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Volumn 109, Issue 1, 2010, Pages 1-12

Mineral phosphate solubilization by rhizosphere bacteria and scope for manipulation of the direct oxidation pathway involving glucose dehydrogenase

Author keywords

Direct oxidation pathway; Gluconic acid; Glucose dehydrogenase; Mineral phosphate solubilization; Rhizosphere bacteria

Indexed keywords

BACTERIA; BIODIVERSITY; CROPS; GENES; GLUCOSE; METABOLITES; MINERALS; MOLECULES; NITROGEN; OXIDATION; SOLUBILITY;

EID: 77953580261     PISSN: 13645072     EISSN: 13652672     Source Type: Journal    
DOI: 10.1111/j.1365-2672.2009.04654.x     Document Type: Review
Times cited : (168)

References (107)
  • 1
    • 0032724927 scopus 로고    scopus 로고
    • Effects of inoculation of EPS-producing Pantoea agglomerans on wheat rhizosphere aggregation
    • Amellal, N., Bartoli, F., Villemin, G., Talouizte, A. Heulin, T. (1999) Effects of inoculation of EPS-producing Pantoea agglomerans on wheat rhizosphere aggregation. Plant Soil 211, 93 101.
    • (1999) Plant Soil , vol.211 , pp. 93-101
    • Amellal, N.1    Bartoli, F.2    Villemin, G.3    Talouizte, A.4    Heulin, T.5
  • 2
    • 0000017215 scopus 로고
    • D-Glucose dehydrogenase of Gluconobacter suboxydans: Solubilization, purification and characterization
    • Ameyama, M., Shinagawa, E., Matsushita, K. Adachi, O. (1981) D-Glucose dehydrogenase of Gluconobacter suboxydans: solubilization, purification and characterization. Agric Biol Chem 45, 851-861.
    • (1981) Agric Biol Chem , vol.45 , pp. 851-861
    • Ameyama, M.1    Shinagawa, E.2    Matsushita, K.3    Adachi, O.4
  • 3
    • 0022372833 scopus 로고
    • Production of 2-keto-L-gluconate, an intermediate in L-ascorbate synthesis, by a genetically modified Erwinia herbicola
    • Anderson, S., Marks, C.B., Lazarus, R., Miller, J., Stafford, K., Seymour, J., Light, D., Rastetter, W. et al. (1985) Production of 2-keto-L-gluconate, an intermediate in L-ascorbate synthesis, by a genetically modified Erwinia herbicola. Science 230, 144-149.
    • (1985) Science , vol.230 , pp. 144-149
    • Anderson, S.1    Marks, C.B.2    Lazarus, R.3    Miller, J.4    Stafford, K.5    Seymour, J.6    Light, D.7    Rastetter, W.8
  • 4
    • 0002205775 scopus 로고
    • Quinoproteins and energy transduction
    • In. ed. Anthony, C.
    • Anthony, C. (1988) Quinoproteins and energy transduction. In Bacterial Energy Transduction ed. Anthony, C. pp. 293 315.
    • (1988) Bacterial Energy Transduction , pp. 293-315
    • Anthony, C.1
  • 5
    • 0032465177 scopus 로고    scopus 로고
    • Potential of Rhizobium and Bradyrhizobium species as plant growth promoting rhizobacteria with non-legumes: Effect on radishes (Raphanus sativus L.)
    • Antoun, H., Beauchamp, C.J., Goussard, N., Chabot, R. Lalande, R. (1998) Potential of Rhizobium and Bradyrhizobium species as plant growth promoting rhizobacteria with non-legumes: effect on radishes (Raphanus sativus L.). Plant Soil 204, 57-67.
    • (1998) Plant Soil , vol.204 , pp. 57-67
    • Antoun, H.1    Beauchamp, C.J.2    Goussard, N.3    Chabot, R.4    Lalande, R.5
  • 7
    • 0028872307 scopus 로고
    • Interaction between barley and mixed cultures of nitrogen fixing and phosphate-solubilizing bacteria
    • Belimov, A.A., Kojemiakov, A.P. Chuvarliyeva, C.V. (1995) Interaction between barley and mixed cultures of nitrogen fixing and phosphate-solubilizing bacteria. Plant Soil 173, 29-37.
    • (1995) Plant Soil , vol.173 , pp. 29-37
    • Belimov, A.A.1    Kojemiakov, A.P.2    Chuvarliyeva, C.V.3
  • 8
    • 0028163513 scopus 로고
    • Influence of low-molecular weight organic acids on the solubilization of phosphates
    • Bolan, N.S., Naidu, R., Mahimairaja, S. Baskaran, S. (1994) Influence of low-molecular weight organic acids on the solubilization of phosphates. Biol Fertil Soils 18, 311-319.
    • (1994) Biol Fertil Soils , vol.18 , pp. 311-319
    • Bolan, N.S.1    Naidu, R.2    Mahimairaja, S.3    Baskaran, S.4
  • 9
    • 0003101374 scopus 로고
    • Oxidative d-xylose metabolism of Gluconobacter oxydans
    • Buchert, J. Viikari, L. (1988) Oxidative d-xylose metabolism of Gluconobacter oxydans. Appl Microbiol Biotechnol 29, 375-379.
    • (1988) Appl Microbiol Biotechnol , vol.29 , pp. 375-379
    • Buchert, J.1    Viikari, L.2
  • 10
    • 0033508343 scopus 로고    scopus 로고
    • Screening for plant growth promoting rhizobacteria to promote early soybean growth
    • Cattelan, A.J., Hartel, P.G. Furhmann, F.F. (1999) Screening for plant growth promoting rhizobacteria to promote early soybean growth. Soil Sci Soc Am J 63, 1670-1680.
    • (1999) Soil Sci Soc Am J , vol.63 , pp. 1670-1680
    • Cattelan, A.J.1    Hartel, P.G.2    Furhmann, F.F.3
  • 11
    • 0032192639 scopus 로고    scopus 로고
    • Effect of phosphorus on root colonization and growth promotion of maize by bioluminescent mutants of phosphate solubilizing Rhizobium leguminosarum biovar Phaseoli
    • Chabot, R., Beauchamp, C.J., Kloepper, J.W. Antoun, H. (1998) Effect of phosphorus on root colonization and growth promotion of maize by bioluminescent mutants of phosphate solubilizing Rhizobium leguminosarum biovar Phaseoli. Soil Biol Biochem 30, 1615-1618.
