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Volumn 78, Issue 1, 2014, Pages 176-197

Utilization of glyphosate as phosphate source: Biochemistry and genetics of bacterial carbon-phosphorus lyase

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; CARBON; GLYPHOSATE; LYASE; METHYLPHOSPHONIC ACID; NEBULARINE; NUCLEOTIDE BINDING PROTEIN; PHOSPHATE; PHOSPHORUS; REGULATOR PROTEIN;

EID: 84896303396     PISSN: 10922172     EISSN: 10985557     Source Type: Journal    
DOI: 10.1128/MMBR.00040-13     Document Type: Review
Times cited : (171)

References (142)
  • 1
    • 58449097846 scopus 로고    scopus 로고
    • Role of translocation as a mechanism of resistance to glyphosate
    • Shaner DL. 2009. Role of translocation as a mechanism of resistance to glyphosate. Weed Sci. 57:118-123. http://dx.doi.org/10.1614/WS-08-050.1.
    • (2009) Weed Sci. , vol.57 , pp. 118-123
    • Shaner, D.L.1
  • 2
    • 79961026819 scopus 로고    scopus 로고
    • Molecular basis of glyphosate resistance - Different approaches through protein engineering
    • Pollegioni L, Schonbrunn E, Siehl D. 2011. Molecular basis of glyphosate resistance - different approaches through protein engineering. FEBS J. 278:2753-2766. http://dx.doi.org/10.1111/j.1742-4658.2011.08214.x.
    • (2011) FEBS J. , vol.278 , pp. 2753-2766
    • Pollegioni, L.1    Schonbrunn, E.2    Siehl, D.3
  • 5
    • 0022395408 scopus 로고
    • Expression in plants of a mutant aroA gene from Salmonella typhimurium confers tolerance to glyphosate
    • Comai L, Facciotti D, Hiatt WR, Thompson G, Rose RE, Stalker DM. 1985. Expression in plants of a mutant aroA gene from Salmonella typhimurium confers tolerance to glyphosate. Nature 317:441-444.
    • (1985) Nature , vol.317 , pp. 441-444
    • Comai, L.1    Facciotti, D.2    Hiatt, W.R.3    Thompson, G.4    Rose, R.E.5    Stalker, D.M.6
  • 7
    • 0001492818 scopus 로고
    • Growth of Escherichia coli on methyl- and ethylphosphonic acids
    • Zeleznick LD, Myers TC, Titchener EB. 1963. Growth of Escherichia coli on methyl- and ethylphosphonic acids. Biochim. Biophys. Acta 78:546-547. http://dx.doi.org/10.1016/0006-3002(63)90921-1.
    • (1963) Biochim. Biophys. Acta , vol.78 , pp. 546-547
    • Zeleznick, L.D.1    Myers, T.C.2    Titchener, E.B.3
  • 8
    • 0000829177 scopus 로고
    • Fragmentative and stereochemical isomerization probes for homolytic carbon to phosphorus bond scission catalyzed by bacterial carbon-phosphorus lyase
    • Shames SL, Wackett LP, LaBarge MS, Kuczkowski RL, Walsh CT. 1987. Fragmentative and stereochemical isomerization probes for homolytic carbon to phosphorus bond scission catalyzed by bacterial carbon-phosphorus lyase. Bioorg. Chem. 15:366-373. http://dx.doi.org/10.1016/0045-2068(87)90033-2.
