New chromophore substrates of aspartic proteases

被引：0

作者：

Litvinova, OV ^{[1
]}

Balandina, GN ^{[1
]}

机构：

[1] Moscow MV Lomonosov State Univ, Fac Chem, Moscow 119899, Russia

来源：

BIOORGANICHESKAYA KHIMIYA | 1999年 / 25卷 / 08期

关键词：

aspartic protease; chromophore substrate; protease activity;

D O I：

暂无

中图分类号：

学科分类号：

摘要：

Chromophore substrates Dnp-Ala-Glu-Phe-Phe-Arg-Arg-NH2 and Dnp-Ala-Ala-Phe-Nle-Ala-Arg-NH2 of aspartic proteases were synthesized by a combination of chemical and enzymic methods. The kinetic parameters of their hydrolysis with pepsin, aspergyllopepsin, and chymosin were determined. The introduction of Nle in the P'(1) position gives stable enzyme-substrate complexes with pepsin and chymosin. A Glu residue at the P-2 position contributes significantly to an increase in k(cat) for the chymosin hydrolysis.

引用

页码：581 / 583

页数：3

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