    • (1998) Soil Biol Biochem , vol.30 , pp. 1615-1618
    • Chabot, R.1    Beauchamp, C.J.2    Kloepper, J.W.3    Antoun, H.4
  • 12
    • 20544473294 scopus 로고    scopus 로고
    • Isolation and characterization of phosphate solubilizing bacteria from the rhizosphere of crop plants of Korea
    • DOI 10.1016/j.soilbio.2005.02.025, PII S0038071705000957
    • Chung, H., Park, M., Madhaiyan, M., Seshadri, S., Song, J., Cho, H. Sa, T. (2005) Isolation and characterization of phosphate solubilizing bacteria from the rhizosphere of crop plants of Korea. Soil Biol and Biochem 37, 1970-1974. (Pubitemid 40837270)
    • (2005) Soil Biology and Biochemistry , vol.37 , Issue.10 , pp. 1970-1974
    • Chung, H.1    Park, M.2    Madhaiyan, M.3    Seshadri, S.4    Song, J.5    Cho, H.6    Sa, T.7
  • 13
    • 0023874871 scopus 로고
    • Cloning of the gene encoding quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus: Evidence for the presence of a second enzyme
    • Cleton-Jansen, A.-M., Goosen, N., Wenzel, T.J. van de Putte, P. (1988) Cloning of the gene encoding quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus: evidence for the presence of a second enzyme. J Bacteriol 170, 2121-2125.
    • (1988) J Bacteriol , vol.170 , pp. 2121-2125
    • Cleton-Jansen, A.-M.1    Goosen, N.2    Wenzel, T.J.3    Van De Putte, P.4
  • 15
    • 0025188604 scopus 로고
    • Cloning mapping and sequencing of the gene encoding Escherichia coli quinoprotein glucose dehydrogenase
    • Cleton-Jansen, A.-M., Goosen, N., Fayet, O. van de Putte, P. (1990) Cloning mapping and sequencing of the gene encoding Escherichia coli quinoprotein glucose dehydrogenase. J Bacteriol 172, 6308-6315.
    • (1990) J Bacteriol , vol.172 , pp. 6308-6315
    • Cleton-Jansen, A.-M.1    Goosen, N.2    Fayet, O.3    Van De Putte, P.4
  • 16
    • 0025939984 scopus 로고
    • A Single amino acid substitution changes the substrate specificity of quinoprotein glucose dehydrogenase in Gluconobacter oxydans
    • Cleton-Jansen, A.-M., Dekker, S., van de Putte, P. Goosen, N. (1991) A Single amino acid substitution changes the substrate specificity of quinoprotein glucose dehydrogenase in Gluconobacter oxydans. Mol Gen Genet 229, 206-212.
    • (1991) Mol Gen Genet , vol.229 , pp. 206-212
    • Cleton-Jansen, A.-M.1    Dekker, S.2    Van De Putte, P.3    Goosen, N.4
  • 18
    • 77953606039 scopus 로고    scopus 로고
    • New molecular tools for enhancing methane production, explaining thermodynamically limited lifestyles and other important biotechnological issues
    • Daniels, C., Michan, C. Ramos, J.L. (2009) New molecular tools for enhancing methane production, explaining thermodynamically limited lifestyles and other important biotechnological issues. Microb Biotechnol 2, 533-536.
    • (2009) Microb Biotechnol , vol.2 , pp. 533-536
    • Daniels, C.1    Michan, C.2    Ramos, J.L.3
  • 19
    • 84984473595 scopus 로고
    • Carbon metabolism
    • In. ed. Calcott, P.H.
    • Dawes, E.A. (1981) Carbon metabolism. In Continuous culture of cells, Vol. 2, ed. Calcott, P.H. pp. 1 38.
    • (1981) Continuous culture of cells , vol.2 , pp. 1-38
    • Dawes, E.A.1
  • 20
    • 84936906704 scopus 로고
    • Solubilization of minerals and related materials by 2-ketogluconic acid producing bacteria
    • Duff, R.B., Webley, D.M. Scott, R.O. (1963) Solubilization of minerals and related materials by 2-ketogluconic acid producing bacteria. Soil Sci 95, 105-114.
    • (1963) Soil Sci , vol.95 , pp. 105-114
    • Duff, R.B.1    Webley, D.M.2    Scott, R.O.3
  • 21
    • 0025830659 scopus 로고
    • Quinoproteins: Enzymes containing the quinonoid cofactor pyrroloquinoline quinone, topaquinone or tryptophan-tryptophan quinone
    • Duine, J.A. (1991) Quinoproteins: enzymes containing the quinonoid cofactor pyrroloquinoline quinone, topaquinone or tryptophan-tryptophan quinone. Eur J Biochem 200, 271-284.
    • (1991) Eur J Biochem , vol.200 , pp. 271-284
    • Duine, J.A.1
  • 22
    • 0018792977 scopus 로고
    • Glucose dehydrogenase from Acinetobacter calcoaceticus: A 'quinoprotein'
    • Duine, J.A., Frank, J. van Zeeland, J.K. (1979) Glucose dehydrogenase from Acinetobacter calcoaceticus: a 'quinoprotein'. FEBS Lett 108, 443-446.
    • (1979) FEBS Lett , vol.108 , pp. 443-446
    • Duine, J.A.1    Frank, J.2    Van Zeeland, J.K.3
  • 23
    • 0034629338 scopus 로고    scopus 로고
    • Functions of amino acid residues in the active site of Escherichia coli pyrroloquinoline quinine-containing quinoprotein glucose dehydrogenase
    • Elias, M.D., Tanaka, M., Izu, H., Matsushita, K., Adachi, O. Yamada, M. (2000) Functions of amino acid residues in the active site of Escherichia coli pyrroloquinoline quinine-containing quinoprotein glucose dehydrogenase. J Biol Chem 275, 7321-7326.
    • (2000) J Biol Chem , vol.275 , pp. 7321-7326
    • Elias, M.D.1    Tanaka, M.2    Izu, H.3    Matsushita, K.4    Adachi, O.5    Yamada, M.6
  • 24
    • 0035930513 scopus 로고    scopus 로고
    • C-terminal periplasmic domain of Escherichia coli quinoprotein glucose dehydrogenase transfers electrons to ubiquinone
    • Elias, M.D., Tanaka, M., Sakai, M., Toyama, H., Matsushita, K., Adachi, O. Yamada, M. (2001) C-terminal periplasmic domain of Escherichia coli quinoprotein glucose dehydrogenase transfers electrons to ubiquinone. J Biol Chem 276, 48356 48361.
    • (2001) J Biol Chem , vol.276 , pp. 48356-48361
    • Elias, M.D.1    Tanaka, M.2    Sakai, M.3    Toyama, H.4    Matsushita, K.5    Adachi, O.6    Yamada, M.7
  • 25
    • 1642453630 scopus 로고    scopus 로고
    • Occurrence of a bound ubiquinone and its function in Escherichia coli membrane-bound quinoprotein glucose dehydrogenase
    • Elias, M.D., Nakamura, S., Migita, C.T., Miyoshi, H., Toyama, H., Matsushita, K., Adachi, O. Yamada, M. (2004) Occurrence of a bound ubiquinone and its function in Escherichia coli membrane-bound quinoprotein glucose dehydrogenase. J Biol Chem 279, 3078-3083.
