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Volumn 109, Issue 5, 2010, Pages 423-432

Bacterial phosphate metabolism and its application to phosphorus recovery and industrial bioprocesses

Author keywords

Bacterial phosphate metabolism; EBPR process; Heatphos; P recovery and recycling; Polyphosphate

Indexed keywords

BACTERIAL PHOSPHATE METABOLISM; EBPR PROCESS; HEATPHOS; POLYPHOSPHATE; POLYPHOSPHATES;

EID: 77949903823     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2009.10.018     Document Type: Review
Times cited : (107)

References (66)
  • 1
    • 0033605537 scopus 로고    scopus 로고
    • A potential phosphate crisis
    • Abelson P.H. A potential phosphate crisis. Science 283 (1999) 2015
    • (1999) Science , vol.283 , pp. 2015
    • Abelson, P.H.1
  • 2
    • 67349203641 scopus 로고    scopus 로고
    • The story of phosphorus: global food security and food for thought
    • Cordell D., Drangert J., and White S. The story of phosphorus: global food security and food for thought. Global Environ. Change 19 (2009) 292-305
    • (2009) Global Environ. Change , vol.19 , pp. 292-305
    • Cordell, D.1    Drangert, J.2    White, S.3
  • 3
    • 0015237202 scopus 로고
    • Phosphate replacements: problems with the washday miracle
    • Hammond A.L. Phosphate replacements: problems with the washday miracle. Science 172 (1971) 361-363
    • (1971) Science , vol.172 , pp. 361-363
    • Hammond, A.L.1
  • 4
    • 0027331252 scopus 로고
    • : Genetic improvement of Escherichia coli for enhanced biological removal of phosphate from wastewater
    • Kato J., Yamada K., Muramatsu A., Hardoyo, and Ohtake H. : Genetic improvement of Escherichia coli for enhanced biological removal of phosphate from wastewater. Appl. Environ. Microbiol. 59 (1993) 3744-3749
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 3744-3749
    • Kato, J.1    Yamada, K.2    Muramatsu, A.3    Hardoyo4    Ohtake, H.5
  • 5
    • 0022338735 scopus 로고
    • Uptake and release of phosphate by a pure culture of Acinetobacter carcoaceticus
    • Ohtake H., Takahashi K., Tsuzuki Y., and Toda K. Uptake and release of phosphate by a pure culture of Acinetobacter carcoaceticus. Water Res. 19 (1985) 1587-1594
    • (1985) Water Res. , vol.19 , pp. 1587-1594
    • Ohtake, H.1    Takahashi, K.2    Tsuzuki, Y.3    Toda, K.4
  • 7
    • 0020981178 scopus 로고
    • Polyphosphate metabolism in micro-organisms
    • Kulaev I.S., and Vagabov V.M. Polyphosphate metabolism in micro-organisms. Adv. Microbiol. Physiol. 24 (1983) 83-171
    • (1983) Adv. Microbiol. Physiol. , vol.24 , pp. 83-171
    • Kulaev, I.S.1    Vagabov, V.M.2
  • 8
    • 0013979409 scopus 로고
    • Inorganic polyphosphates in biology: structure, metabolism, and function
    • Harold F.M. Inorganic polyphosphates in biology: structure, metabolism, and function. Bacteriol. Rev. 30 (1966) 772-794
    • (1966) Bacteriol. Rev. , vol.30 , pp. 772-794
    • Harold, F.M.1
  • 9
    • 0028967488 scopus 로고
    • Inorganic polyphosphate: toward making a forgotten polymer unforgettable
    • Kornberg A. Inorganic polyphosphate: toward making a forgotten polymer unforgettable. J. Bacteriol. 177 (1995) 491-496
    • (1995) J. Bacteriol. , vol.177 , pp. 491-496
    • Kornberg, A.1
  • 10
    • 0028703434 scopus 로고
    • Molecular genetics of carbon-phosphorus bond cleavage in bacteria
