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. 1967 Aug;104(2):369–377. doi: 10.1042/bj1040369

Specificity and stereospecificity of α-chymotrypsin

D W Ingles 1, J R Knowles 1
PMCID: PMC1270596  PMID: 6048779

Abstract

1. The optically pure p-nitrophenyl esters of the d and l enantiomers of N-acetyl-tryptophan, N-acetylphenylalanine and N-acetyl-leucine, and the p-nitrophenyl ester of N-acetylglycine, have been prepared. 2. These materials are all substrates of α-chymotrypsin, and the rates of deacylation of the corresponding acyl-α-chymotrypsins have been determined. 3. As the size of the amino acid side chain increases, the l series deacylate progressively faster than the N-acetylglycyl-enzyme, and the d series progressively more slowly. 4. The results are interpreted in terms of a three-locus model of the enzyme's active site, which accounts for the interrelationship between substrate specificity and stereospecificity observed. 5. The concepts of negative specificity and of specificity saturation are introduced.

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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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