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Volumn 11, Issue 6, 2013, Pages 412-419

Organophosphonates revealed: New insights into the microbial metabolism of ancient molecules

Author keywords

[No Author keywords available]

Indexed keywords

2 AMINOETHYLPHOSPHONIC ACID; 2 OXOGLUTARIC ACID; ACYLTRANSFERASE; CARBOXYLYASE; DNA POLYMERASE; FOSFOMYCIN; GLYPHOSATE; MUTASE; PHOSPHOENOLPYRUVATE; PHOSPHOENOLPYRUVATE PHOSPHOMUTASE; PHOSPHOETHANOLAMINE; PHOSPHONIC ACID DERIVATIVE; PHOSPHONOPYRUVATE DECARBOXYLASE; PHOSPHORIBOSYLTRANSFERASE; RNA POLYMERASE; S ADENOSYLMETHIONINE; UNCLASSIFIED DRUG;

EID: 84878016894     PISSN: 17401526     EISSN: 17401534     Source Type: Journal    
DOI: 10.1038/nrmicro3011     Document Type: Review
Times cited : (187)

References (89)
  • 2
    • 0033607218 scopus 로고    scopus 로고
    • Insight into the mechanism of phosphoenolpyruvate mutase catalysis derived from site-directed mutagenesis studies of active site residues
    • Jia, Y., Lu, Z. B., Huang, K., Herzberg, O. & Dunaway-Mariano, D. Insight into the mechanism of phosphoenolpyruvate mutase catalysis derived from site-directed mutagenesis studies of active site residues. Biochemistry 38, 14165-14173 (1999).
    • (1999) Biochemistry , vol.38 , pp. 14165-14173
    • Jia, Y.1    Lu, Z.B.2    Huang, K.3    Herzberg, O.4    Dunaway-Mariano, D.5
  • 4
    • 0345129307 scopus 로고
    • Cleavage of the carbon to phosphorus bond of organophosphonates by bacterial systems
    • Lacoste, A. M., Dumora, C. & Cassaigne, A. Cleavage of the carbon to phosphorus bond of organophosphonates by bacterial systems. Biochem. Adv. (Life Sci. ) 8, 97-109 (1989).
    • (1989) Biochem. Adv. (Life Sci. ) , vol.8 , pp. 97-109
    • Lacoste, A.M.1    Dumora, C.2    Cassaigne, A.3
  • 5
    • 0000627987 scopus 로고
    • Isolation of 2-aminoethane phosphonic acid from rumen protozoa
    • Horiguchi, M. & Kandatsu, M. Isolation of 2-aminoethane phosphonic acid from rumen protozoa. Nature 184, 901-902 (1959).
    • (1959) Nature , vol.184 , pp. 901-902
    • Horiguchi, M.1    Kandatsu, M.2
  • 7
    • 67650743221 scopus 로고    scopus 로고
    • Biosynthesis of phosphonic and phosphinic acid natural products
    • Metcalf, W. W. & van der Donk, W. A. Biosynthesis of phosphonic and phosphinic acid natural products. Annu. Rev. Biochem. 78, 65-94 (2009).
    • (2009) Annu. Rev. Biochem , vol.78 , pp. 65-94
    • Metcalf, W.W.1    Van Der Donk, W.A.2
  • 8
    • 0014662797 scopus 로고
    • Phosphonomycin, a new antibiotic produced by strains of Streptomyces
    • Hendlin, D. et al. Phosphonomycin, a new antibiotic produced by strains of Streptomyces. Science 166, 122-123 (1969).
    • (1969) Science , vol.166 , pp. 122-123
    • Hendlin, D.1
  • 9
    • 0017142363 scopus 로고
    • Studies on new antimetabolite produced by microorganism 2-amino-5-phosphono-3-pentenoic acid, a new amino-acid from N-1409 substance, an antagonist of threonine
    • Park, B. K., Hirota, A. & Sakai, H. Studies on new antimetabolite produced by microorganism 2-amino-5-phosphono-3-pentenoic acid, a new amino-acid from N-1409 substance, an antagonist of threonine. Agric. Biol. Chem. 40, 1905-1906 (1976).
    • (1976) Agric. Biol. Chem , vol.40 , pp. 1905-1906
    • Park, B.K.1    Hirota, A.2    Sakai, H.3
  • 10
    • 0015530581 scopus 로고
    • Metabolic products of microorganisms. 98. Phosphinothricin and phosphinothricyl-alanyl-analine
    • Bayer, E. et al. Metabolic products of microorganisms. 98. Phosphinothricin and phosphinothricyl-alanyl-analine. Helv. Chim. Acta 55, 224-239 (1972).
    • (1972) Helv. Chim. Acta , vol.55 , pp. 224-239
    • Bayer, E.1
  • 11
    • 34548379026 scopus 로고    scopus 로고
    • New ways to break an old bond: The bacterial carbon-phosphorus hydrolases and their role in biogeochemical phosphorus cycling
    • DOI 10.1111/j.1462-2920.2007.01397.x
    • Quinn, J. P., Kulakova, A. N., Cooley, N. A. & McGrath, J. W. New ways to break an old bond: the bacterial carbon-phosphorus hydrolases and their role in biogeochemical phosphorus cycling. Environ. Microbiol. 9, 2392-2400 (2007). This review describes phosphonate turnover in the marine environment and provides a bioinformatic analysis of the distribution of both C-P lyase and C-P hydrolases. (Pubitemid 47366673)
    • (2007) Environmental Microbiology , vol.9 , Issue.10 , pp. 2392-2400
    • Quinn, J.P.1    Kulakova, A.N.2    Cooley, N.A.3    McGrath, J.W.4
  • 12
    • 0023785036 scopus 로고
    • Catalysis and thermodynamics of the phosphoenolpyruvate phosphonopyruvate rearrangement. Entry into the phosphonate class of naturally-occurring organo-phosphorus compounds
    • Bowman, E., McQueney, M., Barry, R. J. & Dunaway- Mariano, D. Catalysis and thermodynamics of the phosphoenolpyruvate phosphonopyruvate rearrangement. Entry into the phosphonate class of naturally-occurring organo-phosphorus compounds. J. Am. Chem. Soc. 110, 5575-5576 (1988).