    • Wanner B.L. Molecular genetics of carbon-phosphorus bond cleavage in bacteria. Biodegradation 5 (1994) 175-184
    • (1994) Biodegradation , vol.5 , pp. 175-184
    • Wanner, B.L.1
  • 11
    • 0025217032 scopus 로고
    • Molecular biology of carbon-phosphorus bond cleavage. Cloning and sequencing of the phn (psiD) genes involved in alkylphosphonate uptake and C-P lyase activity in Escherichia coli
    • Chen C.M., Ye Q.Z., Zhu Z.M., Wanner B.L., and Walsh C.T. Molecular biology of carbon-phosphorus bond cleavage. Cloning and sequencing of the phn (psiD) genes involved in alkylphosphonate uptake and C-P lyase activity in Escherichia coli. B. J. Biol. Chem. 265 (1990) 4461-4471
    • (1990) B. J. Biol. Chem. , vol.265 , pp. 4461-4471
    • Chen, C.M.1    Ye, Q.Z.2    Zhu, Z.M.3    Wanner, B.L.4    Walsh, C.T.5
  • 12
    • 0023101749 scopus 로고
    • Bacterial carbon-phosphorus lyase: products, rates, and regulation of phosphonic and phosphinic acid metabolism
    • Wackett L.P., Shames S.L., Venditti C.P., and Walsh C.T. Bacterial carbon-phosphorus lyase: products, rates, and regulation of phosphonic and phosphinic acid metabolism. J. Bacteriol. 169 (1987) 710-717
    • (1987) J. Bacteriol. , vol.169 , pp. 710-717
    • Wackett, L.P.1    Shames, S.L.2    Venditti, C.P.3    Walsh, C.T.4
  • 15
    • 0026635712 scopus 로고
    • Phosphate taxis in Pseudomonas aeruginosa
    • Kato J., Ito A., Nikata T., and Ohtake H. Phosphate taxis in Pseudomonas aeruginosa. J. Bacteriol. 174 (1992) 5149-5151
    • (1992) J. Bacteriol. , vol.174 , pp. 5149-5151
    • Kato, J.1    Ito, A.2    Nikata, T.3    Ohtake, H.4
  • 16
    • 48449083218 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa as a model microorganism for investigation of chemotactic behaviors in ecosystem
    • Kato J., Kim H., Takiguchi N., Kuroda A., and Ohtake H. Pseudomonas aeruginosa as a model microorganism for investigation of chemotactic behaviors in ecosystem. J. Biosc. Bioeng. 106 (2008) 1-7
    • (2008) J. Biosc. Bioeng. , vol.106 , pp. 1-7
    • Kato, J.1    Kim, H.2    Takiguchi, N.3    Kuroda, A.4    Ohtake, H.5
  • 17
    • 0025315968 scopus 로고
    • Polyphosphate kinase from Escherichia coli. Purification and demonstration of a phosphoenzyme intermediate
    • Ahn K., and Kornberg A. Polyphosphate kinase from Escherichia coli. Purification and demonstration of a phosphoenzyme intermediate. J. Biol. Chem. 265 (1990) 11734-11739
    • (1990) J. Biol. Chem. , vol.265 , pp. 11734-11739
    • Ahn, K.1    Kornberg, A.2
  • 18
    • 0034635423 scopus 로고    scopus 로고
    • The multiple activities of polyphosphate kinase of Escherichia coli and their subunit structure determined by radiation target analysis
    • Tzeng C.M., and Kornberg A. The multiple activities of polyphosphate kinase of Escherichia coli and their subunit structure determined by radiation target analysis. J. Biol. Chem. 275 (2000) 3977-3983
    • (2000) J. Biol. Chem. , vol.275 , pp. 3977-3983
    • Tzeng, C.M.1    Kornberg, A.2
  • 19
    • 23744488104 scopus 로고    scopus 로고
    • Crystal structure of a polyphosphate kinase and its implications for polyphosphate synthesis
    • Zhu Y., Huang W., Lee S.S., and Xu W. Crystal structure of a polyphosphate kinase and its implications for polyphosphate synthesis. EMBO Rep. 6 (2005) 681-687
    • (2005) EMBO Rep. , vol.6 , pp. 681-687