    • (2004) J Biol Chem , vol.279 , pp. 3078-3083
    • Elias, M.D.1    Nakamura, S.2    Migita, C.T.3    Miyoshi, H.4    Toyama, H.5    Matsushita, K.6    Adachi, O.7    Yamada, M.8
  • 28
    • 0026478668 scopus 로고
    • The Entner-Doudoroff pathway in Escherichia coli is induced for oxidative glucose metabolism via pyrroloquinoline quinone-dependent glucose dehydrogenase
    • Fliege, R., Tong, S., Shibata, A., Nickerson, K.W. Conway, T. (1992) The Entner-Doudoroff pathway in Escherichia coli is induced for oxidative glucose metabolism via pyrroloquinoline quinone-dependent glucose dehydrogenase. Appl Environ Microbiol 58, 3826-3829.
    • (1992) Appl Environ Microbiol , vol.58 , pp. 3826-3829
    • Fliege, R.1    Tong, S.2    Shibata, A.3    Nickerson, K.W.4    Conway, T.5
  • 30
    • 0012991957 scopus 로고
    • Influence of phosphate solubilizing Bacilli on yield and phosphate uptake of wheat
    • Gaur, A.C. Ostwal, K.P. (1972) Influence of phosphate solubilizing Bacilli on yield and phosphate uptake of wheat. Indian J Exp Biol 10, 393-394.
    • (1972) Indian J Exp Biol , vol.10 , pp. 393-394
    • Gaur, A.C.1    Ostwal, K.P.2
  • 31
    • 0002067878 scopus 로고
    • Bacterial mineral phosphate solubilization: Historical perspectives and future prospects
    • Goldstein, A.H. (1986) Bacterial mineral phosphate solubilization: historical perspectives and future prospects. Am J Altern Agric 1, 57-65.
    • (1986) Am J Altern Agric , vol.1 , pp. 57-65
    • Goldstein, A.H.1
  • 33
    • 0028833273 scopus 로고
    • Recent progress in understanding the molecular genetics and biochemistry of calcium phosphate solubilization by Gram-negative bacteria
    • Goldstein, A.H. (1995) Recent progress in understanding the molecular genetics and biochemistry of calcium phosphate solubilization by Gram-negative bacteria. Biol Agric Horti 12, 185-193.
    • (1995) Biol Agric Horti , vol.12 , pp. 185-193
    • Goldstein, A.H.1
  • 35
    • 0023258354 scopus 로고
    • Molecular cloning and regulation a mineral phosphate-solubilizing gene from Erwinia herbicola
    • Goldstein, A.H. Liu, S.-T. (1987) Molecular cloning and regulation a mineral phosphate-solubilizing gene from Erwinia herbicola. Biotechnology 5, 72-74.
    • (1987) Biotechnology , vol.5 , pp. 72-74
    • Goldstein, A.H.1    Liu, S.-T.2
  • 37
    • 0032731321 scopus 로고    scopus 로고
    • Evidence for mutualism between a plant growing in a phosphate-limited desert environment and a mineral phosphate solubilizing (MPS) rhizobacterium
    • Goldstein, A.H., Braverman, K. Osorio, N. (1999) Evidence for mutualism between a plant growing in a phosphate-limited desert environment and a mineral phosphate solubilizing (MPS) rhizobacterium. FEMS Microbiol Ecol 30, 295-300.
    • (1999) FEMS Microbiol Ecol , vol.30 , pp. 295-300
    • Goldstein, A.H.1    Braverman, K.2    Osorio, N.3
  • 38
    • 0038650968 scopus 로고    scopus 로고
    • Research on the metabolic engineering of the direct oxidation pathway for extraction of phosphate from ore has generated preliminary evidence for PQQ biosynthesis in Escherichia coli as well as a possible role for the highly conserved region of quinoprotein dehydrogenases
    • Goldstein, A.H., Lester, T. Brown, J. (2003) Research on the metabolic engineering of the direct oxidation pathway for extraction of phosphate from ore has generated preliminary evidence for PQQ biosynthesis in Escherichia coli as well as a possible role for the highly conserved region of quinoprotein dehydrogenases. Biochim Biophys Acta 1647, 266-271.
    • (2003) Biochim Biophys Acta , vol.1647 , pp. 266-271
    • Goldstein, A.H.1    Lester, T.2    Brown, J.3
  • 39
    • 0023129319 scopus 로고
    • Cloning of the genes involved in synthesis of coenzyme pyrrolo-quinoline quinone from Acinetobacer calcoaceticus
    • Goosen, N., Vermaas, D.A.M. van de Putte, P. (1987) Cloning of the genes involved in synthesis of coenzyme pyrrolo-quinoline quinone from Acinetobacer calcoaceticus. J Bacteriol 169, 303-307.
    • (1987) J Bacteriol , vol.169 , pp. 303-307
    • Goosen, N.1    Vermaas, D.A.M.2    Van De Putte, P.3
  • 40
    • 0024525815 scopus 로고
    • Acinetobacter calcoaceticus genes involved in biosynthesis of the coenzyme pyrrolo-quinolone-quinone: Nucleotide sequence and expression in Escherichia coli K-12
    • Goosen, N., Horsman, H.P.A., Huinen, R.G. van de Putte, P. (1989) Acinetobacter calcoaceticus genes involved in biosynthesis of the coenzyme pyrrolo-quinolone-quinone: nucleotide sequence and expression in Escherichia coli K-12. J Bacteriol 171, 447-455.
    • (1989) J Bacteriol , vol.171 , pp. 447-455
    • Goosen, N.1    Horsman, H.P.A.2    Huinen, R.G.3    Van De Putte, P.4
  • 41
    • 0026580546 scopus 로고
    • A 24-amino-acid polypeptide is essential for the biosynthesis of the coenzyme pyrrolo-quinoline-quinone
    • Goosen, N., Huinen, R.G.M. van de Putte, P. (1992) A 24-amino-acid polypeptide is essential for the biosynthesis of the coenzyme pyrrolo-quinoline-quinone. J Bacteriol 174, 1426-1427.
    • (1992) J Bacteriol , vol.174 , pp. 1426-1427
    • Goosen, N.1    Huinen, R.G.M.2    Van De Putte, P.3
  • 43
    • 37549068171 scopus 로고    scopus 로고
    • Characterization of phosphate-solubilizing fluorescent pseudomonads from the rhizosphere of seabuckthorn growing in the cold deserts of Himalayas
    • Gulati, A., Rahi, P. Vyas, P. (2007) Characterization of phosphate-solubilizing fluorescent pseudomonads from the rhizosphere of seabuckthorn growing in the cold deserts of Himalayas. Curr Microbiol 56, 73-79.
