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References
Barendrecht, H. P., Z. Physik. Chem., 49, 456 (1904).
Henri, V., Lois générales de l'action des diastases (Hermann, Paris, 1903). See Segal, H. L., in The Enzymes, edit. by Boyer, P., Lardy, H. A., and Myrback, K., 1, for a review of the early historical aspects of this topic.
Michaelis, L., and Menten, M. L., Biochem. Z., 49, 333 (1913).
Dixon, M., and Thurlow, S., Biochem. J., 18, 976 (1924).
Walter, C., Advances in Chemical Physics (in the press).
Cellular Regulatory Mechanisms, Cold Spring Harbor Symp. Quant. Biol., Cold Spring Harbor, 26, Section by Monod and Jacob, 390.
Feedback inhibitors are much less likely to be limited to the substrate site. Pardee, A. B., and Gerhart, J. C., (J. Biol. Chem., 237, 891; 1962), report a recent interesting example of a feedback inhibitor of aspartate transcarbamylase, cytidine triphosphate, which appears to bind to this enzyme, at a site different from that which binds the substrate, aspartate.
Walter, C., and Frieden, E., Adv. in Enzymol. (in the press). See Walter, C., and Frieden, E., Fed. Proc., 20, 229 (1961) for an earlier abstract.
Spangler, R. A., and Snell, F. M., Nature, 191, 457 (1961).
Broh-Kahn, R. H., and Mirsky, I. A., Arch. Biochem., 16, 87 (1948).
Calculated using the integrated inhibition equations, for example (25) and (28), 102, Chap. 4 in Laidler, K. J., The Chemical Kinetics of Enzyme Action (Clarendon Press, Oxford, England, 1958).
Schonheyder, F., Biochem. J., 50, 378 (1952).
Huang, H. T., and Niemann, C., J. Amer. Chem. Soc., 73, 1541 (1951).
Schwimmer, S., Biochim. Biophys. Acta, 48, 132 (1961).
Straus, O. H., and Goldstein, A., J. Gen. Physiol., 26, 564 (1943).
Ackermann, W. W., and Potter, V. R., Proc. Soc. Exp. Biol. Med., 72, 1 (1949).
Werkheiser, W. C., J. Biol. Chem., 236, 888 (1961).
Dawson, C. R., Malette, M. F., et al., in A Symposium on Copper Meta-bolism, edit. by McElroy, W. D., and Glass, B. (Johns Hopkins Press, Baltimore, 1950).
Frieden, E., and Maggiolo, I., Biochim. Biophys. Acta, 24, 42 (1957).
Frieden, E., in Horizons in Biochemistry, edit. by Kasha, M., and Pullman, B., 461 (Academic Press, New York, 1962).
Zatman, L. J., Kaplan, N. O., Colowick, S. P., and Ciotti, M., J. Biol. Chem., 200, 197 (1953); 209, 453,467 1954.
Neuhaus, F. C., and Byrne, W. L., J. Biol. Chem., 235, 2019 (1960).
Boyer, P. D., Harrison, W. H., in The Mechanism of Enzyme Action, edit. by McElroy, W. D., and Glass, B., 658 (Johns Hopkins Press, Baltimore, Md., 1954).
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FRIEDEN, E., WALTER, C. Prevalence and Significance of the Product Inhibition of Enzymes. Nature 198, 834–837 (1963). https://doi.org/10.1038/198834a0
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DOI: https://doi.org/10.1038/198834a0
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