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. 1971 Jul;123(3):379–384. doi: 10.1042/bj1230379

The hydrolysis by thermolysin of dipeptide derivatives that contain substituted cysteine

A P Damoglou 1,*, H Lindley 1, I W Stapleton 1
PMCID: PMC1176968  PMID: 5126091

Abstract

1. The preparation of protected dipeptides of the form acetylglycylamino acid amides is described, where the amino acid is phenylalanine, leucine, valine, alanine, S-methylcysteine, S-ethylcysteine, S-benzylcysteine and S-phenylcysteine. 2. Kinetic parameters for the thermolytic hydrolysis of these blocked dipeptides are reported. The rate of hydrolysis was fastest when the amino acid was leucine or phenylalanine, slower when it was S-methylcysteine, valine or S-ethylcysteine, much slower when it was alanine, and negligible for S-phenylcysteine or S-benzylcysteine. 3. The results are compared with those for similar dipeptide derivatives with benzyloxycarbonyl and furylacryloyl blocking groups, which are hydrolysed faster.

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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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