    • Zhu, Y.1    Huang, W.2    Lee, S.S.3    Xu, W.4
  • 20
    • 0026526376 scopus 로고
    • The polyphosphate kinase gene of Escherichia coli. Isolation and sequence of the ppk gene and membrane location of the protein
    • Akiyama M., Crooke E., and Kornberg A. The polyphosphate kinase gene of Escherichia coli. Isolation and sequence of the ppk gene and membrane location of the protein. J. Biol. Chem. 267 (1992) 22556-22561
    • (1992) J. Biol. Chem. , vol.267 , pp. 22556-22561
    • Akiyama, M.1    Crooke, E.2    Kornberg, A.3
  • 21
    • 0027439691 scopus 로고
    • An exopolyphosphatase of Escherichia coli. The enzyme and its ppx gene in a polyphosphate operon
    • Akiyama M., Crooke E., and Kornberg A. An exopolyphosphatase of Escherichia coli. The enzyme and its ppx gene in a polyphosphate operon. J. Biol. Chem. 268 (1993) 633-639
    • (1993) J. Biol. Chem. , vol.268 , pp. 633-639
    • Akiyama, M.1    Crooke, E.2    Kornberg, A.3
  • 22
    • 0030771435 scopus 로고    scopus 로고
    • Guanosine tetra- and pentaphosphate promote accumulation of inorganic polyphosphate in Escherichia coli
    • Kuroda A., Murphy H., Cashel M., and Kornberg A. Guanosine tetra- and pentaphosphate promote accumulation of inorganic polyphosphate in Escherichia coli. J. Biol. Chem. 272 (1997) 21240-21243
    • (1997) J. Biol. Chem. , vol.272 , pp. 21240-21243
    • Kuroda, A.1    Murphy, H.2    Cashel, M.3    Kornberg, A.4
  • 23
    • 0033429137 scopus 로고    scopus 로고
    • Inorganic polyphosphate kinase is required to stimulate protein degradation and for adaptation to amino acid starvation in Escherichia coli
    • Kuroda A., Tanaka S., Ikeda T., Kato J., Takiguchi N., and Ohtake H. Inorganic polyphosphate kinase is required to stimulate protein degradation and for adaptation to amino acid starvation in Escherichia coli. Proc. Natl. Acad. Sci. USA 96 (1999) 14264-14269
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14264-14269
    • Kuroda, A.1    Tanaka, S.2    Ikeda, T.3    Kato, J.4    Takiguchi, N.5    Ohtake, H.6
  • 24
    • 0035958678 scopus 로고    scopus 로고
    • Role of inorganic polyphosphate in promoting ribosomal protein degradation by the Lon protease in E. coli
    • Kuroda A., Nomura K., Ohtomo R., Kato J., Ikeda T., Takiguchi N., Ohtake H., and Kornberg A. Role of inorganic polyphosphate in promoting ribosomal protein degradation by the Lon protease in E. coli. Science 293 (2001) 705-708
    • (2001) Science , vol.293 , pp. 705-708
    • Kuroda, A.1    Nomura, K.2    Ohtomo, R.3    Kato, J.4    Ikeda, T.5    Takiguchi, N.6    Ohtake, H.7    Kornberg, A.8
  • 25
    • 4544343195 scopus 로고    scopus 로고
    • Effects of inorganic polyphosphate on the proteolytic and DNA-binding activities of Lon in Escherichia coli
    • Nomura K., Kato J., Takiguchi N., Ohtake H., and Kuroda A. Effects of inorganic polyphosphate on the proteolytic and DNA-binding activities of Lon in Escherichia coli. J. Biol. Chem. 279 (2004) 34406-34410
    • (2004) J. Biol. Chem. , vol.279 , pp. 34406-34410
    • Nomura, K.1    Kato, J.2    Takiguchi, N.3    Ohtake, H.4    Kuroda, A.5
  • 26
    • 0027817156 scopus 로고
    • Cloning, sequence and characterization of the polyphosphate kinase-encoding gene (ppk) of Klebsiella aerogenes
    • Kato J., Yamamoto T., Yamada K., and Ohtake H. Cloning, sequence and characterization of the polyphosphate kinase-encoding gene (ppk) of Klebsiella aerogenes. Gene 137 (1993) 237-242
