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Volumn 80, Issue 3, 2011, Pages 335-340

Phosphonoacetate biosynthesis: In vitro detection of a novel NADP+-dependent phosphonoacetaldehyde-oxidizing activity in cell-extracts of a marine Roseobacter

Author keywords

2 aminoethylphosphonate; phosphonoacetaldehyde dehydrogenase; phosphonoacetate biosynthesis

Indexed keywords

BACTERIA (MICROORGANISMS); ROSEOBACTER; ROSEOVARIUS NUBINHIBENS ISM;

EID: 79958280148     PISSN: 00262617     EISSN: None     Source Type: Journal    
DOI: 10.1134/S0026261711030076     Document Type: Article
Times cited : (7)

References (25)
  • 1
    • 0001519381 scopus 로고
    • The Presence of Compounds with a Carbon-Phosphorus Bond in Some Marine Invertebrates
    • Quin, L. D., The Presence of Compounds with a Carbon-Phosphorus Bond in Some Marine Invertebrates, Biochemistry, 1965, vol. 4, pp. 324-330.
    • (1965) Biochemistry , vol.4 , pp. 324-330
    • Quin, L.D.1
  • 2
    • 0014939793 scopus 로고
    • Biological Phosphonates - Determination by P-31 Nuclear Magnetic Resonance
    • Glonek, T., Henderson, T. O., Hilderbrand, R. L., and Myers, T. C., Biological Phosphonates - Determination by P-31 Nuclear Magnetic Resonance. Science, 1970, vol. 169 pp. 192-194.
    • (1970) Science , vol.169 , pp. 192-194
    • Glonek, T.1    Henderson, T.O.2    Hilderbrand, R.L.3    Myers, T.C.4
  • 3
    • 67650743221 scopus 로고    scopus 로고
    • Biosynthesis of Phosphonic and Phosphinic Acid Natural Products
    • Metcalf, W. W. and van der Donk, W. A., Biosynthesis of Phosphonic and Phosphinic Acid Natural Products, Annu. Rev. Biochem., 2009, vol. 78, pp 65-94.
    • (2009) Annu. Rev. Biochem , vol.78 , pp. 65-94
    • Metcalf, W.W.1    van der Donk, W.A.2
  • 4
    • 34548379026 scopus 로고    scopus 로고
    • New Ways to Break an Old Bond: the Bacterial Carbon-Phosphorus Hydrolases and Their Role in Biogeochemical Phosphorus Cycling
    • Quinn, J. P., Kulakova, A. N., Cooley, N. A., and McGrath, J. W., New Ways to Break an Old Bond: the Bacterial Carbon-Phosphorus Hydrolases and Their Role in Biogeochemical Phosphorus Cycling, Environ. Microbiol., 2007, vol. 9, pp. 2392-2400.
    • (2007) Environ. Microbiol , vol.9 , pp. 2392-2400
    • Quinn, J.P.1    Kulakova, A.N.2    Cooley, N.A.3    McGrath, J.W.4
  • 5
    • 0032581010 scopus 로고    scopus 로고
    • Insights into the Mechanism of Catalysis by the P-C Bond-Cleaving Enzyme Phosphonoacetaldehyde Hydrolase Derived from Gene Sequence Analysis and Mutagenesis
    • Baker, A. S., Ciocci, M. J., Metcalf, W. W., Kim, J., Babbitt, P. C., Wanner, B. L., Martin, B. M., and Dunaway-Mariano, D., Insights into the Mechanism of Catalysis by the P-C Bond-Cleaving Enzyme Phosphonoacetaldehyde Hydrolase Derived from Gene Sequence Analysis and Mutagenesis, Biochemistry, 1998, vol. 37, pp. 9305-9315.
    • (1998) Biochemistry , vol.37 , pp. 9305-9315
    • Baker, A.S.1    Ciocci, M.J.2    Metcalf, W.W.3    Kim, J.4    Babbitt, P.C.5    Wanner, B.L.6    Martin, B.M.7    Dunaway-Mariano, D.8
  • 6