    • (1988) J. Am. Chem. Soc , vol.110 , pp. 5575-5576
    • Bowman, E.1    McQueney, M.2    Barry, R.J.3    Dunaway-Mariano, D.4
  • 13
    • 0024299578 scopus 로고
    • Phosphonate biosynthesis: Isolation of the enzyme responsible for the formation of a carbon-phosphorus bond
    • Seidel, H. M., Freeman, S., Seto, H. & Knowles, J. R. Phosphonate biosynthesis: isolation of the enzyme responsible for the formation of a carbon-phosphorus bond. Nature 335, 457-458 (1988).
    • (1988) Nature , vol.335 , pp. 457-458
    • Seidel, H.M.1    Freeman, S.2    Seto, H.3    Knowles, J.R.4
  • 14
    • 0142103330 scopus 로고    scopus 로고
    • The Phosphonopyruvate Decarboxylase from Bacteroides fragilis
    • DOI 10.1074/jbc.M305976200
    • Zhang, G. F., Dai, J. Y., Lu, Z. B. & Dunaway-Mariano, D. The phosphonopyruvate decarboxylase from Bacteroides fragilis. J. Biol. Chem. 278, 41302-41308 (2003). (Pubitemid 37280958)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.42 , pp. 41302-41308
    • Zhang, G.1    Dai, J.2    Lu, Z.3    Dunaway-Mariano, D.4
  • 15
    • 0024300794 scopus 로고
    • Elucidation of the 2-aminoethylphosphonate biosynthetic pathway in Tetrahymena pyriformis
    • Barry, R. J., Bowman, E., McQueney, M. & Dunaway-Mariano, D. Elucidation of the 2-aminoethylphosphonate biosynthetic pathway in Tetrahymena pyriformis. Biochem. Biophys. Res. Commun. 153, 177-182 (1988).
    • (1988) Biochem. Biophys. Res. Commun , vol.153 , pp. 177-182
    • Barry, R.J.1    Bowman, E.2    McQueney, M.3    Dunaway-Mariano, D.4
  • 16
    • 77949915670 scopus 로고    scopus 로고
    • Global regulation by the seven-component Pi signaling system
    • Hsieh, Y. J. & Wanner, B. L. Global regulation by the seven-component Pi signaling system. Curr. Opin. Microbiol. 13, 198-203 (2010). This review provides a comprehensive overview of how E. coli detects environmental inorganic orthophosphate to regulate genes of the Pho regulon.
    • (2010) Curr. Opin. Microbiol , vol.13 , pp. 198-203
    • Hsieh, Y.J.1    Wanner, B.L.2
  • 17
    • 42149150462 scopus 로고    scopus 로고
    • The phosphate regulon and bacterial virulence: A regulatory network connecting phosphate homeostasis and pathogenesis
    • DOI 10.1111/j.1574-6976.2008.00101.x
    • Lamarche, M. G., Wanner, B. L., Crepin, S. & Harel, J. The phosphate regulon and bacterial virulence: a regulatory network connecting phosphate homeostasis and pathogenesis. FEMS Microbiol. Rev. 32, 461-473 (2008). (Pubitemid 351538744)
    • (2008) FEMS Microbiology Reviews , vol.32 , Issue.3 , pp. 461-473
    • Lamarche, M.G.1    Wanner, B.L.2    Crepin, S.3    Harel, J.4
  • 18
    • 33744797980 scopus 로고    scopus 로고
    • Genome prediction of PhoB regulated promoters in Sinorhizobium meliloti and twelve proteobacteria
    • DOI 10.1093/nar/gkl365
    • Yuan, Z. C., Zaheer, R., Morton, R. & Finan, T. M. Genome prediction of PhoB regulated promoters in Sinorhizobium meliloti and twelve proteobacteria. Nucleic Acids Res. 34, 2686-2697 (2006). (Pubitemid 43985631)
    • (2006) Nucleic Acids Research , vol.34 , Issue.9 , pp. 2686-2697
    • Yuan, Z.-C.1    Zaheer, R.2    Morton, R.3    Finan, T.M.4
  • 19
    • 0030895003 scopus 로고    scopus 로고
    • The pst operon of Bacillus subtilis has a phosphate-regulated promoter and is involved in phosphate transport but not in regulation of the Pho regulon
    • Qi, Y., Kobayashi, Y. & Hulett, F. M. The pst operon of Bacillus subtilis has a phosphate-regulated promoter and is involved in phosphate transport but not in regulation of the Pho regulon. J. Bacteriol. 179, 2534-2539 (1997). (Pubitemid 27164551)
    • (1997) Journal of Bacteriology , vol.179 , Issue.8 , pp. 2534-2539
    • Qi, Y.1    Kobayashi, Y.2    Hulett, F.M.3
  • 20
    • 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, 175-184 (1994).