    • (2007) Curr Microbiol , vol.56 , pp. 73-79
    • Gulati, A.1    Rahi, P.2    Vyas, P.3
  • 45
    • 0031768004 scopus 로고    scopus 로고
    • Effect of buffering on the phosphate-solubilizing ability of microorganisms
    • Gyaneshwar, P., Naresh Kumar, G. Parekh, L.J. (1998) Effect of buffering on the phosphate-solubilizing ability of microorganisms. World J Microbiol Biotechnol 14, 669-673.
    • (1998) World J Microbiol Biotechnol , vol.14 , pp. 669-673
    • Gyaneshwar, P.1    Naresh Kumar, G.2    Parekh, L.J.3
  • 46
    • 0032966136 scopus 로고    scopus 로고
    • Involvement of a phosphate starvation inducible glucose dehydrogenase in soil phosphate solubilization by Enterobacter asburiae
    • Gyaneshwar, P., Parekh, L.J., Archana, G., Poole, P.S., Collins, M.D., Hutson, R.A. Kumar, N.G. (1999) Involvement of a phosphate starvation inducible glucose dehydrogenase in soil phosphate solubilization by Enterobacter asburiae. FEMS Microbiol Lett 171, 223-229.
    • (1999) FEMS Microbiol Lett , vol.171 , pp. 223-229
    • Gyaneshwar, P.1    Parekh, L.J.2    Archana, G.3    Poole, P.S.4    Collins, M.D.5    Hutson, R.A.6    Kumar, N.G.7
  • 47
    • 21344477614 scopus 로고
    • Solubilization of inorganic phosphate by Rhizobium
    • Halder, A.K. Chakrabartty, P.K. (1993) Solubilization of inorganic phosphate by Rhizobium. Folia Microbiol 38, 325-330.
    • (1993) Folia Microbiol , vol.38 , pp. 325-330
    • Halder, A.K.1    Chakrabartty, P.K.2
  • 48
    • 0342633274 scopus 로고
    • Glucose dehydrogenase: Pseudomonas and Bacterium anitratum
    • Hauge, J.G. (1966) Glucose dehydrogenase: Pseudomonas and Bacterium anitratum. Methods Enzymol 9, 92-98.
    • (1966) Methods Enzymol , vol.9 , pp. 92-98
    • Hauge, J.G.1
  • 49
    • 0024287984 scopus 로고
    • Identification and isolation of glucose dehydrogenase genes of Bacillus megaterium M1286 and their expression in Escherichia coli
    • Heilmann, H.J., Magert, H.J. Gassen, H.G. (1988) Identification and isolation of glucose dehydrogenase genes of Bacillus megaterium M1286 and their expression in Escherichia coli. Eur J Biochem 174, 485-490.
    • (1988) Eur J Biochem , vol.174 , pp. 485-490
    • Heilmann, H.J.1    Magert, H.J.2    Gassen, H.G.3
  • 51
    • 0028974089 scopus 로고
    • Solubilization of inorganic calcium phosphates-solubilization mechanisms
    • Illmer, P. Schinner, F. (1995) Solubilization of inorganic calcium phosphates-solubilization mechanisms. Soil Biol Biochem 27, 265-270.
    • (1995) Soil Biol Biochem , vol.27 , pp. 265-270
    • Illmer, P.1    Schinner, F.2
  • 52
    • 1242341191 scopus 로고    scopus 로고
    • The metal ion in the active site of the membrane glucose dehydrogenase of Escherichia coli
    • James, P.L. Anthony, C. (2003) The metal ion in the active site of the membrane glucose dehydrogenase of Escherichia coli. Biochim Biophys Acta 1647, 200-205.
    • (2003) Biochim Biophys Acta , vol.1647 , pp. 200-205
    • James, P.L.1    Anthony, C.2
  • 53
    • 67649223263 scopus 로고    scopus 로고
    • Characterization of novel plant growth promoting endophytic bacterium achromobacter xylosoxidans from wheat plant
    • Jha, P. Kumar, A. (2009) Characterization of novel plant growth promoting endophytic bacterium achromobacter xylosoxidans from wheat plant. Microb Ecol 58, 179-188.
    • (2009) Microb Ecol , vol.58 , pp. 179-188
    • Jha, P.1    Kumar, A.2
  • 54
    • 77953553119 scopus 로고    scopus 로고
    • Buffering reduces phosphate solubilizing ability of selected strains of bacteria
    • Joseph, S. Jisha, M.S. (2009) Buffering reduces phosphate solubilizing ability of selected strains of bacteria. World J Agric Sci 5, 135-137.
    • (2009) World J Agric Sci , vol.5 , pp. 135-137
    • Joseph, S.1    Jisha, M.S.2
  • 55
    • 0000508103 scopus 로고
    • Phosphate dissolving microorganisms on seed and in the root zone of plants
    • Katznelson, H., Peterson, E.A. Rouatt, J.W. (1962) Phosphate dissolving microorganisms on seed and in the root zone of plants. Can J Bot 40, 1181-1186.
    • (1962) Can J Bot , vol.40 , pp. 1181-1186
    • Katznelson, H.1    Peterson, E.A.2    Rouatt, J.W.3
  • 56
    • 0004604962 scopus 로고
    • The effect of organic root product on the availability of phosphorous to plants
    • In. ed. Harley, J.L. Scott-Russell, R.
    • Kepert, D.G., Robson, A.D. Posner, A.M. (1979) The effect of organic root product on the availability of phosphorous to plants. In The Soil Root Interface ed. Harley, J.L. Scott-Russell, R. pp. 115 124.
    • (1979) The Soil Root Interface , pp. 115-124
    • Kepert, D.G.1    Robson, A.D.2    Posner, A.M.3
  • 57
    • 0345276491 scopus 로고    scopus 로고
    • Pyrroloquinoline-quinone synthesized in Escherichia coli by pyrroloquinoline-quinone synthase of Deinococcus radiodurans plays a role beyond mineral phosphate solubilization
    • Khairnar, N.P., Mishra, H.S. Apte, S.K. (2003) Pyrroloquinoline-quinone synthesized in Escherichia coli by pyrroloquinoline-quinone synthase of Deinococcus radiodurans plays a role beyond mineral phosphate solubilization. Biochem Biophys Res Commun, 312, 303-308.
    • (2003) Biochem Biophys Res Commun , vol.312 , pp. 303-308
    • Khairnar, N.P.1    Mishra, H.S.2    Apte, S.K.3
  • 58
    • 0030616411 scopus 로고    scopus 로고
    • Solubilization of hydroxyapatite by Enterobacter agglomerans and cloned Escherichia coli in culture medium
    • Kim, K.Y., McDonald, G.A. Jordan, D. (1997b) Solubilization of hydroxyapatite by Enterobacter agglomerans and cloned Escherichia coli in culture medium. Biol Fertil Soils 24, 347-352.
