Polyphosphate-Phosphatase : Induction, Localization and Purification from Klebsiella sp. LF 1202

概要

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A bacterial strain, Klebsiella sp. LF 1202,which was isolated from soil as an adenosine-assimilating bacterium (Ling, F/ et al., Agric. Biol. Chem., 55,573-575,1991), was able to use polyphosphate as a source of phosphorus. The bacterium possessed a polyphosphate-phosphatase, an inducible enzyme located in a periplasmic space of the bacterium. The enzyme was purified to a homogenous state on SDS-PAGE, and found to consist of four identical subunits with a molecular weight of 24,000. The enzyme exhibited activity towards tri-, tetra-, hexa-, octa-, and decapolyphosphate at pH 8.0,but not towards pyrophosphate and metaphosphate. The enzyme did not require metal ions for activity, but its activity was strongly inhibited by Zn^<2+>. Chelating agents such as EDTA and CDTA did not affect activity. Since the enzyme activity was not affected by diisopropylfluorophosphate, serine residues do not seem to be involved in the activity.
社団法人日本生物工学会の論文
1993-05-25