    • (1994) Biodegradation , vol.5 , pp. 175-184
    • Wanner, B.L.1
  • 21
    • 0031055690 scopus 로고    scopus 로고
    • Utilization of organophosphonates by environmental microorganisms
    • McGrath, J. W., Ternan, N. G. & Quinn, J. P. Utilization of organophosphonates by environmental microorganisms. Lett. Appl. Microbiol. 24, 69-73 (1997). (Pubitemid 27064574)
    • (1997) Letters in Applied Microbiology , vol.24 , Issue.1 , pp. 69-73
    • McGrath, J.W.1    Ternan, N.G.2    Quinn, J.P.3
  • 22
    • 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. & Walsh, C. T. Bacterial carbon-phosphorus lyase: products, rates, and regulation of phosphonic and phosphinic acid metabolism. J. Bacteriol. 169, 710-717 (1987). (Pubitemid 17010886)
    • (1987) Journal of Bacteriology , vol.169 , Issue.2 , pp. 710-717
    • Wackett, L.P.1    Shames, S.L.2    Venditti, C.P.3    Walsh, C.T.4
  • 24
    • 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 B
    • Chen, C. M., Ye, Q. Z., Zhu, Z. M., Wanner, B. L. & 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, 4461-4471 (1990).
    • (1990) 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
  • 25
    • 0031859636 scopus 로고    scopus 로고
    • Phosphate-independent expression of the carbon-phosphorus lyase activity of Escherichia coli
    • DOI 10.1007/s002530051215
    • Yakovleva, G. M., Kim, S. K. & Wanner, B. L. Phosphate-independent expression of the carbon-phosphorus lyase activity of Escherichia coli. Appl. Microbiol. Biotechnol. 49, 573-578 (1998). (Pubitemid 28267250)
    • (1998) Applied Microbiology and Biotechnology , vol.49 , Issue.5 , pp. 573-578
    • Yakovleva, G.M.1    Kim, S.K.2    Wanner, B.L.3
  • 26
    • 0025819276 scopus 로고
    • Metabolites associated with organophosphonate C-P bond-cleavage: Chemical synthesis and microbial-degradation of [32P]-ethylphosphonic acid
    • Avila, L. Z., Draths, K. M. & Frost, J. W. Metabolites associated with organophosphonate C-P bond-cleavage: chemical synthesis and microbial-degradation of [32P]-ethylphosphonic acid. Bioorg. Med. Chem. Lett. 1, 51-54 (1991).
    • (1991) Bioorg. Med. Chem. Lett , vol.1 , pp. 51-54
    • Avila, L.Z.1    Draths, K.M.2    Frost, J.W.3
  • 27
    • 84867068020 scopus 로고    scopus 로고
    • Catabolism and detoxification of 1-aminoalkylphosphonic acids: N-acetylation by the phnO gene product
    • Hove-Jensen, B., McSorley, F. R. & Zechel, D. L. Catabolism and detoxification of 1-aminoalkylphosphonic acids: N-acetylation by the phnO gene product. PLoS ONE 7, e46416 (2012).
    • (2012) PLoS ONE , vol.7
    • Hove-Jensen, B.1    McSorley, F.R.2    Zechel, D.L.3
  • 28
    • 80053600609 scopus 로고    scopus 로고
    • Structure and mechanism of PhnP, a phosphodiesterase of the carbon-phosphorus lyase pathway
    • He, S. M. et al. Structure and mechanism of PhnP, a phosphodiesterase of the carbon-phosphorus lyase pathway. Biochemistry 50, 8603-8615 (2011).
    • (2011) Biochemistry , vol.50 , pp. 8603-8615
    • He, S.M.1
  • 29
    • 79960983742 scopus 로고    scopus 로고
    • Five phosphonate operon gene products as components of a multi-subunit complex of the carbon-phosphorus lyase pathway
    • Jochimsen, B. et al. Five phosphonate operon gene products as components of a multi-subunit complex of the carbon-phosphorus lyase pathway. Proc. Natl Acad. Sci. USA 108, 11393-11398 (2011). This article is the first to report the purification of a soluble complex of the five proteins central to the reaction catalysed by bacterial C-P lyase.
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 11393-11398
    • Jochimsen, B.1
  • 30
    • 84355162021 scopus 로고    scopus 로고
    • Intermediates in the transformation of phosphonates to phosphate by bacteria
    • Kamat, S. S., Williams, H. J. & Raushel, F. M. Intermediates in the transformation of phosphonates to phosphate by bacteria. Nature 480, 570-573 (2011). This study is the first to achieve C-P lyase activity in vitro, and the authors propose an enzymatic mechanism for this complex reaction.
    • (2011) Nature , vol.480 , pp. 570-573
    • Kamat, S.S.1    Williams, H.J.2    Raushel, F.M.3
  • 31
    • 84863390146 scopus 로고    scopus 로고
    • Answers to the carbon-phosphorus lyase conundrum
    • Zhang, Q. & van der Donk, W. A. Answers to the carbon-phosphorus lyase conundrum. Chembiochem 13, 627-629 (2012).
    • (2012) Chembiochem , vol.13 , pp. 627-629
    • Zhang, Q.1    Van Der Donk, W.A.2
  • 32
    • 38949184271 scopus 로고    scopus 로고
    • Differential regulation of high-affinity phosphate transport systems of Mycobacterium smegmatis: Identification of PhnF, a repressor of the phnDCE operon
    • DOI 10.1128/JB.01764-07
    • Gebhard, S. & Cook, G. M. Differential regulation of high-affinity phosphate transport systems of Mycobacterium smegmatis: identification of PhnF, a repressor of the phnDCE operon. J. Bacteriol. 190, 1335-1343 (2008). (Pubitemid 351215015)
    • (2008) Journal of Bacteriology , vol.190 , Issue.4 , pp. 1335-1343
    • Gebhard, S.1    Cook, G.M.2
  • 33
    • 79952596401 scopus 로고    scopus 로고
    • Physiological role of phnP-specified phosphoribosyl cyclic phosphodiesterase in catabolism of organophosphonic acids by the carbon-phosphorus lyase pathway
    • Hove-Jensen, B., McSorley, F. R. & Zechel, D. L. Physiological role of phnP-specified phosphoribosyl cyclic phosphodiesterase in catabolism of organophosphonic acids by the carbon-phosphorus lyase pathway. J. Am. Chem. Soc. 133, 3617-3624 (2011).
