Purification and Characterization of Pyridoxine 5'-Phosphate Phosphatase from Sinorhizobium meliloti
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概要
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Here we report the purification and biochemical characterization of a pyridoxine 5′-phosphate phosphatase involved in the biosynthesis of pyridoxine in Sinorhizobium meliloti. The phosphatase was localized in the cytoplasm and purified to electrophoretic homogeneity by a combination of EDTA/lysozyme treatment and five chromatography steps. Gel-filtration chromatography with Sephacryl S-200 and SDS/PAGE demonstrated that the protein was a monomer with a molecular size of approximately 29 kDa. The protein required divalent metal ions for pyridoxine 5′-phosphate phosphatase activity, and specifically catalyzed the removal of Pi from pyridoxine and pyridoxal 5′-phosphates at physiological pH (about 7.5). It was inactive on pyridoxamine 5′-phosphate and other physiologically important phosphorylated compounds. The enzyme had the same Michaelis constant (Km) of 385 μM for pyridoxine and pyridoxal 5′-phosphates, but its specific constant [maximum velocity (Vmax)⁄Km] was nearly 2.5 times higher for the former than for the latter.
- 社団法人 日本農芸化学会の論文
- 2005-12-23
著者
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Hoshino Tatsuo
Departments of Medicine, Keio University and The Lankenau Hospital
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Hoshino T
Department Of Applied Microbiology Nippon Roche Research Center
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TAZOE Masaaki
Department of Applied Microbiology, Nippon Roche Research Center
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ICHIKAWA Keiko
Department of Applied Microbiology, Nippon Roche Research Center
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Tazoe Masaaki
Department Of Applied Microbiology Nippon Roche Research Center
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Hoshino Tatsuo
Department Of Applied Microbiology Nippon Roche Research Center
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Tazoe M
Department Of Applied Microbiology Nippon Roche Research Center
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Ichikawa Kimihisa
Department Of Applied Microbiology Nippon Roche Research Center
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