    • (1987) Bioorg. Chem. , vol.15 , pp. 366-373
    • Shames, S.L.1    Wackett, L.P.2    LaBarge, M.S.3    Kuczkowski, R.L.4    Walsh, C.T.5
  • 9
    • 23244445190 scopus 로고    scopus 로고
    • Cloning, expression and crystallization of heterotetrameric sarcosine oxidase from Pseudomonas maltophilia
    • DOI 10.1016/j.pep.2005.03.023, PII S1046592805001038
    • Hassan-Abdallah A, Zhao G, Eschenbrenner M, Chen ZW, Mathews FS, Jorns MS. 2005. Cloning, expression and crystallization of heterotetrameric sarcosine oxidase from Pseudomonas maltophilia. Protein Expr. Purif. 43:33-43. http://dx.doi.org/10.1016/j.pep.2005.03.023. (Pubitemid 41097382)
    • (2005) Protein Expression and Purification , vol.43 , Issue.1 , pp. 33-43
    • Hassan-Abdallah, A.1    Zhao, G.2    Eschenbrenner, M.3    Chen, Z.-W.4    Mathews, F.S.5    Jorns, M.S.6
  • 10
    • 0034832015 scopus 로고    scopus 로고
    • Organization of the genes involved in dimethylglycine and sarcosine degradation in Arthrobacter spp.: Implications for glycine betaine catabolism
    • DOI 10.1046/j.1432-1327.2001.02239.x
    • Meskys R, Harris RJ, Casaite V, Basran J, Scrutton NS. 2001. Organization of the genes involved in dimethylglycine and sarcosine degradation in Arthrobacter spp.: implications for glycine betaine catabolism. Eur. J. Biochem. 268:3390-3398. http://dx.doi.org/10.1046/j.1432-1327.2001.02239.x. (Pubitemid 32862931)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.12 , pp. 3390-3398
    • Meskys, R.1    Harris, R.J.2    Casaite, V.3    Basran, J.4    Scrutton, N.S.5
  • 11
    • 0346365141 scopus 로고    scopus 로고
    • Glyphosate tolerant plants
    • July US patent 5776760
    • Barry GF, Kishore GM. July 1998. Glyphosate tolerant plants. US patent 5776760.
    • (1998)
    • Barry, G.F.1    Kishore, G.M.2
  • 12
    • 0030878441 scopus 로고    scopus 로고
    • Nuclear magnetic resonance timecourse studies of glyphosate metabolism by microbial soil isolates
    • DOI 10.1080/004982597240235
    • Gard JK, Feng PC, Hutton WC. 1997. Nuclear magnetic resonance timecourse studies of glyphosate metabolism by microbial soil isolates. Xenobiotica 27:633-644. http://dx.doi.org/10.1080/004982597240235. (Pubitemid 27301400)
    • (1997) Xenobiotica , vol.27 , Issue.7 , pp. 633-644
    • Gard, J.K.1    Feng, P.C.C.2    Hutton, W.C.3
  • 14
    • 84863445823 scopus 로고    scopus 로고
    • Bacterial glyphosate resistance conferred by overexpression of an E. coli membrane efflux transporter
    • Staub JM, Brand L, Tran M, Kong Y, Rogers SG. 2012. Bacterial glyphosate resistance conferred by overexpression of an E. coli membrane efflux transporter. J. Ind. Microbiol. Biotechnol. 39:641-647. http://dx.doi.org/10. 1007/s10295-011-1057-x.
    • (2012) J. Ind. Microbiol. Biotechnol. , vol.39 , pp. 641-647
    • Staub, J.M.1    Brand, L.2    Tran, M.3    Kong, Y.4    Rogers, S.G.5
  • 15
    • 84865512261 scopus 로고    scopus 로고
    • Identification and analysis of the putative pentose sugar efflux transporters in Escherichia coli
    • Koita K, Rao CV. 2012. Identification and analysis of the putative pentose sugar efflux transporters in Escherichia coli. PLoS One 7:e43700. http://dx.doi.org/10.1371/journal.pone.0043700.