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 3617-3624
    • Hove-Jensen, B.1    McSorley, F.R.2    Zechel, D.L.3
  • 34
    • 84875038227 scopus 로고    scopus 로고
    • The genes and enzymes of phosphonate metabolism by bacteria, and their distribution in the marine environment
    • Villarreal-Chiu, J. F., Quinn, J. P. & McGrath, J. W. The genes and enzymes of phosphonate metabolism by bacteria, and their distribution in the marine environment. Front. Microbiol. 3, 19 (2012).
    • (2012) Front. Microbiol , vol.3 , pp. 19
    • Villarreal-Chiu, J.F.1    Quinn, J.P.2    McGrath, J.W.3
  • 35
    • 0026285717 scopus 로고
    • Evidence for two distinct phosphonate-degrading enzymes (C-P lyases) in Arthrobacter sp. GLP-1
    • Kertesz, M., Elgorriaga, A. & Amrhein, N. Evidence for two distinct phosphonate-degrading enzymes (C-P lyases) in Arthrobacter sp. GLP-1. Biodegradation 2, 53-59 (1991).
    • (1991) Biodegradation , vol.2 , pp. 53-59
    • Kertesz, M.1    Elgorriaga, A.2    Amrhein, N.3
  • 36
    • 84856286561 scopus 로고    scopus 로고
    • Distribution of glyphosate and methylphosphonate catabolism systems in soil bacteria Ochrobactrum anthropi and Achromobacter sp
    • Sviridov, A. V. et al. Distribution of glyphosate and methylphosphonate catabolism systems in soil bacteria Ochrobactrum anthropi and Achromobacter sp. Appl. Microbiol. Biotechnol. 93, 787-796 (2012).
    • (2012) Appl. Microbiol. Biotechnol , vol.93 , pp. 787-796
    • Sviridov, A.V.1
  • 37
    • 30144433545 scopus 로고    scopus 로고
    • Phosphonate utilization by the globally important marine diazotroph Trichodesmium
    • DOI 10.1038/nature04203
    • Dyhrman, S. T. et al. Phosphonate utilization by the globally important marine diazotroph Trichodesmium. Nature 439, 68-71 (2006). This report describes the induction of C-P lyase genes in T. erythraeum str. IMS101 under low-phosphate conditions. Expression of these genes might help to explain the prevalence of Trichodesmium spp. in low-phosphate, oligotrophic marine systems. (Pubitemid 43053629)
    • (2006) Nature , vol.439 , Issue.7072 , pp. 68-71
    • Dyhrman, S.T.1    Chappell, P.D.2    Haley, S.T.3    Moffett, J.W.4    Orchard, E.D.5    Waterbury, J.B.6    Webb, E.A.7
  • 38
    • 50149109783 scopus 로고    scopus 로고
    • Aerobic production of methane in the sea
    • Karl, D. M. et al. Aerobic production of methane in the sea. Nature Geosci. 1, 473-478 (2008). This work shows that C-P lyase catalyses the aerobic production of methane from methylphosphonate in phosphate-stressed marine waters, thereby uncovering an additional source of methane efflux from the oceans.
    • (2008) Nature Geosci , vol.1 , pp. 473-478
    • Karl, D.M.1
  • 39
    • 0000467358 scopus 로고
    • Use of hydrous iron(iii) oxide in a concentration step for the determination of trace amounts of organophosphorus compounds in aqueous-solutions
    • Hori, T. & Sugiyama, M. Use of hydrous iron(iii) oxide in a concentration step for the determination of trace amounts of organophosphorus compounds in aqueous-solutions. Analyst 117, 893-897 (1992).
    • (1992) Analyst , vol.117 , pp. 893-897
    • Hori, T.1    Sugiyama, M.2
  • 40
    • 0035132411 scopus 로고    scopus 로고
    • 31P-NMR spectroscopy: Coastal and hydrothermal vent invertebrates
    • DOI 10.1016/S1096-4959(00)00310-9, PII S1096495900003109
    • Quin, L. D. & Quin, G. S. Screening for carbon-bound phosphorus in marine animals by high-resolution P-31-NMR spectroscopy: coastal and hydrothermal vent invertebrates. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 128, 173-185 (2001). (Pubitemid 32157508)
    • (2001) Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology , vol.128 , Issue.1 , pp. 173-185
    • Quin, L.D.1    Quin, G.S.2
  • 41
    • 0032549018 scopus 로고    scopus 로고
    • Isolation and characterization of the carbon-phosphorus bond-forming enzyme phosphoenolpyruvate mutase from the mollusk Mytilus edulis
    • DOI 10.1074/jbc.273.8.4443
    • Kim, A., Kim, J., Martin, B. M. & Dunaway- Mariano, D. Isolation and characterization of the carbon-phosphorus bond-forming enzyme phosphoenolpyruvate mutase from the mollusk Mytilus edulis. J. Biol. Chem. 273, 4443-4448 (1998). (Pubitemid 28103182)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.8 , pp. 4443-4448
    • Kim, A.1    Kim, J.2    Martin, B.M.3    Dunaway-Mariano, D.4
  • 42
    • 49949132369 scopus 로고
    • The breakdown of aminoethylphosphonate by cell-free extracts of Bacillus cereus
    • La Nauze, J. M. & Rosenberg, H. The breakdown of aminoethylphosphonate by cell-free extracts of Bacillus cereus. Biochim. Biophys. Acta 148, 811-813 (1967). This article provides the first description of the microbial degradation of 2-AEP.