    • (1993) Gene , vol.137 , pp. 237-242
    • Kato, J.1    Yamamoto, T.2    Yamada, K.3    Ohtake, H.4
  • 27
    • 0028050069 scopus 로고
    • Production and release of polyphosphate by a genetically engineered strain of Escherichia coli
    • Hardoyo, Yamada K., Shinjo H., Kato J., and Ohtake H. Production and release of polyphosphate by a genetically engineered strain of Escherichia coli. Appl. Environ. Microbiol. 60 (1994) 3485-3490
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 3485-3490
    • Hardoyo1    Yamada, K.2    Shinjo, H.3    Kato, J.4    Ohtake, H.5
  • 29
    • 0038344436 scopus 로고    scopus 로고
    • A method for screening polyphosphate-accumulating mutants which remove phosphate efficiently from synthetic wastewater
    • Morohoshi T., Yamashita T., Kato J., Ikeda T., Takiguchi N., Ohtake H., and Kuroda A. A method for screening polyphosphate-accumulating mutants which remove phosphate efficiently from synthetic wastewater. J. Biosci. Bioeng. 95 (2003) 637-640
    • (2003) J. Biosci. Bioeng. , vol.95 , pp. 637-640
    • Morohoshi, T.1    Yamashita, T.2    Kato, J.3    Ikeda, T.4    Takiguchi, N.5    Ohtake, H.6    Kuroda, A.7
  • 30
  • 31
    • 34248174397 scopus 로고    scopus 로고
    • Relationship between solid retention time and phosphorus removal in anaerobic-intermittent aeration process
    • Lee D., Kim M., and Chung J. Relationship between solid retention time and phosphorus removal in anaerobic-intermittent aeration process. J. Biosci. Bioeng. 103 (2007) 338-344
    • (2007) J. Biosci. Bioeng. , vol.103 , pp. 338-344
    • Lee, D.1    Kim, M.2    Chung, J.3
  • 32
    • 0032210903 scopus 로고    scopus 로고
    • Microbiology and biochemistry of the enhanced biological phosphate removal process
    • Mino T., Van Loosdrecht M.C.M., and Heijnen J.J. Microbiology and biochemistry of the enhanced biological phosphate removal process. Water Res. 32 (1998) 3193-3207
    • (1998) Water Res. , vol.32 , pp. 3193-3207
    • Mino, T.1    Van Loosdrecht, M.C.M.2    Heijnen, J.J.3
  • 33
    • 0032102056 scopus 로고    scopus 로고
    • Effect of carbon source on the formation of polyhydroxyalkanoates (PHA) by a phosphate-accumulating mixed culture
    • Lemos P.C., Viana C., Salgueiro E.N., Ramos A.M., Crespo J.P.S.G., and Reis M.A.M. Effect of carbon source on the formation of polyhydroxyalkanoates (PHA) by a phosphate-accumulating mixed culture. Enzyme Microb. Technol. 22 (1998) 662-671
    • (1998) Enzyme Microb. Technol. , vol.22 , pp. 662-671
    • Lemos, P.C.1    Viana, C.2    Salgueiro, E.N.3    Ramos, A.M.4    Crespo, J.P.S.G.5    Reis, M.A.M.6
  • 34
    • 0026437361 scopus 로고
    • Uptake of organic substrates and accumulation of polyhydroxyalkanoates linked with glycolysis of intracellular carbohydrates under anaerobic conditions in the biological excess phosphate removal process
    • Satoh H., Mino T., and Matsuo T. Uptake of organic substrates and accumulation of polyhydroxyalkanoates linked with glycolysis of intracellular carbohydrates under anaerobic conditions in the biological excess phosphate removal process. Water Sci. Technol. 26 (1992) 933-942
    • (1992) Water Sci. Technol. , vol.26 , pp. 933-942
    • Satoh, H.1    Mino, T.2    Matsuo, T.3
  • 35
    • 0025198351 scopus 로고