    • (2012) PLoS One , vol.7
    • Koita, K.1    Rao, C.V.2
  • 16
    • 84655166556 scopus 로고    scopus 로고
    • Limited uptake, translocation and enhanced metabolic degradation contribute to glyphosate tolerance in Mucuna pruriens var. Utilis plants
    • Rojano-Delgado AM, Cruz-Hipolito H, De Prado R, Luque de Castro MD, Franco AR. 2012. Limited uptake, translocation and enhanced metabolic degradation contribute to glyphosate tolerance in Mucuna pruriens var. utilis plants. Phytochemistry 73:34-41. http://dx.doi.org/10.1016/j.phytochem.2011.09. 007.
    • (2012) Phytochemistry , vol.73 , pp. 34-41
    • Rojano-Delgado, A.M.1    Cruz-Hipolito, H.2    De Prado, R.3    Luque De Castro, M.D.4    Franco, A.R.5
  • 17
    • 84866866076 scopus 로고    scopus 로고
    • Glyphosate in northern ecosystems
    • Helander M, Saloniemi I, Saikkonen K. 2012. Glyphosate in northern ecosystems. Trends Plant Sci. 17:569-574. http://dx.doi.org/10.1016/j.tplants. 2012.05.008.
    • (2012) Trends Plant Sci. , vol.17 , pp. 569-574
    • Helander, M.1    Saloniemi, I.2    Saikkonen, K.3
  • 18
    • 41349123085 scopus 로고    scopus 로고
    • Fate of glyphosate in soil and the possibility of leaching to ground and surface waters: A review
    • DOI 10.1002/ps.1512
    • Borggaard OK, Gimsing AL. 2008. Fate of glyphosate in soil and the possibility of leaching to ground and surface waters: a review. Pest Manag. Sci. 64:441-456. http://dx.doi.org/10.1002/ps.1512. (Pubitemid 351449468)
    • (2008) Pest Management Science , vol.64 , Issue.4 , pp. 441-456
    • Borggaard, O.K.1    Gimsing, A.L.2
  • 20
    • 0024044036 scopus 로고
    • Phosphate starvation induces uptake of glyphosate by Pseudomonas sp. strain PG2982
    • Fitzgibbon J, Braymer HD. 1988. Phosphate starvation induces uptake of glyphosate by Pseudomonas sp. strain PG2982. Appl. Environ. Microbiol. 54:1886-1888.
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 1886-1888
    • Fitzgibbon, J.1    Braymer, H.D.2
  • 22
    • 33745712494 scopus 로고    scopus 로고
    • Identification of cognate ligands for the Escherichia coli phnD protein product and engineering of a reagentless fluorescent biosensor for phosphonates
    • Rizk SS, Cuneo MJ, Hellinga HW. 2006. Identification of cognate ligands for the Escherichia coli phnD protein product and engineering of a reagentless fluorescent biosensor for phosphonates. Protein Sci. 15:1745-1751. http://dx.doi.org/10.1110/ps.062135206.
    • (2006) Protein Sci. , vol.15 , pp. 1745-1751
    • Rizk, S.S.1    Cuneo, M.J.2    Hellinga, H.W.3
  • 23
    • 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 CM, Ye QZ, Zhu ZM, Wanner BL, Walsh CT. 1990. 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) 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
  • 24
    • 0025730336 scopus 로고
    • Molecular analysis of the cryptic and functional phn operons for phosphonate use in Escherichia coli K-12
    • Makino K, Kim SK, Shinagawa H, Amemura M, Nakata A. 1991. Molecular analysis of the cryptic and functional phn operons for phosphonate use in Escherichia coli K-12. J. Bacteriol. 173:2665-2672.