    • (1967) Biochim. Biophys. Acta , vol.148 , pp. 811-813
    • La Nauze, J.M.1    Rosenberg, H.2
  • 43
    • 0014681185 scopus 로고
    • Transamination of 2-aminoethylphosphonic acid by Pseudomonas aeruginosa
    • Lacoste, A. M. & Neuzil, E. Transamination of 2-aminoethylphosphonic acid by Pseudomonas aeruginosa. C. R. Acad. Sci. Hebd. Seances Acad. Sci. D 269, 254-257 (1969).
    • (1969) C. R. Acad. Sci. Hebd. Seances Acad. Sci. D , vol.269 , pp. 254-257
    • Lacoste, A.M.1    Neuzil, E.2
  • 44
    • 0017410535 scopus 로고
    • Aldolase like imine formation in the mechanism of action of phosphonoacetaldehyde hydrolase
    • La Nauze, J. M., Coggins, J. R. & Dixon, H. B. Aldolase-like imine formation in the mechanism of action of phosphonoacetaldehyde hydrolase. Biochem. J. 165, 409-411 (1977). (Pubitemid 8154802)
    • (1977) Biochemical Journal , vol.165 , Issue.2 , pp. 409-411
    • La Nauze, J.M.1    Coggins, J.R.2    Dixon, H.B.F.3
  • 45
    • 0024465789 scopus 로고
    • Phosphonoacetaldehyde hydrolase from Pseudomonas aeruginosa: Purification properties and comparison with Bacillus cereus enzyme
    • DOI 10.1016/0167-4838(89)90186-6
    • Dumora, C., Lacoste, A. M. & Cassaigne, A. Phosphonoacetaldehyde hydrolase from Pseudomonas aeruginosa: purification, properties and comparison with Bacillus cereus enzyme. Biochim. Biophys. Acta 997, 193-198 (1989). (Pubitemid 19217037)
    • (1989) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.997 , Issue.3 , pp. 193-198
    • Dumora, C.1    Lacoste, A.-M.2    Cassaigne, A.3
  • 46
    • 0034730072 scopus 로고    scopus 로고
    • The crystal structure of Bacillus cereus phosphonoacetaldehyde hydrolase: Insight into catalysis of phosphorus bond cleavage and catalytic diversification within the had enzyme superfamily
    • DOI 10.1021/bi001171j
    • Morais, M. C. et al. The crystal structure of Bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily. Biochemistry 39, 10385-10396 (2000). (Pubitemid 30655914)
    • (2000) Biochemistry , vol.39 , Issue.34 , pp. 10385-10396
    • Morais, M.C.1    Zhang, W.2    Baker, A.S.3    Zhang, G.4    Dunaway-Mariano, D.5    Allen, K.N.6
  • 47
    • 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
    • DOI 10.1021/bi972677d
    • Baker, A. S. et al. Insights into the mechanism of catalysis by the P-C bond-cleaving enzyme phosphonoacetaldehyde hydrolase derived from gene sequence analysis and mutagenesis. Biochemistry 37, 9305-9315 (1998). (Pubitemid 28307684)
    • (1998) Biochemistry , vol.37 , Issue.26 , 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
  • 48
    • 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. & 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. 177, 6411-6421 (1995).
    • (1995) J. Bacteriol , vol.177 , pp. 6411-6421
    • Jiang, W.H.1    Metcalf, W.W.2    Lee, K.S.3    Wanner, B.L.4
  • 49
    • 0031716877 scopus 로고    scopus 로고
    • Phosphate starvation-independent 2-aminoethylphosphonic acid biodegradation in a newly isolated strain of pseudomonas putida, NG2
    • Ternan, N. G. & Quinn, J. P. Phosphate starvation-independent 2-aminoethylphosphonic acid biodegradation in a newly isolated strain of Pseudomonas putida NG2. Syst. Appl. Microbiol. 21, 346-352 (1998). (Pubitemid 28456838)
    • (1998) Systematic and Applied Microbiology , vol.21 , Issue.3 , pp. 346-352
    • Ternan, N.G.1    Quinn, J.P.2
  • 50
    • 0028791603 scopus 로고
    • The purification and properties of phosphonoacetate hydrolase, a novel carbon-phosphorus bond-cleaving enzyme from Pseudomonas fluorescens 23F Eur
    • McGrath, J. W., Wisdom, G. B., McMullan, G., Larkin, M. J. & Quinn, J. P. The purification and properties of phosphonoacetate hydrolase, a novel carbon-phosphorus bond-cleaving enzyme from Pseudomonas fluorescens 23F Eur. J. Biochem. 234, 225-230 (1995).
    • (1995) 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
  • 51
    • 79955411030 scopus 로고    scopus 로고
    • Divergence of chemical function in the alkaline phosphatase superfamily: Structure and mechanism of the P-C bond cleaving enzyme phosphonoacetate hydrolase
    • Kim, A. et al. Divergence of chemical function in the alkaline phosphatase superfamily: structure and mechanism of the P-C bond cleaving enzyme phosphonoacetate hydrolase. Biochemistry 50, 3481-3494 (2011).
    • (2011) Biochemistry , vol.50 , pp. 3481-3494
    • Kim, A.1
  • 52
    • 80055084842 scopus 로고    scopus 로고
    • Structural and mechanistic insights into C-P bond hydrolysis by phosphonoacetate hydrolase
    • Agarwal, V., Borisova, S. A., Metcalf, W. W., van der Donk, W. A. & Nair, S. K. Structural and mechanistic insights into C-P bond hydrolysis by phosphonoacetate hydrolase. Chem. Biol. 18, 1230-1240 (2011).
