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. 1972 Jul;69(7):1786–1790. doi: 10.1073/pnas.69.7.1786

In Vitro Synthesis of Enzymes of the Tryptophan Operon of Escherichia coli

P H Pouwels 1, J Van Rotterdam 1
PMCID: PMC426802  PMID: 4558657

Abstract

Two active enzymes of the tryptophan operon of E. coli, anthranilate synthetase (product of trp E and trp D) and tryptophan synthetase (EC 4.2.1.20) (product of trp B and trp A), have been synthesized in a DNA-dependent preparation for protein synthesis. Anthranilate synthetase and the two components of tryptophan synthetase (tryptophan synthetase A and B) are made in vitro in equimolar amounts, suggesting that regulation of the translation is similar in vivo and in vitro. Kinetics of the synthesis of the two enzymes suggest that transcription and translation proceed in vitro in a correct temporal sequence.

Keywords: anthranilate synthetase, tryptophan synthetase, DNA-dependent protein synthesis

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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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