In the preceding paper (1) it was demonstrated that cell-free extracts of Escherichia coli converted n-erythrose 4-phosphate and phosphoenolpyruvate almost quantitatively to 5-dehydroquinic acid. It was postulated that the initial reaction in this conversion is a condensation of phosphoenolpyruvate and n-erythrose 4-phosphate to yield inorganic phosphate and 2-keto3-deoxy-n-arabo-heptonic acid 7-phosphate. The present paper describes the purification and properties of the enzyme carrying out this reaction, and the identification of the product as KDHPr by comparison with the chemically synthesized compound. The name KDHP synthetase is suggested for this enzyme. The later stages of the enzyme purification were greatly aided by the discovery of Weissbach and Hurwitz (3) (communicated to us before publication) that P-formylpyruvic acid, derived from KDHP by the action of periodate, reacts with thiobarbituric acid to give an intense pink color with an absorption maximum at 549 mp. A part of these results was published in preliminary form (4).
2-Keto-3-deoxy-D-arabo-heptonic acid 7-phosphate synthetase.
P. R. Srinivasan,D. B. Sprinson
Published 1959 in Journal of Biological Chemistry
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- Publication year
1959
- Venue
Journal of Biological Chemistry
- Publication date
1959-04-01
- Fields of study
Biology, Medicine, Chemistry
- Identifiers
- External record
- Source metadata
Semantic Scholar, PubMed
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