PMID:4218228
| Citation |
Camakaris, J and Pittard, J (1974) Purification and properties of 3-deoxy-D-arabionheptulosonic acid-7-phosphate synthetase (trp) from Escherichia coli. J. Bacteriol. 120:590-7 |
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| Abstract |
The 3-deoxy-d-arabinoheptulosonic acid-7-phosphate synthetase which is subject to regulation by tryptophan has been partially purified from a strain of Escherichia coli K-12, in which this is the only functional form of this enzyme activity, and from a similar strain possessing a feedback-resistant form of the enzyme. Maximal observed inhibition by tryptophan of the feedback-sensitive enzyme was 56%. There was no evidence for cooperativity in the saturation of the enzyme with tryptophan or E4P. The molecular weights of the feedback-sensitive and feedback-resistant forms of the enzyme were the same (52,000), and no change was detected in the molecular weight of the feedback-sensitve enzyme in the presence of tryptophan. The effect of tryptophan analogues was tested to determine the nature of the tryptophan binding site. Treatment with ethylenediaminetetraacetic acid removed 80% of the activity of the feedback-sensitive enzyme. This activity was restored upon the addition of Co(2+) or Mn(2+). Neither treatment with ethylenediaminetetraacetic acid nor addition of Co(2+) or Mn(2+) affected the activity of the feedback-resistant enzyme. |
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| Keywords |
Aldehyde-Lyases/isolation & purification; Ammonium Sulfate; Arabinose; Bacterial Proteins/analysis; Chloromercuribenzoates/pharmacology; Chromatography; Chromatography, DEAE-Cellulose; Chromatography, Gel; Computers; Edetic Acid/pharmacology; Electrophoresis, Polyacrylamide Gel; Escherichia coli/analysis; Escherichia coli/enzymology; Escherichia coli/growth & development; Feedback; Heptoses; Hydroxyapatites; Kinetics; Mercaptoethanol/pharmacology; Molecular Weight; Nucleic Acids/isolation & purification; Phosphates; Phosphoenolpyruvate; Tryptophan/analogs & derivatives; Tryptophan/pharmacology |
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