    • (1991) J. Bacteriol. , vol.173 , pp. 2665-2672
    • Makino, K.1    Kim, S.K.2    Shinagawa, H.3    Amemura, M.4    Nakata, A.5
  • 25
    • 4444325284 scopus 로고    scopus 로고
    • Reversible phase variation in the phnE gene, which is required for phosphonate metabolism in Escherichia coli K-12
    • DOI 10.1128/JB.186.18.6118-6123.2004
    • Iqbal S, Parker G, Davidson H, Moslehi-Rahmani E, Robson RL. 2004. Reversible phase variation in the phnE gene, which is required for phosphonate metabolism in Escherichia coli K-12. J. Bacteriol. 186:6118-6123. http://dx.doi.org/10.1128/JB.186.18.6118-6123.2004. (Pubitemid 39187000)
    • (2004) Journal of Bacteriology , vol.186 , Issue.18 , pp. 6118-6123
    • Iqbal, S.1    Parker, G.2    Davidson, H.3    Moslehi-Rahmani, E.4    Robson, R.L.5
  • 26
    • 84855904410 scopus 로고    scopus 로고
    • Activation of the cryptic PhnE permease promotes rapid adaptive evolution in a population of Escherichia coli K-12 starved for phosphate
    • Guillemet ML, Moreau PL. 2012. Activation of the cryptic PhnE permease promotes rapid adaptive evolution in a population of Escherichia coli K-12 starved for phosphate. J. Bacteriol. 194:253-260. http://dx.doi.org/10.1128/JB. 06094-11.
    • (2012) J. Bacteriol. , vol.194 , pp. 253-260
    • Guillemet, M.L.1    Moreau, P.L.2
  • 27
    • 0037926376 scopus 로고
    • Biosynthesis of serine in Escherichia coli and Salmonella typhimurium
    • Umbarger HE, Umbarger MA, Siu PM. 1963. Biosynthesis of serine in Escherichia coli and Salmonella typhimurium. J. Bacteriol. 85:1431-1439.
    • (1963) J. Bacteriol. , vol.85 , pp. 1431-1439
    • Umbarger, H.E.1    Umbarger, M.A.2    Siu, P.M.3
  • 28
    • 0027121349 scopus 로고
    • Molecular genetic studies of a 10.9-kb operon in Escherichia coli for phosphonate uptake and biodegradation
    • Wanner BL, Metcalf WW. 1992. Molecular genetic studies of a 10.9-kb operon in Escherichia coli for phosphonate uptake and biodegradation. FEMS Microbiol. Lett. 79:133-139. (Pubitemid 23008513)
    • (1992) FEMS Microbiology Letters , vol.100 , Issue.1-3 , pp. 133-139
    • Wanner, B.L.1    Metcalf, W.W.2
  • 29
    • 0027262172 scopus 로고
    • Mutational analysis of an Escherichia coli fourteen-gene operon for phosphonate degradation, using TnphoA' elements
    • Metcalf WW, Wanner BL. 1993. Mutational analysis of an Escherichia coli fourteen-gene operon for phosphonate degradation, using TnphoA′ elements. J. Bacteriol. 175:3430-3442. (Pubitemid 23163387)
    • (1993) Journal of Bacteriology , vol.175 , Issue.11 , pp. 3430-3442
    • Metcalf, W.W.1    Wanner, B.L.2
  • 30
    • 3042815976 scopus 로고    scopus 로고
    • Two C-P lyase operons in Pseudomonas stutzeri and their roles in the oxidation of phosphonates, phosphite, and hypophosphite
    • DOI 10.1128/JB.186.14.4730-4739.2004
    • White AK, Metcalf WW. 2004. Two C-P lyase operons in Pseudomonas stutzeri and their roles in the oxidation of phosphonates, phosphite, and hypophosphite. J. Bacteriol. 186:4730-4739. http://dx.doi.org/10.1128/JB.186.14.4730-4739. 2004. (Pubitemid 38891035)
    • (2004) Journal of Bacteriology , vol.186 , Issue.14 , pp. 4730-4739
    • White, A.K.1    Metcalf, W.W.2
  • 31
    • 84875038227 scopus 로고    scopus 로고
    • The genes and enzymes of phosphonate metabolism by bacteria, and their distribution in the marine environment
    • Villarreal-Chiu JF, Quinn JP, McGrath JW. 2012. The genes and enzymes of phosphonate metabolism by bacteria, and their distribution in the marine environment. Front. Microbiol. 3:19. http://dx.doi.org/10.3389/fmicb.2012.00019.
