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. 1974 Nov;120(2):590–597. doi: 10.1128/jb.120.2.590-597.1974

Purification and Properties of 3-Deoxy-d-Arabinoheptulosonic Acid-7-Phosphate Synthetase (trp) from Escherichia coli

J Camakaris a,1, J Pittard a
PMCID: PMC245816  PMID: 4218228

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 Co2+ or Mn2+. Neither treatment with ethylenediaminetetraacetic acid nor addition of Co2+ or Mn2+ affected the activity of the feedback-resistant enzyme.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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