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. 1969 Jun;113(2):363–368. doi: 10.1042/bj1130363

The inhibition of pepsin-catalysed reactions by products and product analogues. Kinetic evidence for ordered release of products

P Greenwell 1, J R Knowles 1, Hilary Sharp 1
PMCID: PMC1184643  PMID: 4897199

Abstract

1. The inhibition of pepsin-catalysed hydrolysis of N-acetyl-l-phenylalanyl-l-phenylalanylglycine by products and product analogues was studied. 2. The non-competitive nature of the inhibition by the product N-acetyl-l-phenylalanine confirms an ordered release of products, and points to a common mechanism (involving an amino-enzyme) for pepsin-catalysed transpeptidation and hydrolysis reactions. 3. N-Acetyl-l-phenylalanine ethyl ester is also a non-competitive inhibitor, but here the inhibition is of the `dead-end' type. No ethanol is detectable in reaction mixtures, indicating that this ester cannot act as an amino group acceptor in a transpeptidation process. 4. The same is true for N-methanesulphonyl-l-phenylalanine methyl and methyl thiol esters. No methanethiol is liberated when the methyl thiol ester is present as an inhibitor of the hydrolytic reaction, and the hope that such a thiol ester would effectively trap the amino-enzyme was not fulfilled.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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