    • (2012) Front. Microbiol. , vol.3 , pp. 19
    • Villarreal-Chiu, J.F.1    Quinn, J.P.2    McGrath, J.W.3
  • 34
    • 0026285717 scopus 로고
    • Evidence for two distinct phosphonate-degrading enzymes (C-P lyases) in Arhtrobacter sp. GLP-1
    • Kertesz M, Elgorriga A, Amrhein N. 1991. Evidence for two distinct phosphonate-degrading enzymes (C-P lyases) in Arhtrobacter sp. GLP-1. Biodegradation 2:53-59. http://dx.doi.org/10.1007/BF00122425.
    • (1991) Biodegradation , vol.2 , pp. 53-59
    • Kertesz, M.1    Elgorriga, A.2    Amrhein, N.3
  • 38
    • 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 GM. 2008. 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. http://dx.doi.org/10.1128/JB.01764-07. (Pubitemid 351215015)
    • (2008) Journal of Bacteriology , vol.190 , Issue.4 , pp. 1335-1343
    • Gebhard, S.1    Cook, G.M.2
  • 39
    • 84867068020 scopus 로고    scopus 로고
    • Catabolism and detoxification of 1-aminoalkylphosphonic acids: N-acetylation by the phnO gene product
    • Hove-Jensen B, McSorley FR, Zechel DL. 2012. Catabolism and detoxification of 1-aminoalkylphosphonic acids: N-acetylation by the phnO gene product. PLoS One 7:e46416. http://dx.doi.org/10.1371/journal.pone.0046416.
    • (2012) PLoS One , vol.7
    • Hove-Jensen, B.1    McSorley, F.R.2    Zechel, D.L.3
  • 40
    • 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, Lolle S, McSorley FR, Nabi M, Stougaard J, Zechel DL, Hove-Jensen B. 2011. Five phosphonate operon gene products as components of a multi-subunit complex of the carbon-phosphorus lyase pathway. Proc. Natl. Acad. Sci. U. S. A. 108:11393-11398. http://dx.doi.org/10.1073/pnas.1104922108.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 11393-11398
    • Jochimsen, B.1    Lolle, S.2    McSorley, F.R.3    Nabi, M.4    Stougaard, J.5    Zechel, D.L.6    Hove-Jensen, B.7
  • 41
    • 84355162021 scopus 로고    scopus 로고
    • Intermediates in the transformation of phosphonates to phosphate by bacteria
    • Kamat SS, Williams HJ, Raushel FM. 2011. Intermediates in the transformation of phosphonates to phosphate by bacteria. Nature 480:570-573. http://dx.doi.org/10.1038/nature10622.
    • (2011) Nature , vol.480 , pp. 570-573
    • Kamat, S.S.1    Williams, H.J.2    Raushel, F.M.3
  • 42
    • 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 FR, Zechel DL. 2011. 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. http://dx.doi.org/10.1021/ja1102713.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 3617-3624
    • Hove-Jensen, B.1    McSorley, F.R.2    Zechel, D.L.3
  • 43
    • 84877584386 scopus 로고    scopus 로고
    • The catalytic mechanism for aerobic formation of methane by bacteria
    • Kamat SS, Williams HJ, Dangott LJ, Chakrabarti M, Raushel FM. 2013. The catalytic mechanism for aerobic formation of methane by bacteria. Nature 497:132-136. http://dx.doi.org/10.1038/nature12061.
