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由一种特定的四肽醛与灰色链霉菌丝氨酸蛋白酶形成的共价复合物的晶体学和动力学研究。

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

作者信息

Brayer G D, Delbaere L T, James M N, Bauer C A, Thompson R C

出版信息

Proc Natl Acad Sci U S A. 1979 Jan;76(1):96-100. doi: 10.1073/pnas.76.1.96.

DOI:10.1073/pnas.76.1.96
PMID:106392
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC382883/
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.

摘要

X射线晶体学数据表明，一种特定的四肽醛抑制剂（N-乙酰基脯氨酰丙氨酰脯氨酰苯丙氨醛）与来自灰色链霉菌的丝氨酸蛋白酶SGPA形成了稳定的、共价的四面体加成复合物。基于动力学测量对这种连接的共价性质的早期推测得到了证实，并且这种醛抑制剂的差分电子密度图表明，在抑制剂结合时，组氨酸-57侧链发生了主要的构象变化。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/95bd/382883/9bc7eaa7e57d/pnas00001-0106-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/95bd/382883/1d5bd50aca19/pnas00001-0106-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/95bd/382883/9bc7eaa7e57d/pnas00001-0106-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/95bd/382883/1d5bd50aca19/pnas00001-0106-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/95bd/382883/9bc7eaa7e57d/pnas00001-0106-b.jpg

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1
Crystallographic and kinetic investigations of the covalent complex formed by a specific tetrapeptide aldehyde and the serine protease from Streptomyces griseus.由一种特定的四肽醛与灰色链霉菌丝氨酸蛋白酶形成的共价复合物的晶体学和动力学研究。
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本文引用的文献

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Complex between carboxypeptidase A and a hydrated ketomethylene substrate analogue.羧肽酶A与水合酮亚甲基底物类似物之间的复合物。
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Substrate binding site in bovine chymotrypsin A-gamma. A crystallographic study using peptide chloromethyl ketones as site-specific inhibitors.牛胰凝乳蛋白酶A-γ中的底物结合位点。使用肽氯甲基酮作为位点特异性抑制剂的晶体学研究。
Biochemistry. 1971 Sep 28;10(20):3728-38. doi: 10.1021/bi00796a014.
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An x-ray crystallographic study of the binding of peptide chloromethyl ketone inhibitors to subtilisin BPN'.肽氯甲基酮抑制剂与枯草杆菌蛋白酶BPN'结合的X射线晶体学研究。
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Can J Biochem. 1971 Nov;49(11):1195-201. doi: 10.1139/o71-171.
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Real-space refinement of the structure of hen egg-white lysozyme.鸡蛋清溶菌酶结构的实空间精修
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The structure of chymostatin, a chymotrypsin inhibitor.糜蛋白酶抑制剂抑肽酶的结构。
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