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Volumn 66, Issue 5, 2002, Pages 1022-1031

Purification, molecular cloning, and characterization of pyridoxine 4-oxidase from microbacterium luteolum

Author keywords

Flavoprotein; GMC oxidoreductase; Metabolic pathway; Vitamin B6

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; MESORHIZOBIUM; MESORHIZOBIUM LOTI; MICROBACTERIUM; MICROBACTERIUM LUTEOLUM; PROKARYOTA;

EID: 0036559818     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.66.1022     Document Type: Article
Times cited : (17)

References (24)
  • 1
    • 85012583553 scopus 로고
    • The metabolism of vitamin B6
    • Florkin, M. and Stotz, E. H., Elsevier /North Holland, New York, vol
    • 6. In “Comprehensive Biochemistry” eds. Florkin, M. and Stotz, E. H., Elsevier /North Holland, New York, vol. 21, pp. 47-67 (1971).
    • (1971) Comprehensive Biochemistry , vol.21 , pp. 47-67
    • Snell, E.E.1    Haskell, B.E.2
  • 2
    • 0022929840 scopus 로고
    • Enzymes of vitamin B6 degradation. Purification and properties of 5-pyri-doxic acid oxygenase from Arthrobacter sp
    • 6 degradation. Purification and properties of 5-pyri-doxic acid oxygenase from Arthrobacter sp. J. Biol. Chem., 261, 15115-15120 (1986).
    • (1986) J. Biol. Chem. , vol.261 , pp. 15115-15120
    • Nelson, M.J.1    Snell, E.E.2
  • 3
    • 0014690503 scopus 로고
    • The bacterial oxidation of vitamin B6. V. The enzymatic formation of pyridoxal and isopyridoxal from pyridoxine
    • 6. V. The enzymatic formation of pyridoxal and isopyridoxal from pyridoxine. J. Biol. Chem., 244, 2577-2584 (1969).
    • (1969) J. Biol. Chem. , vol.244 , pp. 2577-2584
    • Sundaram, T.K.1    Snell, E.E.2
  • 4
    • 85009634128 scopus 로고    scopus 로고
    • Purification and characterization of pyridoxal 4-dehydrogenase from Microbacterium luteolum
    • press
    • Trongpanich, Y., Abe, K., Kaneda, Y., Morita, T., and Yagi, T., Purification and characterization of pyridoxal 4-dehydrogenase from Microbacterium luteolum. Biosci. Biotechnol. Biochem., in press.
    • Biosci. Biotechnol. Biochem
    • Trongpanich, Y.1    Abe, K.2    Kaneda, Y.3    Morita, T.4    Yagi, T.5
  • 5
    • 0022351341 scopus 로고
    • A simple preparation method for apoaspartate aminotransferase from Escherichia coli B, and its application for the assay of pyridoxal and pyridoxamine 5β-phosphate
    • Yagi, T., Kirino, J., Yamamoto, S. and Nozaki, M., A simple preparation method for apoaspartate aminotransferase from Escherichia coli B, and its application for the assay of pyridoxal and pyridoxamine 5β-phosphate 98, 921-926 (1985).
    • (1985) J. Biochem. (Tokyo) , vol.98 , pp. 921-926
    • Yagi, T.1    Kirino, J.2    Yamamoto, S.3    Nozaki, M.4
  • 6
    • 0001515809 scopus 로고
    • The enzymatic oxidation of pyridoxine and pyridoxamine phosphate
    • Wada, H. and Snell, E. E., The enzymatic oxidation of pyridoxine and pyridoxamine phosphate. J. Biol. Chem., 236, 2089-2095 (1961).
    • (1961) J. Biol. Chem. , vol.236 , pp. 2089-2095
    • Wada, H.1    Snell, E.E.2
  • 7
    • 0018865050 scopus 로고
    • Use of 3,5-dichloro-2-hydroxybenzenesulfonic acid /4-aminophenazone chromogenic system in direct enzymic assay of uric acid in serum and urine
    • Fossati, P., Principe, L., and Berti, G., Use of 3,5-dichloro-2-hydroxybenzenesulfonic acid /4-aminophenazone chromogenic system in direct enzymic assay of uric acid in serum and urine. Clin. Chem., 26, 227-231 (1980).
    • (1980) Clin. Chem. , vol.26 , pp. 227-231
    • Fossati, P.1    Principe, L.2    Berti, G.3
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Chem., 72, 248-254 (1976).
    • (1976) Anal. Chem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 10
    • 50549178319 scopus 로고
    • Preparation of transforming deoxyribonucleic acid by phenol treatment
    • Saito, H. and Miura, K., Preparation of transforming deoxyribonucleic acid by phenol treatment. Biochim. Biophys. Acta, 72, 619-629 (1963).
    • (1963) Biochim. Biophys. Acta , vol.72 , pp. 619-629
    • Saito, H.1    Miura, K.2
  • 11
    • 0033551692 scopus 로고    scopus 로고
    • Purification, molecular cloning, and catalytic activity of Schizosaccharomyces pombe pyridoxal reductase. A possible additional family in the aldo-keto reductase superfamily
    • Nakano, M., Morita, T., Yamamoto, T., Sano, H., Ashiuchi, M., Masui, R., Kuramitsu, S., and Yagi, T., Purification, molecular cloning, and catalytic activity of Schizosaccharomyces pombe pyridoxal reductase. A possible additional family in the aldo-keto reductase superfamily. J. Biol. Chem., 274, 23185-23190 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 23185-23190
