Investigations into the properties of 6-PG dehydrogenase in cell free extracts ofEscherichia coli revealed a pit optimum at pH 9.5 with a sharp decline on both sides of the optimum. The addition of 1.0 โข 10 -3 ~ MgCI 2 produced maximal activity, whereas higher concentrations caused inhibition. The K
In vitro Synthesis of a Constitutive Enzyme of Escherichia coli, 6-phosphogluconate Dehydrogenase
โ Scribed by Tomas Isturiz and Richard E. Wolf
- Book ID
- 123653468
- Publisher
- National Academy of Sciences
- Year
- 1975
- Tongue
- English
- Weight
- 663 KB
- Volume
- 72
- Category
- Article
- ISSN
- 0027-8424
- DOI
- 10.2307/64960
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A protein fraction, called At (= anti termination) factor, has been isolated from extracts of E. coli and partially purified. The At factor stimulates the synthesis in vitro of anthranilate synthetase, an enzyme encoded by two genes of the tryptophan (trp) operon, but has no effect on the synthesis