    • (1997) Biol Fertil Soils , vol.24 , pp. 347-352
    • Kim, K.Y.1    McDonald, G.A.2    Jordan, D.3
  • 59
    • 0032008227 scopus 로고    scopus 로고
    • Expression of genes from Rahnella aquatilis that are necessary for mineral phosphate solubilization in Escherichia coli
    • Kim, K.Y., Jordan, D. Krishnan, H.B. (1998) Expression of genes from Rahnella aquatilis that are necessary for mineral phosphate solubilization in Escherichia coli. FEMS Microbiol Lett 159, 121-127.
    • (1998) FEMS Microbiol Lett , vol.159 , pp. 121-127
    • Kim, K.Y.1    Jordan, D.2    Krishnan, H.B.3
  • 60
    • 0344464830 scopus 로고    scopus 로고
    • Cloning and expression of pyrroloquinoline quinine (PQQ) genes from a phosphate-solubilizing bacterium Enterobacter intermedium
    • Kim, C.H., Han, S.H., Kim, K.Y., Cho, B.H., Kim, Y.H., Koo, B.S. Kim, Y.C. (2003) Cloning and expression of pyrroloquinoline quinine (PQQ) genes from a phosphate-solubilizing bacterium Enterobacter intermedium. Curr Microbiol 47, 457-461.
    • (2003) Curr Microbiol , vol.47 , pp. 457-461
    • Kim, C.H.1    Han, S.H.2    Kim, K.Y.3    Cho, B.H.4    Kim, Y.H.5    Koo, B.S.6    Kim, Y.C.7
  • 61
    • 0035910161 scopus 로고    scopus 로고
    • Cloning of a Serratia marcescens DNA fragment that induces quinoprotein glucose dehydrogenase-mediated gluconic acid production in Escherichia coli in the presence of a stationary phase Serratia marcescens
    • Krishnaraj, P.U. Goldstein, A.H. (2001) Cloning of a Serratia marcescens DNA fragment that induces quinoprotein glucose dehydrogenase-mediated gluconic acid production in Escherichia coli in the presence of a stationary phase Serratia marcescens. FEMS Microbiol Lett 205, 215-220.
    • (2001) FEMS Microbiol Lett , vol.205 , pp. 215-220
    • Krishnaraj, P.U.1    Goldstein, A.H.2
  • 62
    • 70349467396 scopus 로고
    • Microbially mediated increases in plant available phosphorous
    • Kucey, R.M.N., Janzen, H.H. Legget, M.E. (1989) Microbially mediated increases in plant available phosphorous. Adv Agron 42, 198-228.
    • (1989) Adv Agron , vol.42 , pp. 198-228
    • Kucey, R.M.N.1    Janzen, H.H.2    Legget, M.E.3
  • 63
    • 0032945621 scopus 로고    scopus 로고
    • Solubilization of inorganic phosphates and growth emergence of wheat as affected by Azotobacter chroococcum mutants
    • Kumar, V. Narula, N. (1999) Solubilization of inorganic phosphates and growth emergence of wheat as affected by Azotobacter chroococcum mutants. Biol Fertil Soils 28, 301-305.
    • (1999) Biol Fertil Soils , vol.28 , pp. 301-305
    • Kumar, V.1    Narula, N.2
  • 64
    • 0021119496 scopus 로고
    • Alternative pathways of carbohydrate utilization in Pseudomonas
    • Lessie, T.G. Phibbs, P.B. (1984) Alternative pathways of carbohydrate utilization in Pseudomonas. Ann Rev Microbiol 38, 359-387.
    • (1984) Ann Rev Microbiol , vol.38 , pp. 359-387
    • Lessie, T.G.1    Phibbs, P.B.2
  • 65
    • 58549102318 scopus 로고    scopus 로고
    • Phosphate solubilizing Gluconacetobacter sp. Burkholderia sp. and their potential interactions with cowpea (Vigna unguiculata L. (Walp)
    • Linu, M.S., Stephen, J. Jisha, M.S. (2009) Phosphate solubilizing Gluconacetobacter sp. Burkholderia sp. and their potential interactions with cowpea (Vigna unguiculata L. (Walp). Int J Agric Res 4, 79-87.
    • (2009) Int J Agric Res , vol.4 , pp. 79-87
    • Linu, M.S.1    Stephen, J.2    Jisha, M.S.3
  • 66
    • 0026669828 scopus 로고
    • Cloning of an Erwinia herbicola gene necessary for the gluconic acid production and enhanced mineral phosphate solubilization in Escherichia coli HB101: Nucleotide sequence and probable involvement in biosynthesis of the coenzyme pyrrolo quinoline quinone
    • Liu, S.-T., Lee, L.-Y., Tai, C.-Y., Hung, C.-H., Chang, Y.-S., Wolfram, J.H., Rogers, R. Goldstein, A.H. (1992) Cloning of an Erwinia herbicola gene necessary for the gluconic acid production and enhanced mineral phosphate solubilization in Escherichia coli HB101: nucleotide sequence and probable involvement in biosynthesis of the coenzyme pyrrolo quinoline quinone. J Bacteriol 174, 5814-5819.
    • (1992) J Bacteriol , vol.174 , pp. 5814-5819
    • Liu, S.-T.1    Lee, L.-Y.2    Tai, C.-Y.3    Hung, C.-H.4    Chang, Y.-S.5    Wolfram, J.H.6    Rogers, R.7    Goldstein, A.H.8
  • 67
    • 4143131171 scopus 로고    scopus 로고
    • Occurrence of Gluconacetobacter diazotrophicus in tropical and subtropical plants of Western Ghats, India
    • Madhaiyan, M., Saravanan, V.S., Jovi, D.B., Lee, H., Thenmozhi, R., Hari, K. Sa, T. (2004) Occurrence of Gluconacetobacter diazotrophicus in tropical and subtropical plants of Western Ghats, India. Microbiol Res 159, 233-243.
    • (2004) Microbiol Res , vol.159 , pp. 233-243
    • Madhaiyan, M.1    Saravanan, V.S.2    Jovi, D.B.3    Lee, H.4    Thenmozhi, R.5    Hari, K.6    Sa, T.7
  • 68
    • 0009934156 scopus 로고    scopus 로고
    • Mineral phosphate solubilizing activity of Acetobacter diazotrophicus: A bacterium associated with sugarcane
    • Maheshkumar, K.S., Krishnaraj, P.U. Alagawadi, A.R. (1999) Mineral phosphate solubilizing activity of Acetobacter diazotrophicus: a bacterium associated with sugarcane. Curr Sci 76, 874-875.