    • (2013) Nature , vol.497 , pp. 132-136
    • Kamat, S.S.1    Williams, H.J.2    Dangott, L.J.3    Chakrabarti, M.4    Raushel, F.M.5
  • 44
    • 0008036668 scopus 로고
    • Monomeric metaphosphate formation during radical-based dephosphorylation
    • Avila LZ, Frost JW. 1988. Monomeric metaphosphate formation during radical-based dephosphorylation. J. Am. Chem. Soc. 110:7904-7906. http://dx.doi.org/10.1021/ja00231a067.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 7904-7906
    • Avila, L.Z.1    Frost, J.W.2
  • 45
    • 0001513561 scopus 로고
    • Degradation and detoxification of organophosphonates: Cleavage of the carbon to phosphorus bond
    • Cordeiro ML, Pompliano DL, Frost JW. 1986. Degradation and detoxification of organophosphonates: cleavage of the carbon to phosphorus bond. J. Am. Chem. Soc. 108:332-334. http://dx.doi.org/10.1021/ja00262a044.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 332-334
    • Cordeiro, M.L.1    Pompliano, D.L.2    Frost, J.W.3
  • 46
    • 0023110479 scopus 로고
    • Radical-based dephosphorylation and organophosphonate biodegradation
    • DOI 10.1021/ja00241a039
    • Frost JW, Loo S, Cordeiro ML, Li D. 1987. Radical-based dephosphorylation and organophosphonate biodegradation. J. Am. Chem. Soc. 109:2166-2171. http://dx.doi.org/10.1021/ja00241a039. (Pubitemid 17043738)
    • (1987) Journal of the American Chemical Society , vol.109 , Issue.7 , pp. 2166-2171
    • Frost, J.W.1    Loo, S.2    Cordeiro, M.L.3    Li, D.4
  • 47
    • 0032900614 scopus 로고    scopus 로고
    • Rhizobium (Sinorhizobium) meliloti phn genes: Characterization and identification of their protein products
    • Parker GF, Higgins TP, Hawkes T, Robson RL. 1999. Rhizobium (Sinorhizobium) meliloti phn genes: characterization and identification of their protein products. J. Bacteriol. 181:389-395. (Pubitemid 29045127)
    • (1999) Journal of Bacteriology , vol.181 , Issue.2 , pp. 389-395
    • Parker, G.F.1    Higgins, T.P.2    Hawkes, T.3    Robson, R.L.4
  • 48
    • 84863390146 scopus 로고    scopus 로고
    • Answers to the carbon-phosphorus lyase conundrum
    • Zhang Q, van der Donk WA. 2012. Answers to the carbon-phosphorus lyase conundrum. Chembiochem 13:627-629. http://dx.doi.org/10.1002/cbic.201200020.
    • (2012) Chembiochem , vol.13 , pp. 627-629
    • Zhang, Q.1    Van Der Donk, W.A.2
  • 50
    • 67650523967 scopus 로고    scopus 로고
    • Structure of PhnP, a phosphodiesterase of the carbon-phosphorus lyase pathway for phosphonate degradation
    • Podzelinska K, He SM, Wathier M, Yakunin A, Proudfoot M, Hove-Jensen B, Zechel DL, Jia Z. 2009. Structure of PhnP, a phosphodiesterase of the carbon-phosphorus lyase pathway for phosphonate degradation. J. Biol. Chem. 284:17216-17226. http://dx.doi.org/10.1074/jbc.M808392200.
    • (2009) J. Biol. Chem. , vol.284 , pp. 17216-17226
    • Podzelinska, K.1    He, S.M.2    Wathier, M.3    Yakunin, A.4    Proudfoot, M.5    Hove-Jensen, B.6    Zechel, D.L.7    Jia, Z.8
  • 51
    • 73849123139 scopus 로고    scopus 로고
    • Accumulation of intermediates of the carbon-phosphorus lyase pathway for phosphonate degradation in phn mutants of Escherichia coli
    • Hove-Jensen B, Rosenkrantz TJ, Zechel DL, Willemoës M. 2010. Accumulation of intermediates of the carbon-phosphorus lyase pathway for phosphonate degradation in phn mutants of Escherichia coli. J. Bacteriol. 192:370-374. http://dx.doi.org/10.1128/JB.01131-09.