    • (2011) Chem. Biol , vol.18 , pp. 1230-1240
    • Agarwal, V.1    Borisova, S.A.2    Metcalf, W.W.3    Van Der Donk, W.A.4    Nair, S.K.5
  • 53
    • 0026684624 scopus 로고
    • Detection of a novel carbon-phosphorus bond-cleavage activity in cell-free-extracts of an environmental Pseudomonas fluorescens isolate
    • McMullan, G. & Quinn, J. P. Detection of a novel carbon-phosphorus bond-cleavage activity in cell-free-extracts of an environmental Pseudomonas fluorescens isolate. Biochem. Biophys. Res. Commun. 184, 1022-1027 (1992).
    • (1992) Biochem. Biophys. Res. Commun , vol.184 , pp. 1022-1027
    • McMullan, G.1    Quinn, J.P.2
  • 54
    • 0026554431 scopus 로고
    • Metabolism of phosphonoacetate as the sole carbon and phosphorus source by an environmental bacterial isolate
    • McMullan, G., Harrington, F. & Quinn, J. P. Metabolism of phosphonoacetate as the sole carbon and phosphorus source by an environmental bacterial isolate. Appl. Environ. Microbiol. 58, 1364-1366 (1992).
    • (1992) Appl. Environ. Microbiol , vol.58 , pp. 1364-1366
    • McMullan, G.1    Harrington, F.2    Quinn, J.P.3
  • 55
    • 77953596410 scopus 로고    scopus 로고
    • The construction of a whole-cell biosensor for phosphonoacetate, based on the LysR-like transcriptional regulator PhnR from Pseudomonas fluorescens 23F
    • Kulakova, A. N., Kulakov, L. A., McGrath, J. W. & Quinn, J. P. The construction of a whole-cell biosensor for phosphonoacetate, based on the LysR-like transcriptional regulator PhnR from Pseudomonas fluorescens 23F. Microb. Biotechnol. 2, 234-240 (2009).
    • (2009) Microb. Biotechnol , vol.2 , pp. 234-240
    • Kulakova, A.N.1    Kulakov, L.A.2    McGrath, J.W.3    Quinn, J.P.4
  • 57
    • 79959360686 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of a pathway for the degradation of 2-aminoethylphosphonate in Sinorhizobium meliloti 1021
    • Borisova, S. A. et al. Genetic and biochemical characterization of a pathway for the degradation of 2-aminoethylphosphonate in Sinorhizobium meliloti 1021. J. Biol. Chem. 286, 22283-22290 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 22283-22290
    • Borisova, S.A.1
  • 58
    • 79958280148 scopus 로고    scopus 로고
    • Phosphonoacetate biosynthesis: In vitro detection of a novel NADP+ dependent phosphonoacetaldehyde oxidizing activity in cell extracts of a marine Roseobacter
    • Cooley, N. A. et al. Phosphonoacetate biosynthesis: in vitro detection of a novel NADP+ dependent phosphonoacetaldehyde oxidizing activity in cell extracts of a marine Roseobacter. Microbiology 80, 335-340 (2011).
    • (2011) Microbiology , vol.80 , pp. 335-340
    • Cooley, N.A.1
  • 59
    • 73349117182 scopus 로고    scopus 로고
    • Widespread known and novel phosphonate utilization pathways in marine bacteria revealed by functional screening and metagenomic analyses
    • Martinez, A., Tyson, G. W. & DeLong, E. F. Widespread known and novel phosphonate utilization pathways in marine bacteria revealed by functional screening and metagenomic analyses. Environ. Microbiol. 12, 222-238 (2010).
    • (2010) Environ. Microbiol , vol.12 , pp. 222-238
    • Martinez, A.1    Tyson, G.W.2    Delong, E.F.3
  • 60
    • 84861395902 scopus 로고    scopus 로고
    • PhnY and PhnZ comprise a new oxidative pathway for enzymatic cleavage of a carbon- phosphorus bond
    • McSorley, F. R. et al. PhnY and PhnZ comprise a new oxidative pathway for enzymatic cleavage of a carbon- phosphorus bond. J. Am. Chem. Soc. 134, 8364-8367 (2012).
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 8364-8367
    • McSorley, F.R.1
  • 61
    • 13844253483 scopus 로고    scopus 로고
    • Phosphonate catabolism by Campylobacter spp
    • Mendz, G. L., Megraud, F. & Korolik, V. Phosphonate catabolism by Campylobacter spp. Arch. Microbiol. 183, 113-120 (2005).
    • (2005) Arch. Microbiol , vol.183 , pp. 113-120
    • Mendz, G.L.1    Megraud, F.2    Korolik, V.3
  • 63
    • 78650625847 scopus 로고    scopus 로고
    • Alternative pathways for phosphonate metabolism in thermophilic cyanobacteria from microbial mats
    • Gomez-Garcia, M. R., Davison, M., Blain-Hartnung, M., Grossman, A. R. & Bhaya, D. Alternative pathways for phosphonate metabolism in thermophilic cyanobacteria from microbial mats. ISME J. 5, 141-149 (2011).
    • (2011) ISME J , vol.5 , pp. 141-149
    • Gomez-Garcia, M.R.1    Davison, M.2    Blain-Hartnung, M.3    Grossman, A.R.4    Bhaya, D.5
  • 64
    • 0019331352 scopus 로고
    • Metabolism of 2-amino-3-phosphono[3-14C]propionic acid in cell-free preparations of Tetrahymena
    • Horigane, A., Horiguchi, M. & Matsumoto, T. Metabolism of 2-amino-3-phosphono[3-14C]propionic acid in cell-free preparations of Tetrahymena. Biochim. Biophys. Acta 618, 383-388 (1980).
