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. 1979 Jan;76(1):96–100. doi: 10.1073/pnas.76.1.96

Crystallographic and kinetic investigations of the covalent complex formed by a specific tetrapeptide aldehyde and the serine protease from Streptomyces griseus.

G D Brayer, L T Delbaere, M N James, C A Bauer, R C Thompson
PMCID: PMC382883  PMID: 106392

Abstract

X-ray crystallographic data show that a specific tetrapeptide aldehyde inhibitor (N-acetylprolylalanylprolylphenylalaninal) forms a stable, covalent, tetrahedral addition complex with the serine protease, SGPA, from Streptomyces griseus. Earlier proposals, based on kinetic measurements, for the covalent nature of such linkages are confirmed, and the difference electron density map of this aldehyde inhibitor indicates that a major conformational change of the histidyl-57 side chain occurs on inhibitor binding.

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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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