文章基本信息

标题：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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作者：G D Brayer ; L T Delbaere ; M N James 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1979
卷号：76
期号：1
页码：96-100
DOI：10.1073/pnas.76.1.96
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.