P1-specificity of aqualysin I (a subtilisin-type serine protease) from Thermus aquaticus YT-1, using P1-substituted derivatives of Streptomyces subtilisin inhibitor

被引：9

作者：

Tanaka, T

Matsuzawa, H

Kojima, S

Kumagai, I

Miura, K

Ohta, T

机构：

[1] Univ Tokyo, Dept Biotechnol, Bunkyo Ku, Tokyo 1138657, Japan

[2] Univ Tokyo, Dept Ind Chem, Fac Engn, Bunkyo Ku, Tokyo 1138657, Japan

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1998年 / 62卷 / 10期

关键词：

aqualysin I; alkaline serine protease; subtilisin; substrate specificity; Streptomyces subtilisin inhibitor;

D O I：

10.1271/bbb.62.2035

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Aqualysin I is an alkaline serine protease isolated from Thermus aquaticus YT-1, an extreme thermophile. We have measured the P1-specificity of aqualysin I, using wildtype and five P1-substituted derivatives of Streptomyces subtilisin inhibitor (SSI). SSIs efficiently inhibited the activity of aqualysin I, with low substrate specificity. Charge and hydrophobicity of side chain of the P1 amino acid residue showed no significant effect to the P1-specificity of this enzyme.

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收藏

页码：2035 / 2038

页数：4

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