CRYSTALLOGRAPHIC AND KINETIC INVESTIGATIONS OF THE COVALENT COMPLEX FORMED BY A SPECIFIC TETRAPEPTIDE ALDEHYDE AND THE SERINE PROTEASE FROM STREPTOMYCES-GRISEUS

被引：65
|
作者：
BRAYER, GD
DELBAERE, LTJ
JAMES, MNG
BAUER, CA
THOMPSON, RC
机构：
[1] TEMPLE UNIV,DEPT CHEM,PHILADELPHIA,PA 19122
[2] UNIV LUND,DEPT BIOCHEM,S-22007 LUND 7,SWEDEN
来源：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1979年 / 76卷 / 01期
关键词：
D O I：
10.1073/pnas.76.1.96
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
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.
引用
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页码：96 / 100
页数：5
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