    • Polyphosphate-accumulating bacteria from sewage plants with different processes for biological phosphorus removal
    • Straichan M., Golecki J.R., and Schön G. Polyphosphate-accumulating bacteria from sewage plants with different processes for biological phosphorus removal. FEMS Microbiol. Lett. 73 (1990) 113-124
    • (1990) FEMS Microbiol. Lett. , vol.73 , pp. 113-124
    • Straichan, M.1    Golecki, J.R.2    Schön, G.3
  • 36
    • 0028271364 scopus 로고
    • Development of an rRNA-targeted oligonucleotide probe specific for the genus Acinetobacter and its application for in situ monitoring in activated sludge
    • Wagner M., Erhart R., Manz W., Amann R., Lemmer H., Wedi D., and Schleifer K.H. Development of an rRNA-targeted oligonucleotide probe specific for the genus Acinetobacter and its application for in situ monitoring in activated sludge. Appl. Environ. Microbiol. 60 (1994) 792-800
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 792-800
    • Wagner, M.1    Erhart, R.2    Manz, W.3    Amann, R.4    Lemmer, H.5    Wedi, D.6    Schleifer, K.H.7
  • 37
    • 0032822623 scopus 로고    scopus 로고
    • Enrichment, phylogenetic analysis and detection of a bacterium that performs enhanced biological phosphate removal in activated sludge
    • Hesselmann R.P., Werlen C., Hahn D., van der Meer J.R., and Zehnder A.J. Enrichment, phylogenetic analysis and detection of a bacterium that performs enhanced biological phosphate removal in activated sludge. Syst. Appl. Microbiol. 22 (1999) 454-465
    • (1999) Syst. Appl. Microbiol. , vol.22 , pp. 454-465
    • Hesselmann, R.P.1    Werlen, C.2    Hahn, D.3    van der Meer, J.R.4    Zehnder, A.J.5
  • 39
    • 0037023910 scopus 로고    scopus 로고
    • A simple method to release polyphosphate from activated sludge for phosphorus reuse and recycling
    • Kuroda A., Takiguchi N., Gotanda T., Nomura K., Kato J., Ikeda T., and Ohtake H. A simple method to release polyphosphate from activated sludge for phosphorus reuse and recycling. Biotechnol. Bioeng. 78 (2002) 333-338
    • (2002) Biotechnol. Bioeng. , vol.78 , pp. 333-338
    • Kuroda, A.1    Takiguchi, N.2    Gotanda, T.3    Nomura, K.4    Kato, J.5    Ikeda, T.6    Ohtake, H.7
  • 40
    • 0033526531 scopus 로고    scopus 로고
    • Anaerobic phosphate release from activated sludge with enhanced biological phosphorus removal. A possible mechanism of intracellular pH control
    • Bond P.L., Keller J., and Blackall L.L. Anaerobic phosphate release from activated sludge with enhanced biological phosphorus removal. A possible mechanism of intracellular pH control. Biotechnol. Bioeng. 63 (1999) 507-515
    • (1999) Biotechnol. Bioeng. , vol.63 , pp. 507-515
    • Bond, P.L.1    Keller, J.2    Blackall, L.L.3
  • 41
    • 0348195637 scopus 로고    scopus 로고
    • Pilot plant tests on the novel process for phosphorus recovery from municipal wastewater
    • Takiguchi N., Kuroda A., Kato J., Nukanobu K., and Ohtake H. Pilot plant tests on the novel process for phosphorus recovery from municipal wastewater. J. Chem. Eng. Japan 36 (2003) 1143-1146
    • (2003) J. Chem. Eng. Japan , vol.36 , pp. 1143-1146
    • Takiguchi, N.1    Kuroda, A.2    Kato, J.3    Nukanobu, K.4    Ohtake, H.5
  • 42
    • 0032789682 scopus 로고    scopus 로고
    • Struvite formation in wastewater treatment plants: opportunities for nutrient recovery