    • 0028801167 scopus 로고
    • Molecular-Cloning, Mapping, and Regulation of pho Regulon Genes for Phosphonate Breakdown by the Phosphonatase Pathway of Salmonella typhimurium LT2
    • Jiang, W. H., Metcalf, W. W., Lee, K. S., and Wanner, B. L., Molecular-Cloning, Mapping, and Regulation of pho Regulon Genes for Phosphonate Breakdown by the Phosphonatase Pathway of Salmonella typhimurium LT2, J. Bacteriol., 1995, vol. 177, pp. 6411-6421.
    • (1995) J. Bacteriol , vol.177 , pp. 6411-6421
    • Jiang, W.H.1    Metcalf, W.W.2    Lee, K.S.3    Wanner, B.L.4
  • 7
    • 0031771343 scopus 로고    scopus 로고
    • Organophosphonates: Occurrence, Synthesis and Biodegradation by Microorganisms
    • Ternan, N. G., McGrath, J. W., McMullan, G., and Quinn, J. P., Organophosphonates: Occurrence, Synthesis and Biodegradation by Microorganisms, World J. Microb. Biot., 1998, vol. 14, pp. 635-647.
    • (1998) World J. Microb. Biot , vol.14 , pp. 635-647
    • Ternan, N.G.1    McGrath, J.W.2    McMullan, G.3    Quinn, J.P.4
  • 8
    • 0031716877 scopus 로고    scopus 로고
    • Phosphate Starvation-Independent 2-Aminoethylphosphonic Acid Biodegradation in a Newly Isolated Strain of Pseudomonas putida, NG2
    • Ternan, N. G. and Quinn, J. P., Phosphate Starvation-Independent 2-Aminoethylphosphonic Acid Biodegradation in a Newly Isolated Strain of Pseudomonas putida, NG2, Syst. Appl. Microbiol., 1998, vol. 21, pp. 346-352.
    • (1998) Syst. Appl. Microbiol , vol.21 , pp. 346-352
    • Ternan, N.G.1    Quinn, J.P.2
  • 9
    • 0000288758 scopus 로고
    • The Marine Gram-Negative Eubacteria: Genera Photobacterium, Beneckea, Alteromonas, Pseudomonas, and Alcaligenes
    • M. P. Starr, H. Stolp, A. Truper, A. Balows, and H. G. Schlegel (Eds.), Berlin: Springer
    • Baumann, P. and Baumann L., The Marine Gram-Negative Eubacteria: Genera Photobacterium, Beneckea, Alteromonas, Pseudomonas, and Alcaligenes, in The Prokaryotes, Starr, M. P., Stolp, H., Truper, A., Balows, A., and Schlegel, H. G., Eds., Berlin, Springer, 1981, pp. 1302-1331.
    • (1981) The Prokaryotes , pp. 1302-1331
    • Baumann, P.1    Baumann, L.2
  • 10
    • 0029878360 scopus 로고    scopus 로고
    • Degradation of Pentaerythritol Tetranitrate by Enterobacter cloacae PB2
    • Binks, P. R., French, C. E., Nicklin, S., and Bruce N. C., Degradation of Pentaerythritol Tetranitrate by Enterobacter cloacae PB2. Appl. Environ. Microbiol., 1996, vol. 62, pp. 1214-1219.
    • (1996) Appl. Environ. Microbiol , vol.62 , pp. 1214-1219
    • Binks, P.R.1    French, C.E.2    Nicklin, S.3    Bruce, N.C.4
  • 11
    • 0000154206 scopus 로고
    • The Colorimetric Determination of Phosphorus
    • Fiske, C. H. and Subbarow, Y., The Colorimetric Determination of Phosphorus, J. Biol. Chem., 1925, vol. 66, pp. 375-400.
    • (1925) J. Biol. Chem , vol.66 , pp. 375-400
    • Fiske, C.H.1    Subbarow, Y.2
  • 12
    • 0028791603 scopus 로고
    • The Purification and Properties of Phosphonoacetate Hydrolase, a Novel Carbon-Phosphorus Bond-Cleavage Enzyme from Pseudomonas fluorescens, 23F