    • (1980) Biochim. Biophys. Acta , vol.618 , pp. 383-388
    • Horigane, A.1    Horiguchi, M.2    Matsumoto, T.3
  • 65
    • 0031746836 scopus 로고    scopus 로고
    • Phosphoenolpyruvate phosphomutase activity in an L-phosphonoalanine- mineralizing strain of Burkholderia cepacia
    • Ternan, N. G., McGrath, J. W. & Quinn, J. P. Phosphoenolpyruvate phosphomutase activity in an l-phosphonoalanine-mineralizing strain of Burkholderia cepacia. Appl. Environ. Microbiol. 64, 2291-2294 (1998). (Pubitemid 28252804)
    • (1998) Applied and Environmental Microbiology , vol.64 , Issue.6 , pp. 2291-2294
    • Ternan, N.G.1    McGrath, J.W.2    Quinn, J.P.3
  • 66
    • 59349117794 scopus 로고    scopus 로고
    • Expression of the phosphonoalanine-degradative gene cluster from Variovorax sp. Pal2 is induced by growth on phosphonoalanine and phosphonopyruvate
    • Kulakova, A. N. et al. Expression of the phosphonoalanine-degradative gene cluster from Variovorax sp. Pal2 is induced by growth on phosphonoalanine and phosphonopyruvate. FEMS Microbiol. Lett. 292, 100-106 (2009).
    • (2009) FEMS Microbiol. Lett , vol.292 , pp. 100-106
    • Kulakova, A.N.1
  • 67
    • 0037931360 scopus 로고    scopus 로고
    • The purification and characterization of phosphonopyruvate hydrolase, a novel carbon-phosphorus bond cleavage enzyme from Variovorax sp. Pal2
    • DOI 10.1074/jbc.M301871200
    • Kulakova, A. N., Wisdom, G. B., Kulakov, L. A. & Quinn, J. P. The purification and characterization of phosphonopyruvate hydrolase, a novel carbon-phosphorus bond cleavage enzyme from Variovorax sp. Pal2. J. Biol. Chem. 278, 23426-23431 (2003). (Pubitemid 36830159)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.26 , pp. 23426-23431
    • Kulakova, A.N.1    Wisdom, G.B.2    Kulakov, L.A.3    Quinn, J.P.4
  • 68
    • 33749010624 scopus 로고    scopus 로고
    • Structure and kinetics of phosphonopyruvate hydrolase from Voriovorax sp. Pal2: New insight into the divergence of catalysis within the pep mutase/isocitrate lyase superfamily
    • DOI 10.1021/bi061208l
    • Chen, C. C. H. et al. Structure and kinetics of phosphonopyruvate hydrolase from Variovorax sp. Pal2: new insight into the divergence of catalysis within the PEP mutase/isocitrate lyase superfamily. Biochemistry 45, 11491-11504 (2006). (Pubitemid 44453997)
    • (2006) Biochemistry , vol.45 , Issue.38 , pp. 11491-11504
    • Chen, C.C.H.1    Han, Y.2    Niu, W.3    Kulakova, A.N.4    Howard, A.5    Quinn, J.P.6    Dunaway-Mariano, D.7    Herzberg, O.8
  • 70
    • 64549104585 scopus 로고    scopus 로고
    • Studies on the biodegradation of fosfomycin: Growth of Rhizobium huakuii PMY1 on possible intermediates synthesised chemically
    • McGrath, J. W., Hammerschmidt, F., Preusser, W., Quinn, J. P. & Schweifer, A. Studies on the biodegradation of fosfomycin: growth of Rhizobium huakuii PMY1 on possible intermediates synthesised chemically. Org. Biomol. Chem. 7, 1944-1953 (2009).
    • (2009) Org. Biomol. Chem , vol.7 , pp. 1944-1953
    • McGrath, J.W.1    Hammerschmidt, F.2    Preusser, W.3    Quinn, J.P.4    Schweifer, A.5
  • 71
    • 81255173261 scopus 로고    scopus 로고
    • Studies on the biodegradation of fosfomycin: Synthesis of 13C-labeled intermediates, feeding experiments with Rhizobium huakuii PMY1, and isolation of labeled amino acids from cell mass by HPLC
    • McGrath, J. W. et al. Studies on the biodegradation of fosfomycin: synthesis of 13C-labeled intermediates, feeding experiments with Rhizobium huakuii PMY1, and isolation of labeled amino acids from cell mass by HPLC. Chemistry 17, 13341-13348 (2011).
    • (2011) Chemistry , vol.17 , pp. 13341-13348
    • McGrath, J.W.1
  • 72
    • 33847706072 scopus 로고    scopus 로고
    • The oceanic phosphorus cycle
    • DOI 10.1021/cr0503613
    • Paytan, A. & McLaughlin, K. The oceanic phosphorus cycle. Chem. Rev. 107, 563-576 (2007). (Pubitemid 46381033)
    • (2007) Chemical Reviews , vol.107 , Issue.2 , pp. 563-576
    • Paytan, A.1    McLaughlin, K.2
  • 74
    • 0035073170 scopus 로고    scopus 로고
    • Composition and cycling of marine organic phosphorus
    • Kolowith, L. C., Ingall, E. D. & Benner, R. Composition and cycling of marine organic phosphorus. Limnol. Oceanogr. 46, 309-320 (2001). (Pubitemid 32281607)
    • (2001) Limnology and Oceanography , vol.46 , Issue.2 , pp. 309-320
    • Kolowith, L.C.1    Ingall, E.D.2    Benner, R.3
  • 75
    • 84868369211 scopus 로고    scopus 로고
    • Streamlining and core genome conservation among highly divergent members of the SAR11 clade
    • Grote, J. et al. Streamlining and core genome conservation among highly divergent members of the SAR11 clade. mBio 3, e00252-12 (2012).
