Purification and Characterization of Pyridoxine 5′-Phosphate Phosphatase from<i>Sinorhizobium meliloti</i>

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  • TAZOE Masaaki
    Department of Applied Microbiology, Nippon Roche Research Center
  • ICHIKAWA Keiko
    Department of Applied Microbiology, Nippon Roche Research Center
  • HOSHINO Tatsuo
    Department of Applied Microbiology, Nippon Roche Research Center

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  • Purification and Characterization of Pyridoxine 5'-Phosphate Phosphatase from Sinorhizobium meliloti

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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.

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