    • Nakano, M.1    Morita, T.2    Yamamoto, T.3    Sano, H.4    Ashiuchi, M.5    Masui, R.6    Kuramitsu, S.7    Yagi, T.8
  • 12
    • 0032053878 scopus 로고    scopus 로고
    • Growth phase-dependent active transport of pyridoxine in a fission yeast, Schizosaccharomyces pombe
    • Yagi, T., Tanouchi, A., and Hiraoka, Y., Growth phase-dependent active transport of pyridoxine in a fission yeast, Schizosaccharomyces pombe. FEMS Microbial. Lett., 161, 145-150 (1998).
    • (1998) FEMS Microbial. Lett. , vol.161 , pp. 145-150
    • Yagi, T.1    Tanouchi, A.2    Hiraoka, Y.3
  • 13
    • 0028177441 scopus 로고
    • Measurement of endogenous and TNF a-mediated H2O2 production in supernatants of SK-N-SH neuroblastoma cells with an enhanced chemiluminescence assay
    • 2 production in supernatants of SK-N-SH neuroblastoma cells with an enhanced chemiluminescence assay. J. Biolumin. Chemilumin., 9, 267-272 (1994).
    • (1994) J. Biolumin. Chemilumin. , vol.9 , pp. 267-272
    • Carmine, T.C.1    Bruchelt, G.2    Hahn, T.3    Nielthammer, D.4
  • 14
    • 0018845283 scopus 로고
    • Activity staining for flavoprotein oxidase
    • Tsuge, H. and Nakanishi, Y., Activity staining for flavoprotein oxidase. Methods Enzymol., 66, 344-350 (1980).
    • (1980) Methods Enzymol. , vol.66 , pp. 344-350
    • Tsuge, H.1    Nakanishi, Y.2
  • 15
    • 78651153791 scopus 로고
    • Method and application to human serum proteins
    • Davis, B. J., Method and application to human serum proteins. Ann. NY. Acad. Sci., 121, 404-427 (1964).
    • (1964) Ann. NY. Acad. Sci. , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 18
    • 0025883547 scopus 로고
    • Characterization of an Escherichia coli gene encoding betaine aldehyde dehydrogenase (BADH): Structural similarity to mammalian ALDHs and a plant BADH
    • Boyd, L. A., Adam, L., Pelcher, L. E., McHughen, A., Hirji, R., and Selvaraj, G., Characterization of an Escherichia coli gene encoding betaine aldehyde dehydrogenase (BADH): structural similarity to mammalian ALDHs and a plant BADH. Gene, 103, 45-52 (1991).
    • (1991) Gene , vol.103 , pp. 45-52
    • Boyd, L.A.1    Adam, L.2    Pelcher, L.E.3    McHughen, A.4    Hirji, R.5    Selvaraj, G.6
  • 19
    • 0031946706 scopus 로고    scopus 로고
    • Ntn genes determining the early steps in the divergent catabolism of 4-nitrotoluene and toluene in Pseudomonas sp. Strain TW3
    • James, K. D. and Williams, P. A., Ntn genes determining the early steps in the divergent catabolism of 4-nitrotoluene and toluene in Pseudomonas sp. strain TW3. J. Bacteriol., 180, 2043-2049 (1998).
    • (1998) J. Bacteriol. , vol.180 , pp. 2043-2049
    • James, K.D.1    Williams, P.A.2
  • 21
    • 0026672013 scopus 로고
    • Characterization of the complex pdxH-tryS operon of Escherichia coli K-12 and pleiotropic phenotypes caused by pdxH insertion mutations
    • Lam, H. M. and Winkler, M. E., Characterization of the complex pdxH-tryS operon of Escherichia coli K-12 and pleiotropic phenotypes caused by pdxH insertion mutations. J. Bacteriol., 174, 6033-6045 (1992).
    • (1992) J. Bacteriol. , vol.174 , pp. 6033-6045
    • Lam, H.M.1    Winkler, M.E.2
  • 22
    • 0030739874 scopus 로고    scopus 로고
    • Gene cloning, sequence analysis, and expression of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase
    • Chaiyen, P., Ballou, D. P., and Massey, V., Gene cloning, sequence analysis, and expression of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase. Proc. Natl. Acad. Sci. USA, 94, 7233-7238 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7233-7238
    • Chaiyen, P.1    Ballou, D.P.2    Massey, V.3
  • 23
    • 0030774720 scopus 로고    scopus 로고
    • Prediction of protein secondary structure using the 3D-1D compatibility algorithm
    • Ito, M., Matsuo, Y., and Nishikawa, K., Prediction of protein secondary structure using the 3D-1D compatibility algorithm. Comput. Appl. Biosci., 13, 415-424 (1997).
    • (1997) Comput. Appl. Biosci. , vol.13 , pp. 415-424
    • Ito, M.1    Matsuo, Y.2    Nishikawa, K.3
  • 24
    • 0027397187 scopus 로고
    • Crystal structure of glucose oxidase from Aspergillus niger refined at 2.3 A resolution
    • Hecht, H. J., Kalisz, H. M., Hendle, J., Schmid, R. D., and Schomburg, D., Crystal structure of glucose oxidase from Aspergillus niger refined at 2.3 A resolution. J. Mol. Biol., 229, 153-172 (1993).
    • (1993) J. Mol. Biol. , vol.229 , pp. 153-172
    • Hecht, H.J.1    Kalisz, H.M.2    Hendle, J.3    Schmid, R.D.4    Schomburg, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.