Abstract
IT has recently been suggested1 that the apparent first-order kinetics observed in the hydrolysis of certain synthetic substrates (for example, acetyl-L-phenylalanyl-L-tyrosine) by pepsin could be explained if one of the hydrolysis products (acetyl-L-phenyl-alanine) were only slowly released from the enzyme, as indicated in the following scheme: where k 4<k 3. (A, acetyl-L-phenylalanine; B, L-tyrosine. The small letters will be used as symbols for the concentrations of the various species, in the equations which follow.) The reaction-rate was measured by the rate of production of B (L-tyrosine amino nitrogen). This scheme would not, however, explain the observed results.
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Baker, L. E., J. Biol. Chem., 211, 701 (1954).
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GREEN, N. Action of Pepsin on Synthetic Substrates. Nature 178, 145 (1956). https://doi.org/10.1038/178145a0
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DOI: https://doi.org/10.1038/178145a0
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