Cloning of Phosphatase I Gene from a Psychrophile, Shewanella sp., and Some Properties of the Recombinant Enzyme.
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概要
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Psychrophilic phosphatase I from Shewanella sp. is a cold enzyme that was found as a novel protein-tyrosine-phosphatase (PTPase, EC 3. 1. 3. 48) with a histidine as its catalytic residue [Tsuruta and Aizono (1999) J. Biochem. 125, 690-695]. Here, we determined the nucleotide sequence of a DNA fragment (2, 004 bp) containing the phosphatase I gene by cloning with polymerase chain reaction (PCR) and inverted PCR techniques. The deduced amino acid sequence, of the enzyme contained a conserved region of proteinserineithreonine-phosphatase (PPase). The 38.5 kDa-recombinant protein expressed in Escherichia coli was purified to homogeneity by glutathione-Sepharose 4 B column chromatography, treatment with endoproteinase and Mono-Q column chromatography. The recombinant enzyme had a specific activity of 49.4 units and, like native psychrophilic phosphatase I, exhibited high catalytic activity at low temperature and PTPase activity.
- 社団法人 日本生化学会の論文
著者
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Aizono Yasuo
Laboratory Of Biological Chemistry Department Of Biofunctinal Chemistry Faculty Of Agriculture Kobe
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Tsuruta Hiroki
Laboratory of Biological Chemistry Department of Biofunctional Chemistry Faculty of Agriculture, Kobe University
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Tsuruta Hiroki
Laboratory of Biochemistry, Department of Biofunctional Chemistry, Faculty of Agriculture, Kobe University
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Aizono Yasuo
Laboratory of Biochemistry, Department of Biofunctional Chemistry, Faculty of Agriculture, Kobe University
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