Purification and Characterization of Pyridoxine 5'-Phosphate Phosphatase from Sinorhizobium meliloti
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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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- HOSHINO Tatsuo
- Department of Applied Microbiology, Nippon Roche Research Center
Bibliographic Information
- Other Title
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- Purification and Characterization of Pyridoxine 5′-Phosphate Phosphatase from<i>Sinorhizobium meliloti</i>
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Description
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.
Journal
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 69 (12), 2277-2284, 2005
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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Keywords
Details 詳細情報について
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- CRID
- 1390001206474993792
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- NII Article ID
- 130000030441
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- NII Book ID
- AA10824164
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- ISSN
- 13476947
- 09168451
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- NDL BIB ID
- 7755849
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed