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

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 76 ·No. 1 ·1979-01-00 ·Pages 96-100

Brayer GD, Delbaere LT, James MN, Bauer CA, Thompson RC

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.

MeSH Terms

Aldehydes/pharmacology Binding Sites Crystallography Endopeptidases Kinetics Oligopeptides/pharmacology Protease Inhibitors Protein Binding Protein Conformation Serine Streptomyces griseus/enzymology Structure-Activity Relationship

Chemicals

Aldehydes Oligopeptides Protease Inhibitors Serine Endopeptidases

Authors & Affiliations

5 authors, click to expand affiliations / ORCID

Brayer G D

Delbaere L T

James M N

Bauer C A

Thompson R C

References (31)

31 references, click to expand

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Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.76.1.96

Published

1979-01-00

Pages

96-100

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC382883

Subset

External Links

PubMed source DOI: 10.1073/pnas.76.1.96 PMC Full Text View journal details

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

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