    • (1999) Curr Sci , vol.76 , pp. 874-875
    • Maheshkumar, K.S.1    Krishnaraj, P.U.2    Alagawadi, A.R.3
  • 69
    • 0040356017 scopus 로고
    • Membrane bound D-glucose dehydrogenase from Pseudomonas sp: Solubilization, purification, and characterization
    • Matsushita, K., Ohno, Y., Shinagawa, E., Adachi, O. Ameyama, M. (1980) Membrane bound D-glucose dehydrogenase from Pseudomonas sp: solubilization, purification, and characterization. Agric Biol Chem 44, 1505-1512.
    • (1980) Agric Biol Chem , vol.44 , pp. 1505-1512
    • Matsushita, K.1    Ohno, Y.2    Shinagawa, E.3    Adachi, O.4    Ameyama, M.5
  • 70
    • 0018399611 scopus 로고
    • Membrane-bound d-gluconate dehydrogenase from Pseudomonas aeruginosa
    • Matsushita, K., Shinagawa, E., Adachi, O. Ameyama, M. (1979) Membrane-bound d-gluconate dehydrogenase from Pseudomonas aeruginosa. J Biochem 85, 1173-1181.
    • (1979) J Biochem , vol.85 , pp. 1173-1181
    • Matsushita, K.1    Shinagawa, E.2    Adachi, O.3    Ameyama, M.4
  • 71
    • 0020435678 scopus 로고
    • D-Glucose dehydrogenase from Pseudomonas fluorescens, membrane-bound
    • Matsushita, K., Shinagawa, E. Ameyama, M. (1982) d-Glucose dehydrogenase from Pseudomonas fluorescens, membrane-bound. Methods Enzymol 89, 187-193.
    • (1982) Methods Enzymol , vol.89 , pp. 187-193
    • Matsushita, K.1    Shinagawa, E.2    Ameyama, M.3
  • 72
    • 0022544376 scopus 로고
    • Immunological evidence for two types of PQQ dependent D-glucose dehydrogenase in bacterial membranes and the location of the enzyme in Escherichia coli
    • Matsushita, K., Shinagawa, E., Inoue, T., Adachi, O. Ameyama, M. (1986) Immunological evidence for two types of PQQ dependent D-glucose dehydrogenase in bacterial membranes and the location of the enzyme in Escherichia coli. FEMS Microbiol Lett 37, 141-144.
    • (1986) FEMS Microbiol Lett , vol.37 , pp. 141-144
    • Matsushita, K.1    Shinagawa, E.2    Inoue, T.3    Adachi, O.4    Ameyama, M.5
  • 74
    • 0026549104 scopus 로고
    • Nucleotide sequence and structure of the Klebsiella pneumoniae pqq operon
    • Meulenberg, J.J.M., Sellink, E., Riegman, N.H. Postma, P.W. (1992) Nucleotide sequence and structure of the Klebsiella pneumoniae pqq operon. Mol Gen Genet 232, 284-292.
    • (1992) Mol Gen Genet , vol.232 , pp. 284-292
    • Meulenberg, J.J.M.1    Sellink, E.2    Riegman, N.H.3    Postma, P.W.4
  • 75
    • 0015577755 scopus 로고
    • The regulation of glucose and methyl glucose uptake in Pseudomonas aeruginosa
    • Midgley, M. Dawes, E.A. (1973) The regulation of glucose and methyl glucose uptake in Pseudomonas aeruginosa. Biochem J 132, 141-154.
    • (1973) Biochem J , vol.132 , pp. 141-154
    • Midgley, M.1    Dawes, E.A.2
  • 76
    • 49349138918 scopus 로고
    • Characterization of rhizosphere products especially 2-ketogluconic acid
    • Moghimi, A., Tate, M.E. Oades, J.M. (1978) Characterization of rhizosphere products especially 2-ketogluconic acid. Soil Biol Biochem 10, 283-287.
    • (1978) Soil Biol Biochem , vol.10 , pp. 283-287
    • Moghimi, A.1    Tate, M.E.2    Oades, J.M.3
  • 77
    • 18144403554 scopus 로고    scopus 로고
    • Improving enzyme properties: When are closer mutations better?
    • Morley, K.L. Kazlauskas, R.J. (2005) Improving enzyme properties: when are closer mutations better? Trends Biotechnol 23, 231-237.
    • (2005) Trends Biotechnol , vol.23 , pp. 231-237
    • Morley, K.L.1    Kazlauskas, R.J.2
  • 78
    • 52049118563 scopus 로고    scopus 로고
    • Amino acid residues interacting with both the bound quinone and coenzyme, pyrroloquinoline quinone, in Escherichia coli membrane-bound glucose dehydrogenase
    • Mustafa, G., Ishikawam, Y., Kobayashi, K., Migita, C.T., Elias, M.D., Nakamura, S., Tagawa, S. Yamada, M. (2008) Amino acid residues interacting with both the bound quinone and coenzyme, pyrroloquinoline quinone, in Escherichia coli membrane-bound glucose dehydrogenase. J Biol Chem 283 (32 22215 22221.
    • (2008) J Biol Chem , vol.283 , Issue.32 , pp. 22215-22221
    • Mustafa, G.1    Ishikawam, Y.2    Kobayashi, K.3    Migita, C.T.4    Elias, M.D.5    Nakamura, S.6    Tagawa, S.7    Yamada, M.8
  • 79
    • 0020546201 scopus 로고
    • Glucose metabolism by K-limited Klebsiella aerogenes, evidence for the involvement of a quinoprotein glucose dehydrogenase
    • Neijssel, O.M., Tempest, D.W., Postma, P.W., Duine, J.A. Frank, J. (1983) Glucose metabolism by K-limited Klebsiella aerogenes, evidence for the involvement of a quinoprotein glucose dehydrogenase. FEMS Microbiol Lett 20, 35-39.
    • (1983) FEMS Microbiol Lett , vol.20 , pp. 35-39
    • Neijssel, O.M.1    Tempest, D.W.2    Postma, P.W.3    Duine, J.A.4    Frank, J.5
  • 80
    • 34547842057 scopus 로고    scopus 로고
    • Isolation and characterization of mineral phosphate-solubilizing bacteria naturally colonizing a limonitic crust in the south-eastern Venezuelan region
    • Perez, E., Sulbaran, M., Ball, M.M. Yarzabal, L.A. (2007) Isolation and characterization of mineral phosphate-solubilizing bacteria naturally colonizing a limonitic crust in the south-eastern Venezuelan region. Soil Biol Biochem 39, 2905-2914.
    • (2007) Soil Biol Biochem , vol.39 , pp. 2905-2914
    • Perez, E.1    Sulbaran, M.2    Ball, M.M.3    Yarzabal, L.A.4
  • 81
    • 77950341500 scopus 로고    scopus 로고
    • Plant growth promoting rhizobacteria
    • In. ed. Gnanamanickam, S.S.
    • Podile, A.R. Kishore, G.K. (2006) Plant growth promoting rhizobacteria. In Plant Associated Bacteria ed. Gnanamanickam, S.S. pp. 195 230.