    • Booker N.A., Priestley A.J., and Fraser I.H. Struvite formation in wastewater treatment plants: opportunities for nutrient recovery. Environ. Technol. 20 (1999) 777-782
    • (1999) Environ. Technol. , vol.20 , pp. 777-782
    • Booker, N.A.1    Priestley, A.J.2    Fraser, I.H.3
  • 43
    • 0034810189 scopus 로고    scopus 로고
    • Conditions influencing the precipitation of magnesium ammonium phosphate
    • Stratful I., Scrimshaw M.D., and Lester J.N. Conditions influencing the precipitation of magnesium ammonium phosphate. Water Res. 35 (2001) 4191-4199
    • (2001) Water Res. , vol.35 , pp. 4191-4199
    • Stratful, I.1    Scrimshaw, M.D.2    Lester, J.N.3
  • 44
    • 0032767968 scopus 로고    scopus 로고
    • Struvite precipitation in the sludge stream at slough wastewater treatment plant and opportunities for phosphorus recovery
    • Williams S. Struvite precipitation in the sludge stream at slough wastewater treatment plant and opportunities for phosphorus recovery. Environ. Technol. 20 (1999) 743-747
    • (1999) Environ. Technol. , vol.20 , pp. 743-747
    • Williams, S.1
  • 45
    • 0035667730 scopus 로고    scopus 로고
    • Three years experience of operating and selling recovered struvite from full-scale plant
    • Ueno Y., and Fujii M. Three years experience of operating and selling recovered struvite from full-scale plant. Environ. Technol. 22 (2001) 1373-1381
    • (2001) Environ. Technol. , vol.22 , pp. 1373-1381
    • Ueno, Y.1    Fujii, M.2
  • 46
    • 0034797540 scopus 로고    scopus 로고
    • Prospects for using soil microorganisms to improve the acquisition of phosphorus by plants
    • Richardson A.E. Prospects for using soil microorganisms to improve the acquisition of phosphorus by plants. Aust. J. Plant Physiol. 28 (2001) 897-906
    • (2001) Aust. J. Plant Physiol. , vol.28 , pp. 897-906
    • Richardson, A.E.1
  • 47
    • 77956672236 scopus 로고    scopus 로고
    • Growth promotion of plants inoculated with phosphate-solubilizing fungi
    • Whitelaw M. Growth promotion of plants inoculated with phosphate-solubilizing fungi. Adv. Agronomy 6 (2000) 99-151
    • (2000) Adv. Agronomy , vol.6 , pp. 99-151
    • Whitelaw, M.1
  • 48
    • 0141455033 scopus 로고    scopus 로고
    • Removal of phosphorus from wastewater by crystallization on the surface of macroporous TiO2 with a fibrous microstructure
    • Nagamine S., Ueda T., Masuda I., Mori T., Sasaoka E., and Joko I. Removal of phosphorus from wastewater by crystallization on the surface of macroporous TiO2 with a fibrous microstructure. Ind. Eng. Chem. Res. 42 (2003) 4748-4752
    • (2003) Ind. Eng. Chem. Res. , vol.42 , pp. 4748-4752
    • Nagamine, S.1    Ueda, T.2    Masuda, I.3    Mori, T.4    Sasaoka, E.5    Joko, I.6
  • 49
    • 0033622688 scopus 로고    scopus 로고
    • Phosphate removal using blast furnace slags and opoka-mechanisms
    • Johansson L., and Gustafsson J.P. Phosphate removal using blast furnace slags and opoka-mechanisms. Water Res. 34 (2000) 259-265
    • (2000) Water Res. , vol.34 , pp. 259-265
    • Johansson, L.1    Gustafsson, J.P.2
  • 51
    • 57149116931 scopus 로고    scopus 로고
    • Recovery of high purity phosphorus from municipal wastewater secondary effluent by a high-speed adsorbent
    • Midorikawa I., Aoki H., Omori A., Shimizu T., Kawaguchi Y., Kassai K., and Murakami T. Recovery of high purity phosphorus from municipal wastewater secondary effluent by a high-speed adsorbent. Water Sci. Technol. 58 (2008) 1601-1607
