Characterization of the pro-aminopeptidase from Aeromonas caviae T-64

被引：2

作者：

Zhang, ZZ

Nirasawa, S ^{[1
]}

Nakajima, Y

Yoshida, M

Kusakabe, I

Hayashi, K

机构：

[1] Natl Food Res Inst, Appl Enzymol Lab, Tsukuba, Ibaraki 3058642, Japan

[2] Sci Univ Tokyo, Dept Biol Sci & Technol, Noda, Chiba 2788510, Japan

[3] Univ Tsukuba, Inst Appl Biochem, Tsukuba, Ibaraki 3058572, Japan

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 2001年 / 65卷 / 02期

关键词：

Aeromonas caviae; aminopeptidase; enzyme stability; pro-enzyme; substrate specificity;

D O I：

10.1271/bbb.65.420

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：

The pro-aminopeptidase from Aeromonas caviae T-64 (pro-apAC) had maximal activity at 60 degreesC and was more stable than mature apAC at temperature up to 65 degreesC for 1 hour. The pH stability of pro-apAC ranged from 4.0 to 8.0, which is broader than the range for the mature apAC. The k(cat)/K-m of pro-apAC was 1.4% to 24% of that of mature apAC.

引用

收藏

页码：420 / 423

页数：4

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