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Masaaki Onda, Mayumi Hayashi, Masahito Suiko, Ming-Cheh Liu, Hiroshi Nakajima, Purification and Characterization of Adenosine 5′-Phosphosulfate Kinase from the Thermophilic Bacterium Bacillus stearothermophilus, Bioscience, Biotechnology, and Biochemistry, Volume 60, Issue 1, 1 January 1996, Pages 134–136, https://doi.org/10.1271/bbb.60.134
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Abstract
Adenosine 5′-phosphosulfate (APS) kinase from a thermophilic bacterium, Bacillus st ear other mophilus, 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 Km for ATP and APS were 220 µM and 42 µM, respectively.