Abstract
Tyrosine-inhibitable 3-deoxy-D-arabinoheptulosonic acid-7-phosphate (DAHP) synthase was purified to homogeneity without significant loss of sensitivity to inhibition by tyrosine from an operator-constitutive strain (tyrOc) of Salmonella. The enzyme had an apparent molecular weight of 76,000 by gel filtration and a subunit molecular weight of 40,000 by sodium dodecyl sulfate-gel electrophoresis and by reaction with dimethyl suberimidate. It had an isoelectric point of 4.68. Inhibition by L-tyrosine showed a Hill coefficient of 1.8 at pH 7.0, suggesting cooperative interaction between tyrosine-binding sites, and was competitive with phosphoenol pyruvate and noncompetitive with erythrose-4-phosphate.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Reference26 articles.
1. The gel-filtration behaviour of proteins related to their molecular weights over a wide range;Andrews P.;Biochem. J.,1965
2. Ballou C. E. and D. L. MacDonald. 1963. Synthesis of aldose phosphates by glycol cleavage p. 293-297. In R. L. Whistler and M. L. Wolfrom (ed.) Methods in carbohydrate chemistry vol. 2. Academic Press Inc. New York.
3. The stereochemistry of pyruvate kinase;Bondinell W. E.;Biochem. Biophys. Res. Commun.,1970
4. A stable enzyme-phosphoenolpyruvate intermediate in the synthesis of uridine-5'-diphospho-N-acety1-2-amino-2- deoxyglucose 3-0-enolpyruvyl ether;Cassidy P. J.;Biochemistry,1973
5. An improved synthesis of phosphoenol pyruvate;Clark V. M.;Biochim. Biophys. Acta,1963
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