia coli K-12. ''J. Bacteriol.'' '''138''':933-43
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!align=left  |Abstract
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Starvation of cells of Escherichia coli K-12 for the aromatic amino acids results in an increased rate of synthesis of shikimate kinase activity. The two controlling amino acids are tyrosine and tryptophan, and starvation for both results in derepression. The product of the regulator gene tyrR also participates in this control, and shikimate kinase synthesis was depressed in tyrR mutants. Chromatography of cell extracts on diethylaminoethyl-Sephadex allowed partial separation of two shikimate kinase enzymes and demonstrated that only one of these subject to specific repression control involving tyrR. By contrast, chromatography of cell extracts with G-75 or G-200 columns revealed a singl-molecular-weight species of shikimate kinase activity with an apparent molecular weight of 20,000. The levels of shikimate kinase in a series of partial diploid strains indicated that aroL, the structural gene for the tyrR-controlled shikimate kinase enzyme, is located on the E. coli chromosome between the structural genes proC and purE. By means of localized mutagenesis, an aroL mutant of E. coli was isolated. The mutant was an aromatic prototroph and, by the criterion of column chromatography, appeared to have only a single functional species of shikimate kinase enzyme.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=222728 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC218124 PMC218124]


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|{{TableHeadingColor}} |'''Abstract''' || Starvation of cells of Escherichia coli K-12 for the aromatic amino acids results in an increased rate of synthesis of shikimate kinase activity. The two controlling amino acids are tyrosine and tryptophan, and starvation for both results in derepression. The product of the regulator gene tyrR also participates in this control, and shikimate kinase synthesis was depressed in tyrR mutants. Chromatography of cell extracts on diethylaminoethyl-Sephadex allowed partial separation of two shikimate kinase enzymes and demonstrated that only one of these subject to specific repression control involving tyrR. By contrast, chromatography of cell extracts with G-75 or G-200 columns revealed a singl-molecular-weight species of shikimate kinase activity with an apparent molecular weight of 20,000. The levels of shikimate kinase in a series of partial diploid strains indicated that aroL, the structural gene for the tyrR-controlled shikimate kinase enzyme, is located on the E. coli chromosome between the structural genes proC and purE. By means of localized mutagenesis, an aroL mutant of E. coli was isolated. The mutant was an aromatic prototroph and, by the criterion of column chromatography, appeared to have only a single functional species of shikimate kinase enzyme.
!align=left  |Keywords
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Amino Acids/biosynthesis; Enzyme Repression; Escherichia coli/genetics; Escherichia coli/metabolism; Genes; Mutation; Phenylalanine/metabolism; Phosphotransferases/biosynthesis; Phosphotransferases/genetics; Shikimic Acid/metabolism; Tryptophan/metabolism; Tyrosine/metabolism
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=222728 PubMed]
 
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Latest revision as of 04:42, 15 September 2013

Citation

Ely, B and Pittard, J (1979) Aromatic amino acid biosynthesis: regulation of shikimate kinase in Escherichia coli K-12. J. Bacteriol. 138:933-43

Abstract

Starvation of cells of Escherichia coli K-12 for the aromatic amino acids results in an increased rate of synthesis of shikimate kinase activity. The two controlling amino acids are tyrosine and tryptophan, and starvation for both results in derepression. The product of the regulator gene tyrR also participates in this control, and shikimate kinase synthesis was depressed in tyrR mutants. Chromatography of cell extracts on diethylaminoethyl-Sephadex allowed partial separation of two shikimate kinase enzymes and demonstrated that only one of these subject to specific repression control involving tyrR. By contrast, chromatography of cell extracts with G-75 or G-200 columns revealed a singl-molecular-weight species of shikimate kinase activity with an apparent molecular weight of 20,000. The levels of shikimate kinase in a series of partial diploid strains indicated that aroL, the structural gene for the tyrR-controlled shikimate kinase enzyme, is located on the E. coli chromosome between the structural genes proC and purE. By means of localized mutagenesis, an aroL mutant of E. coli was isolated. The mutant was an aromatic prototroph and, by the criterion of column chromatography, appeared to have only a single functional species of shikimate kinase enzyme.

Links

PubMed PMC218124

Keywords

Amino Acids/biosynthesis; Enzyme Repression; Escherichia coli/genetics; Escherichia coli/metabolism; Genes; Mutation; Phenylalanine/metabolism; Phosphotransferases/biosynthesis; Phosphotransferases/genetics; Shikimic Acid/metabolism; Tryptophan/metabolism; Tyrosine/metabolism

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