    • McGrath, J. W., Wisdom, G. B., McMullan, G., Larkin, M. J., and Quinn, J. P., The Purification and Properties of Phosphonoacetate Hydrolase, a Novel Carbon-Phosphorus Bond-Cleavage Enzyme from Pseudomonas fluorescens, 23F. Eur. J. Biochem., 1995, vol. 234, pp. 225-230.
    • (1995) Eur. J. Biochem , vol.234 , pp. 225-230
    • McGrath, J.W.1    Wisdom, G.B.2    McMullan, G.3    Larkin, M.J.4    Quinn, J.P.5
  • 13
    • 0017184389 scopus 로고
    • A rapid and Sensitive Detection Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding
    • Bradford, M. M., A rapid and Sensitive Detection Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding, Anal. Biochem., 1976, vol. 72, pp. 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 14
    • 0016284688 scopus 로고
    • New Assay Method of Gamma-Amino Acid Aminotransferase with ortho-aminobenzaldehyde
    • Toyama, S., New Assay Method of Gamma-Amino Acid Aminotransferase with ortho-aminobenzaldehyde, Agr. Biol. Chem., 1974, vol. 38, pp. 2263-2265.
    • (1974) Agr. Biol. Chem , vol.38 , pp. 2263-2265
    • Toyama, S.1
  • 15
    • 0035491591 scopus 로고    scopus 로고
    • Isolation of an Aldehyde Dehydrogenase Involved in the Oxidation of Fluoroacetaldehyde to Fluoroacetate in Streptomyces cattleya
    • Murphy, C. D., Moss, S. J., and O'Hagan, D. Isolation of an Aldehyde Dehydrogenase Involved in the Oxidation of Fluoroacetaldehyde to Fluoroacetate in Streptomyces cattleya, Appl. Environ. Microbiol., 2001, vol 67, pp. 4919-4921.
    • (2001) Appl. Environ. Microbiol , vol.67 , pp. 4919-4921
    • Murphy, C.D.1    Moss, S.J.2    O'Hagan, D.3
  • 16
    • 5444257938 scopus 로고    scopus 로고
    • Sulfoacetate Generated by Rhodopseudomonas palustris from Taurine
    • Denger, K., Weinitschke, S., Hollemeyer, K., and Cook, A. M., Sulfoacetate Generated by Rhodopseudomonas palustris from Taurine, Arch. Microbiol., 2004, vol. 182, pp. 254-258.
    • (2004) Arch. Microbiol , vol.182 , pp. 254-258
    • Denger, K.1    Weinitschke, S.2    Hollemeyer, K.3    Cook, A.M.4
  • 17
    • 47349097845 scopus 로고    scopus 로고
    • Sulfoacetate Released during the Assimilation of Taurine-Nitrogen by Neptuniibacter caesariensis: Purification of Sulfoacetaldehyde Dehydrogenase
    • Krejcik, Z., Denger, K., Weinitschke, S., Hollemeyer, K., Paces, V., Cook, A. M., and Smits, T. H. M., Sulfoacetate Released during the Assimilation of Taurine-Nitrogen by Neptuniibacter caesariensis: Purification of Sulfoacetaldehyde Dehydrogenase, Arch. Microbiol., 2008, vol. 190, pp. 159-168.
    • (2008) Arch. Microbiol , vol.190 , pp. 159-168
    • Krejcik, Z.1    Denger, K.2    Weinitschke, S.3    Hollemeyer, K.4    Paces, V.5    Cook, A.M.6    Smits, T.H.M.7
  • 18
    • 0035031803 scopus 로고    scopus 로고
    • Structural and Functional Analysis of the Phosphonoacetate Hydrolase (phnA) Gene Region in Pseudomonas fluorescens 23F
    • Kulakova, A. N., Kulakov, L. A., Akulenko, N. V., Ksenzenko, V. N., Hamilton, J. T. G., and Quinn, J. P., Structural and Functional Analysis of the Phosphonoacetate Hydrolase (phnA) Gene Region in Pseudomonas fluorescens 23F, J. Bacteriol., 2001, vol. 183, pp. 3268-3275.