    • (2008) Water Sci. Technol. , vol.58 , pp. 1601-1607
    • Midorikawa, I.1    Aoki, H.2    Omori, A.3    Shimizu, T.4    Kawaguchi, Y.5    Kassai, K.6    Murakami, T.7
  • 52
    • 0035668114 scopus 로고    scopus 로고
    • Development of artificial seed crystal for crystallization of calcium phosphate
    • Moriyama K., Kojima T., Minawa Y., Matsumoto S., and Nakamachi K. Development of artificial seed crystal for crystallization of calcium phosphate. Environ. Technol. 22 (2001) 1245-1252
    • (2001) Environ. Technol. , vol.22 , pp. 1245-1252
    • Moriyama, K.1    Kojima, T.2    Minawa, Y.3    Matsumoto, S.4    Nakamachi, K.5
  • 55
    • 77949894904 scopus 로고    scopus 로고
    • Bio-based production of rock phosphate for resource recycling and environmental protection
    • Ohtake H., Omasa K., and Honda K. Bio-based production of rock phosphate for resource recycling and environmental protection. J. Biotechnol. 136S (2008) 5602
    • (2008) J. Biotechnol. , vol.136 S , pp. 5602
    • Ohtake, H.1    Omasa, K.2    Honda, K.3
  • 56
    • 0026358279 scopus 로고
    • Volcanic production of polyphosphate and its relevance to prebiotic evolution
    • Yamagata Y., Watanabe H., Saitoh M., and Namba T. Volcanic production of polyphosphate and its relevance to prebiotic evolution. Nature 352 (1991) 516-520
    • (1991) Nature , vol.352 , pp. 516-520
    • Yamagata, Y.1    Watanabe, H.2    Saitoh, M.3    Namba, T.4
  • 57
    • 0027404023 scopus 로고
    • Convergent evolution of similar enzymatic function on different protein folds: the hexokinase, ribokinase, and galactokinase families of sugar kinases
    • Bork P., Sander C., and Valencia A. Convergent evolution of similar enzymatic function on different protein folds: the hexokinase, ribokinase, and galactokinase families of sugar kinases. Protein Sci. 2 (1993) 31-40
    • (1993) Protein Sci. , vol.2 , pp. 31-40
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 58
    • 0000183334 scopus 로고
    • Inorganic polyphosphate glucokinase of Mycobacterium phlei
    • Szymona M., and Ostrowski W. Inorganic polyphosphate glucokinase of Mycobacterium phlei. Biochim. Biophys. Acta 85 (1964) 283-295
    • (1964) Biochim. Biophys. Acta , vol.85 , pp. 283-295
    • Szymona, M.1    Ostrowski, W.2
  • 59
    • 0016195744 scopus 로고
    • A kinetic study on inorganic polyphosphate glucokinase from Mycobacterium tuberculosis H37RA
    • Szymona M., and Widomski J. A kinetic study on inorganic polyphosphate glucokinase from Mycobacterium tuberculosis H37RA. Physiol. Chem. Phys. 6 (1974) 393-404
    • (1974) Physiol. Chem. Phys. , vol.6 , pp. 393-404
    • Szymona, M.1    Widomski, J.2
  • 60
    • 0021992308 scopus 로고
    • Phosphorylation enzymes of the propionic acid bacteria and the roles of ATP inorganic pyrophosphate, and polyphosphates
    • Wood H.G., and Goss N.H. Phosphorylation enzymes of the propionic acid bacteria and the roles of ATP inorganic pyrophosphate, and polyphosphates. Proc. Natl. Acad. Sci. USA 82 (1985) 312-315
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 312-315
    • Wood, H.G.1    Goss, N.H.2
  • 61
    • 0028887833 scopus 로고
    • Microlunatus phosphovorus gen. nov., sp. nov., a new gram-positive polyphosphate-accumulating bacterium isolated from activated sludge