    • (2006) Plant Associated Bacteria , pp. 195-230
    • Podile, A.R.1    Kishore, G.K.2
  • 82
    • 42149106127 scopus 로고    scopus 로고
    • The pyrroloquinoline quinone biosynthesis pathway revisited: A structural approach
    • Puehringer, S., Metlitzky, M. Schwarzenbacher, R. (2008) The pyrroloquinoline quinone biosynthesis pathway revisited: a structural approach. BMC Biochem 8 : 9.
    • (2008) BMC Biochem , vol.89
    • Puehringer, S.1    Metlitzky, M.2    Schwarzenbacher, R.3
  • 83
    • 0033775638 scopus 로고    scopus 로고
    • Phosphorous acquisition; plant in the driver's seat!
    • Raghothama, K.G. (2000) Phosphorous acquisition; plant in the driver's seat! Trends Plant Sci 5, 412-413.
    • (2000) Trends Plant Sci , vol.5 , pp. 412-413
    • Raghothama, K.G.1
  • 84
    • 0343593686 scopus 로고    scopus 로고
    • Phosphate solubilizing bacteria and their role in plant growth promotion
    • Rodriguez, H. Fraga, R. (1999) Phosphate solubilizing bacteria and their role in plant growth promotion. Biotechnol Adv 17, 319-339.
    • (1999) Biotechnol Adv , vol.17 , pp. 319-339
    • Rodriguez, H.1    Fraga, R.2
  • 85
    • 0034736408 scopus 로고    scopus 로고
    • Expression of a mineral phosphate-solubilizing gene from Erwinia herbicola in two rhizobacterial strains
    • Rodriguez, H., Gonzalez, T. Selman, G. (2000) Expression of a mineral phosphate-solubilizing gene from Erwinia herbicola in two rhizobacterial strains. J Biotechnol 84, 155-161.
    • (2000) J Biotechnol , vol.84 , pp. 155-161
    • Rodriguez, H.1    Gonzalez, T.2    Selman, G.3
  • 86
    • 77950661324 scopus 로고    scopus 로고
    • Transgenic expression of glucose dehydrogenase in Azotobacter vinelandii enhances mineral phosphate solubilization and growth of sorghum seedlings
    • Sashidhar, B. Podile, A.R. (2009) Transgenic expression of glucose dehydrogenase in Azotobacter vinelandii enhances mineral phosphate solubilization and growth of sorghum seedlings. Microbial Biotechnol 2, 521-529.
    • (2009) Microbial Biotechnol , vol.2 , pp. 521-529
    • Sashidhar, B.1    Podile, A.R.2
  • 87
    • 77649319210 scopus 로고    scopus 로고
    • Highly conserved Asp-204 and Gly-776 are important for activity of the quinoprotein glucose dehydrogenase of Escherichia coli and for mineral phosphate solubilization
    • in press.
    • Sashidhar, B., Kishore, I.K., Lalitha, G., Anil, K., Gopinath, K. Podile, A.R. (2010) Highly conserved Asp-204 and Gly-776 are important for activity of the quinoprotein glucose dehydrogenase of Escherichia coli and for mineral phosphate solubilization. J Mol Microbiol Biotechnol, in press.
    • (2010) J Mol Microbiol Biotechnol
    • Sashidhar, B.1    Kishore, I.K.2    Lalitha, G.3    Anil, K.4    Gopinath, K.5    Podile, A.R.6
  • 88
    • 0021826930 scopus 로고
    • Energy transduction by electron transfer via pyrrolo-quinoline quinone-dependent glucose dehydrogenase in Escherichia coli, Pseudomonas aeuriginosa, and Acinetobacter calcoaceticus (var. lwoffi)
    • van Schie, B.J., Hellingwerf, K.J., van Dijken, J.P., Elferink, M.G.L., van Dijl, J.M., Kuenen, J.G. Konings, W.N. (1985) Energy transduction by electron transfer via pyrrolo-quinoline quinone-dependent glucose dehydrogenase in Escherichia coli, Pseudomonas aeuriginosa, and Acinetobacter calcoaceticus (var. lwoffi). J Bacteriol 163, 493-499.
    • (1985) J Bacteriol , vol.163 , pp. 493-499
    • Van Schie, B.J.1    Hellingwerf, K.J.2    Van Dijken, J.P.3    Elferink, M.G.L.4    Van Dijl, J.M.5    Kuenen, J.G.6    Konings, W.N.7
  • 89
    • 0021171062 scopus 로고
    • Non-coordinated synthesis of glucose dehydrogenase and its prosthetic group PQQ in Acinetobacter and Pseudomonas species
    • Van Schie, B.J., van Dijken, J.P. Kuenen, J.G. (1984) Non-coordinated synthesis of glucose dehydrogenase and its prosthetic group PQQ in Acinetobacter and Pseudomonas species. FEMS Microbiol Lett 24, 133-138.
    • (1984) FEMS Microbiol Lett , vol.24 , pp. 133-138
    • Van Schie, B.J.1    Van Dijken, J.P.2    Kuenen, J.G.3
  • 91
    • 0013050778 scopus 로고
    • D-gluconate dehydrogenase, 2-keto-D-gluconate yielding, from Gluconobacter dioxyacetonicus: Purification and characterization
    • Shinagawa, E., Matsushita, K., Adachi, O. Ameyama, M. (1984) D-gluconate dehydrogenase, 2-keto-D-gluconate yielding, from Gluconobacter dioxyacetonicus: purification and characterization. Agric Biol Chem 48, 1517-1522.
    • (1984) Agric Biol Chem , vol.48 , pp. 1517-1522
    • Shinagawa, E.1    Matsushita, K.2    Adachi, O.3    Ameyama, M.4
  • 92
    • 0032892021 scopus 로고    scopus 로고
    • Inoculation with phosphate-solubilizing microorganisms and a vesicular-arbuscular mycorrhizal fungus improves dry matter yield nutrient uptake by wheat grown in a sandy soil
    • Singh, S. Kapoor, K.K. (1999) Inoculation with phosphate-solubilizing microorganisms and a vesicular-arbuscular mycorrhizal fungus improves dry matter yield nutrient uptake by wheat grown in a sandy soil. Biol Fert Soils 28, 139-144.
    • (1999) Biol Fert Soils , vol.28 , pp. 139-144
    • Singh, S.1    Kapoor, K.K.2
  • 93
    • 0030733901 scopus 로고    scopus 로고
    • Improved substrate specificity and dynamic range for glucose measurement of Escherichia coli PQQ glucose dehydrogenase by site directed mutagenesis
    • Sode, K. Kojima, K. (1997) Improved substrate specificity and dynamic range for glucose measurement of Escherichia coli PQQ glucose dehydrogenase by site directed mutagenesis. Biotechnol Lett 19, 1073-1077.
