Purification and characterization of adenosine 5'-phosphosulfate kinase from the Thermophilic bacterium Bacillus stearothermophilus

被引：6

作者：

Onda, M

Hayashi, M

Suiko, M

Liu, MC

Nakajima, H

机构：

[1] MIYAZAKI UNIV, DEPT BIOL RESOURCE SCI, MIYAZAKI 88921, JAPAN

[2] UNIV TEXAS, CTR HLTH, DEPT BIOCHEM, TYLER, TX 75710 USA

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1996年 / 60卷 / 01期

关键词：

APS kinase; thermophilic bacterium; ATP sulfurylase; adenosine 5'-phosphosulfate; 3'-phosphoadenosine-5'-phosphosulfate;

D O I：

10.1271/bbb.60.134

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：

Adenosine 5'-phosphosulfate (APS) kinase from a thermophilic bacterium, Bacillus stearothermophilus, was purified to apparent homogeneity. The apparent molecular weight was 50 kDa, consisting of two 26-kDa subunits, The enzyme was very thermostable and lacked cysteine and methionine residues, Enzyme activity was more stimulated with Mn2+, Zn2+, or Co2+ than with Mg2+ and the K-m for ATP and APS mere 220 mu M and 42 mu M, respectively.

引用

页码：134 / 136

页数：3