    • (2012) MBio , vol.3 , pp. 00252-312
    • Grote, J.1
  • 76
    • 18544407281 scopus 로고    scopus 로고
    • Bioavailability of dissolved organic phosphorus in the euphotic zone at Station ALOHA, North Pacific Subtropical Gyre
    • Bjorkman, K. M. & Karl, D. M. Bioavailability of dissolved organic phosphorus in the euphotic zone at station ALOHA, North Pacific Subtropical Gyre. Limnol. Oceanogr. 48, 1049-1057 (2003). (Pubitemid 36631946)
    • (2003) Limnology and Oceanography , vol.48 , Issue.3 , pp. 1049-1057
    • Bjorkman, K.M.1    Karl, D.M.2
  • 77
    • 78651355676 scopus 로고    scopus 로고
    • Depth distributions of alkaline phosphatase and phosphonate utilization genes in the North Pacific Subtropical Gyre
    • Luo, H. W., Zhang, H. M., Long, R. A. & Benner, R. Depth distributions of alkaline phosphatase and phosphonate utilization genes in the North Pacific Subtropical Gyre. Aquat. Microb. Ecol. 62, 61-69 (2011).
    • (2011) Aquat. Microb. Ecol , vol.62 , pp. 61-69
    • Luo, H.W.1    Zhang, H.M.2    Long, R.A.3    Benner, R.4
  • 78
    • 75849143326 scopus 로고    scopus 로고
    • Subcellular localization of marine bacterial alkaline phosphatases
    • Luo, H., Benner, R., Long, R. A. & Hu, J. Subcellular localization of marine bacterial alkaline phosphatases. Proc. Natl Acad. Sci. USA 106, 21219-21223 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 21219-21223
    • Luo, H.1    Benner, R.2    Long, R.A.3    Hu, J.4
  • 79
    • 0032482346 scopus 로고    scopus 로고
    • Marine phosphorus is selectively remineralized
    • Clark, L. L., Ingall, E. D. & Benner, R. Marine phosphorus is selectively remineralized. Nature 393, 426-426 (1998).
    • (1998) Nature , vol.393 , pp. 426-426
    • Clark, L.L.1    Ingall, E.D.2    Benner, R.3
  • 81
    • 65349154502 scopus 로고    scopus 로고
    • Detection and expression of the phosphonate transporter gene phnD in marine and freshwater picocyanobacteria
    • Ilikchyan, I. N., McKay, R. M. L., Zehr, J. P., Dyhrman, S. T. & Bullerjahn, G. S. Detection and expression of the phosphonate transporter gene phnD in marine and freshwater picocyanobacteria. Environ. Microbiol. 11, 1314-1324 (2009).
    • (2009) Environ. Microbiol , vol.11 , pp. 1314-1324
    • Ilikchyan, I.N.1    McKay, R.M.L.2    Zehr, J.P.3    Dyhrman, S.T.4    Bullerjahn, G.S.5
  • 82
    • 58149240855 scopus 로고    scopus 로고
    • Potential for phosphonoacetate utilization by marine bacteria in temperate coastal waters
    • Gilbert, J. A. et al. Potential for phosphonoacetate utilization by marine bacteria in temperate coastal waters. Environ. Microbiol. 11, 111-125 (2009).
    • (2009) Environ. Microbiol , vol.11 , pp. 111-125
    • Gilbert, J.A.1
  • 83
    • 77149122718 scopus 로고    scopus 로고
    • Evidence for phosphonate usage in the coral holobiont
    • Thomas, S. et al. Evidence for phosphonate usage in the coral holobiont. ISME J. 4, 459-461 (2010).
    • (2010) ISME J , vol.4 , pp. 459-461
    • Thomas, S.1
  • 84
    • 84865535718 scopus 로고    scopus 로고
    • Synthesis of methylphosphonic acid by marine microbes: A source for methane in the aerobic ocean
    • Metcalf, W. W. et al. Synthesis of methylphosphonic acid by marine microbes: a source for methane in the aerobic ocean. Science 337, 1104-1107 (2012). This paper provides evidence for the production of methylphosphonate by the marine archaeon N. maritimus, a finding that might help to further resolve the oceanic methane paradox.
    • (2012) Science , vol.337 , pp. 1104-1107
    • Metcalf, W.W.1
  • 85
    • 0038739203 scopus 로고    scopus 로고
    • Environmental chemistry of phosphonates
    • DOI 10.1016/S0043-1354(03)00079-4
    • Nowack, B. Environmental chemistry of phosphonates. Water Res. 37, 2533-2546 (2003). (Pubitemid 36561459)
    • (2003) Water Research , vol.37 , Issue.11 , pp. 2533-2546
    • Nowack, B.1
  • 87
    • 0019473828 scopus 로고
    • Phosphonates as analogs of biological phosphates
    • Blackburn, G. M. Phosphonates as analogs of biological phosphates. Chem. Ind. 7, 134-138 (1981).
    • (1981) Chem. Ind , vol.7 , pp. 134-138
    • Blackburn, G.M.1
  • 88
    • 41349085389 scopus 로고    scopus 로고
    • Glyphosate: A once-in-a-century herbicide
    • DOI 10.1002/ps.1518
    • Duke, S. O. & Powles, S. B. Glyphosate: a once-in-a-century herbicide. Pest Manage. Sci. 64, 319-325 (2008). (Pubitemid 351449451)
    • (2008) Pest Management Science , vol.64 , Issue.4 , pp. 319-325
    • Duke, S.O.1    Powles, S.B.2


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