    • (1997) Biotechnol Lett , vol.19 , pp. 1073-1077
    • Sode, K.1    Kojima, K.2
  • 94
    • 0028286184 scopus 로고
    • Glu 742 substitution to Lys enhances the EDTA tolerance of Escherichia coli PQQ glucose dehydrogenase
    • Sode, K. Sano, H. (1994) Glu 742 substitution to Lys enhances the EDTA tolerance of Escherichia coli PQQ glucose dehydrogenase. Biotechnol Lett 16, 455-460.
    • (1994) Biotechnol Lett , vol.16 , pp. 455-460
    • Sode, K.1    Sano, H.2
  • 95
    • 0029068329 scopus 로고
    • Elucidation of the region responsible for EDTA tolerance in PQQ glucose dehydrogenase by constructing Escherichia coli and Acinetobacter calcoaceticus chimeric enzymes
    • Sode, K., Yoshida, H., Matsumura, K., Kikuchi, T., Watanabe, M., Yasutake, N., Ito, S. Sano, H. (1995a) Elucidation of the region responsible for EDTA tolerance in PQQ glucose dehydrogenase by constructing Escherichia coli and Acinetobacter calcoaceticus chimeric enzymes. Biochem Biophys Res Commun 211, 268-273.
    • (1995) Biochem Biophys Res Commun , vol.211 , pp. 268-273
    • Sode, K.1    Yoshida, H.2    Matsumura, K.3    Kikuchi, T.4    Watanabe, M.5    Yasutake, N.6    Ito, S.7    Sano, H.8
  • 99
    • 34547544268 scopus 로고    scopus 로고
    • Properties of chimeric glucose dehydrogenase improved by site directed mutagenesis
    • Tripura, C.B. Podile, A.R. (2007) Properties of chimeric glucose dehydrogenase improved by site directed mutagenesis. J Biotechnol 131, 197-204.
    • (2007) J Biotechnol , vol.131 , pp. 197-204
    • Tripura, C.B.1    Podile, A.R.2
  • 100
  • 101
    • 33846269685 scopus 로고    scopus 로고
    • Ethyl methanesulfonate mutagenesis enhanced mineral phosphate solubilization by groundnut-associated Serratia marcescens GPS 5
    • Tripura, C.B., Sashidhar, B. Podile, A.R. (2007a) Ethyl methanesulfonate mutagenesis enhanced mineral phosphate solubilization by groundnut-associated Serratia marcescens GPS 5. Current Microbiology 54, 79-84.
    • (2007) Current Microbiology , vol.54 , pp. 79-84
    • Tripura, C.B.1    Sashidhar, B.2    Podile, A.R.3
  • 102
    • 54849430064 scopus 로고    scopus 로고
    • Glucose dehydrogenase of a rhizobacterial strain of Enterobacter asburiae involved in mineral phosphate solubilization shares properties and sequence homology with other members of enterobacteriaceae
    • Tripura, C.B., Sudhakar Reddy, P., Reddy, M.K., Sashidhar, B. Podile, A.R. (2007b) Glucose dehydrogenase of a rhizobacterial strain of Enterobacter asburiae involved in mineral phosphate solubilization shares properties and sequence homology with other members of enterobacteriaceae. Indian J Microbiol 47, 126-131.
    • (2007) Indian J Microbiol , vol.47 , pp. 126-131
    • Tripura, C.B.1    Sudhakar Reddy, P.2    Reddy, M.K.3    Sashidhar, B.4    Podile, A.R.5
  • 103
    • 0027311303 scopus 로고
    • Topological analysis of quinoprotein glucose dehydrogenase in Escherichia coli and its ubiquinone binding site
    • Yamada, M., Sumi, K., Matsushita, K., Adachi, O. Yamada, Y. (1993) Topological analysis of quinoprotein glucose dehydrogenase in Escherichia coli and its ubiquinone binding site. J Biol Chem 268, 12812 12817.
    • (1993) J Biol Chem , vol.268 , pp. 12812-12817
    • Yamada, M.1    Sumi, K.2    Matsushita, K.3    Adachi, O.4    Yamada, Y.5
  • 104
    • 0032555651 scopus 로고    scopus 로고
    • Mutant isolation of the Escherichia coli quinoprotein glucose dehydrogenase and anlaysis of crucial residues Asp-730 and His-775 for its Function
    • Yamada, M., Inbe, H., Tanaka, M., Sumi, K., Matsushita, K. Adachi, O. (1998) Mutant isolation of the Escherichia coli quinoprotein glucose dehydrogenase and anlaysis of crucial residues Asp-730 and His-775 for its Function. J Biol Chem 273, 22021 22027.
    • (1998) J Biol Chem , vol.273 , pp. 22021-22027
    • Yamada, M.1    Inbe, H.2    Tanaka, M.3    Sumi, K.4    Matsushita, K.5    Adachi, O.6
  • 105
    • 0038312036 scopus 로고    scopus 로고
    • Escherichia coli PQQ-containing quinoprotein glucose dehydrogenase: Its structure comparison with other quinoprioteins
    • Yamada, M., Elias, M.D., Matsushita, K., Migita, C.T. Adachi, O. (2003) Escherichia coli PQQ-containing quinoprotein glucose dehydrogenase: its structure comparison with other quinoprioteins. Biochim Biophys Acta 1647, 185-192.
    • (2003) Biochim Biophys Acta , vol.1647 , pp. 185-192
    • Yamada, M.1    Elias, M.D.2    Matsushita, K.3    Migita, C.T.4    Adachi, O.5
  • 106
    • 0033007416 scopus 로고    scopus 로고
    • Engineering a chimeric pyrroloquinoline quinone glucose dehydrogenase: Improvement of EDTA tolerance, thermal stability and substrate specificity
    • Yoshida, H., Kojima, K., Witarto, A.B. Sode, K. (1999) Engineering a chimeric pyrroloquinoline quinone glucose dehydrogenase: improvement of EDTA tolerance, thermal stability and substrate specificity. Protein Eng 12, 63-70.
    • (1999) Protein Eng , vol.12 , pp. 63-70
    • Yoshida, H.1    Kojima, K.2    Witarto, A.B.3    Sode, K.4
  • 107
    • 0030668086 scopus 로고    scopus 로고
    • Cloning and expression of a gene cluster encoding three subunits of membrane-bound gluconate dehydrogenase from Erwinia cypripedii ATCC
    • 29267 in Escherichia coli.
    • Yum, D.-Y., Lee, Y.-P. Pan, J.G. (1997) Cloning and expression of a gene cluster encoding three subunits of membrane-bound gluconate dehydrogenase from Erwinia cypripedii ATCC 29267 in Escherichia coli. J Bacteriol 179, 6566-6572.
    • (1997) J Bacteriol , vol.179 , pp. 6566-6572
    • Yum, D.-Y.1    Lee, Y.-P.2    Pan, J.G.3


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