BINDING CENTER OF LEUCINE AMINOPEPTIDASE - INVESTIGATIONS WITH SUBSTRATE ANALOGOUS AND SPIN-LABELED INHIBITORS

被引：6

作者：

FITTKAU, S ^{[1
]}

KAMMERER, G ^{[1
]}

DAMERAU, W ^{[1
]}

机构：

[1] ACAD SCI GDR,CENT INST MOLEC BIOL,BERLIN,GER DEM REP

来源：

OPHTHALMIC RESEARCH | 1979年 / 11卷 / 5-6期

关键词：

D O I：

10.1159/000265038

中图分类号：

R77 [眼科学];

学科分类号：

100212 ;

摘要：

As shown by kinetic experiments with competitive inhibitors like Thr(But)-Phe-X peptide ligans are bound by hydrophobic interactions at two nonpolar subsites S1 and S2. This contact region prefers with high selectivity L-configuration in P1 and P2 position. The additional binding P3-S3 differs in polarity and stereospecifical requirement. The nitroxide-labeled inhibitor Thr(But)-Phe-SL is competitively bound at two types of binding sites. The main type, obtained from electron spin resonance spectroscopy, is in agreement with results from kinetic studies and represents the binding of two inhibitor molecules per subunit of the enzyme.

引用

页码：381 / 385

页数：5