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.
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