    • Nakamura K., Hiraishi A., Yoshimi Y., Kawaharasaki M., Masuda K., and Kamagata Y. Microlunatus phosphovorus gen. nov., sp. nov., a new gram-positive polyphosphate-accumulating bacterium isolated from activated sludge. Int. J. Syst. Bacteriol. 45 (1995) 17-22
    • (1995) Int. J. Syst. Bacteriol. , vol.45 , pp. 17-22
    • Nakamura, K.1    Hiraishi, A.2    Yoshimi, Y.3    Kawaharasaki, M.4    Masuda, K.5    Kamagata, Y.6
  • 62
    • 0041835984 scopus 로고    scopus 로고
    • Strictly polyphosphate-dependent glucokinase in a polyphosphate-accumulating bacterium, Microlunatus phosphovorus
    • Tanaka S., Lee S.O., Hamaoka K., Kato J., Takiguchi N., Nakamura K., Ohtake H., and Kuroda A. Strictly polyphosphate-dependent glucokinase in a polyphosphate-accumulating bacterium, Microlunatus phosphovorus. J. Bacteriol. 185 (2003) 5654-5656
    • (2003) J. Bacteriol. , vol.185 , pp. 5654-5656
    • Tanaka, S.1    Lee, S.O.2    Hamaoka, K.3    Kato, J.4    Takiguchi, N.5    Nakamura, K.6    Ohtake, H.7    Kuroda, A.8
  • 63
    • 0035665974 scopus 로고    scopus 로고
    • A sensitive method for detecting AMP by utilizing polyphosphate-dependent ATP regeneration and bioluminescence reactions
    • Tanaka S., Kuroda S., Kato J., Ikeda T., Takiguchi N., and Ohtake H. A sensitive method for detecting AMP by utilizing polyphosphate-dependent ATP regeneration and bioluminescence reactions. Biochem. Eng. J. 9 (2001) 193-197
    • (2001) Biochem. Eng. J. , vol.9 , pp. 193-197
    • Tanaka, S.1    Kuroda, S.2    Kato, J.3    Ikeda, T.4    Takiguchi, N.5    Ohtake, H.6
  • 64
    • 34548514448 scopus 로고    scopus 로고
    • Use of an Escherichia coli recombinant producing thermostable polyphosphate kinase as an ATP regenerator to produce fructose 1,6-diphosphate
    • Iwamoto S., Motomura K., Shinoda Y., Urata M., Kato J., Takiguchi N., Ohtake H., Hirota R., and Kuroda A. Use of an Escherichia coli recombinant producing thermostable polyphosphate kinase as an ATP regenerator to produce fructose 1,6-diphosphate. Appl. Environ. Microbiol. 73 (2007) 5676-5678
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 5676-5678
    • Iwamoto, S.1    Motomura, K.2    Shinoda, Y.3    Urata, M.4    Kato, J.5    Takiguchi, N.6    Ohtake, H.7    Hirota, R.8    Kuroda, A.9
  • 65
    • 33947166251 scopus 로고    scopus 로고
    • Thermostable ATP regeneration system using polyphosphate kinase from Thermosynechococcus elongatus BP-1 for D-amino acid dipeptide synthesis
    • Sato M., Masuda Y., Kirimura K., and Kino K. Thermostable ATP regeneration system using polyphosphate kinase from Thermosynechococcus elongatus BP-1 for D-amino acid dipeptide synthesis. J. Biosci. Bioeng. 103 (2007) 179-184
    • (2007) J. Biosci. Bioeng. , vol.103 , pp. 179-184
    • Sato, M.1    Masuda, Y.2    Kirimura, K.3    Kino, K.4
  • 66
    • 33751421505 scopus 로고    scopus 로고
    • Substrate specificity of thermostable D-alanine-D-alanine ligase from Thermotoga maritima ATCC 43589
    • Sato M., Kirimura K., and Kino K. Substrate specificity of thermostable D-alanine-D-alanine ligase from Thermotoga maritima ATCC 43589. Biosci. Biotechnol. Biochem. 70 (2006) 2790-2792
    • (2006) Biosci. Biotechnol. Biochem. , vol.70 , pp. 2790-2792
    • Sato, M.1    Kirimura, K.2    Kino, K.3


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