    • (2001) J. Bacteriol , vol.183 , pp. 3268-3275
    • Kulakova, A.N.1    Kulakov, L.A.2    Akulenko, N.V.3    Ksenzenko, V.N.4    Hamilton, J.T.G.5    Quinn, J.P.6
  • 19
    • 0030792169 scopus 로고    scopus 로고
    • Cloning of the Phosphonoacetate Hydrolase Gene from Pseudomonas fluorescens 23F Encoding a New Type of Carbon-Phosphorus Bond Cleaving Enzyme and Its Expression in Escherichia coli and Pseudomonas putida
    • Kulakova, A. N., Kulakov, L. A., and Quinn, J. P. Cloning of the Phosphonoacetate Hydrolase Gene from Pseudomonas fluorescens 23F Encoding a New Type of Carbon-Phosphorus Bond Cleaving Enzyme and Its Expression in Escherichia coli and Pseudomonas putida, Gene, 1997, vol. 195, pp. 49-53.
    • (1997) Gene , vol.195 , pp. 49-53
    • Kulakova, A.N.1    Kulakov, L.A.2    Quinn, J.P.3
  • 20
    • 0023656153 scopus 로고
    • Three Different Proteins Exhibiting NAD-Dependent Acetaldehyde Dehydrogenase-Activity from Alcaligenes eutrophus
    • Jendrossek, D., Steinbuchel, A., and Schlegel, H. G., Three Different Proteins Exhibiting NAD-Dependent Acetaldehyde Dehydrogenase-Activity from Alcaligenes eutrophus, Eur. J. Biochem 1987, vol. 167, pp. 541-548.
    • (1987) Eur. J. Biochem , vol.167 , pp. 541-548
    • Jendrossek, D.1    Steinbuchel, A.2    Schlegel, H.G.3
  • 21
    • 27044437181 scopus 로고
    • Purification and Properties of 5 NADP-Dependent Aldehyde Dehydrogenases from Aceto-bacter aceti
    • Muraoka, H., Watabe, Y., Ogasawara, N., and Takahashi, H., Purification and Properties of 5 NADP-Dependent Aldehyde Dehydrogenases from Aceto-bacter aceti, J. Ferment. Technol., 1980, vol. 58, pp. 501-507.
    • (1980) J. Ferment. Technol , vol.58 , pp. 501-507
    • Muraoka, H.1    Watabe, Y.2    Ogasawara, N.3    Takahashi, H.4
  • 22
    • 0035209306 scopus 로고    scopus 로고
    • NAD(P)-Dependent Aldehyde Dehydrogenases Induced during Growth of Ralstonia eutropha Strain Bo on Tetrahydrofurfuryl Alcohol
    • Schrader, T., Zarnt, G., and Andreesen, J. R., NAD(P)-Dependent Aldehyde Dehydrogenases Induced during Growth of Ralstonia eutropha Strain Bo on Tetrahydrofurfuryl Alcohol, J. Bacteriol., 2001, vol. 183, pp. 7408-7411.
    • (2001) J. Bacteriol , vol.183 , pp. 7408-7411
    • Schrader, T.1    Zarnt, G.2    Andreesen, J.R.3
  • 24
    • 33645457997 scopus 로고    scopus 로고
    • Detection of Phosphonoacetate Degradation and phnA Genes in Soil Bacteria from Distinct Geographical Origins Suggest Its Possible Biogenic Origin
    • Panas, P., Ternan, N. G., Dooley, J. S. G., and McMullan, G., Detection of Phosphonoacetate Degradation and phnA Genes in Soil Bacteria from Distinct Geographical Origins Suggest Its Possible Biogenic Origin, Environ. Microbiol., 2006, vol. 8, pp 939-945.
    • (2006) Environ. Microbiol , vol.8 , pp. 939-945
    • Panas, P.1    Ternan, N.G.2    Dooley, J.S.G.3    McMullan, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.