    • (2010) J. Bacteriol. , vol.192 , pp. 370-374
    • Hove-Jensen, B.1    Rosenkrantz, T.J.2    Zechel, D.L.3    Willemoës, M.4
  • 52
    • 0037407702 scopus 로고    scopus 로고
    • Escherichia coli phnN, encoding ribose 1,5-bisphosphokinase activity (phosphoribosyl diphosphate forming): Dual role in phosphonate degradation and NAD biosynthesis pathways
    • DOI 10.1128/JB.185.9.2793-2801.2003
    • Hove-Jensen B, Rosenkrantz TJ, Haldimann A, Wanner BL. 2003. Escherichia coli phnN, encoding ribose 1,5-bisphosphokinase activity (phosphoribosyl diphosphate forming): dual role in phosphonate degradation and NAD biosynthesis pathways. J. Bacteriol. 185:2793-2801. http://dx.doi.org/10.1128/JB.185.9.2793- 2801.2003. (Pubitemid 36514590)
    • (2003) Journal of Bacteriology , vol.185 , Issue.9 , pp. 2793-2801
    • Hove-Jensen, B.1    Rosenkrantz, T.J.2    Haldimann, A.3    Wanner, B.L.4
  • 54
    • 33947210693 scopus 로고    scopus 로고
    • Transcriptome analysis of phosphate starvation response in Escherichia coli
    • Baek JH, Lee SY. 2007. Transcriptome analysis of phosphate starvation response in Escherichia coli. J. Microbiol. Biotechnol. 17:244-252. http://www.jmb.or.kr/journal/download.php?Filedir=../submission/Journal/017/ &num=28. (Pubitemid 46421029)
    • (2007) Journal of Microbiology and Biotechnology , vol.17 , Issue.2 , pp. 244-252
    • Baek, J.H.1    Lee, S.Y.2
  • 55
    • 84887807265 scopus 로고    scopus 로고
    • Discovery of a cyclic phosphodiesterase that catalyzes the sequential hydrolysis of both ester bonds to phosphorus
    • Ghodge SV, Cummings JA, Williams HJ, Raushel FM. 2013. Discovery of a cyclic phosphodiesterase that catalyzes the sequential hydrolysis of both ester bonds to phosphorus. J. Am. Chem. Soc. 135:16360-16363. http://dx.doi.org/10. 1021/ja409376k.
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 16360-16363
    • Ghodge, S.V.1    Cummings, J.A.2    Williams, H.J.3    Raushel, F.M.4
  • 56
    • 0031740750 scopus 로고    scopus 로고
    • Molecular genetic analysis of phosphite and hypophosphite oxidation by Pseudomonas stutzeri WM88
    • Metcalf WW, Wolfe RS. 1998. Molecular genetic analysis of phosphite and hypophosphite oxidation by Pseudomonas stutzeri WM88. J. Bacteriol. 180:5547-5558. (Pubitemid 28489844)
    • (1998) Journal of Bacteriology , vol.180 , Issue.21 , pp. 5547-5558
    • Metcalf, W.W.1    Wolfe, R.S.2
  • 59
    • 79959360686 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of a pathway for the degradation of 2-aminoethylphosphonate in Sinorhizobium meliloti 1021
    • Borisova SA, Christman HD, Metcalf ME, Zulkepli NA, Zhang JK, van der Donk WA, Metcalf WW. 2011. Genetic and biochemical characterization of a pathway for the degradation of 2-aminoethylphosphonate in Sinorhizobium meliloti 1021. J. Biol. Chem. 286:22283-22290. http://dx.doi.org/10.1074/jbc.M111.237735.
    • (2011) J. Biol. Chem. , vol.286 , pp. 22283-22290
    • Borisova, S.A.1    Christman, H.D.2    Metcalf, M.E.3    Zulkepli, N.A.4    Zhang, J.K.5    Van Der Donk, W.A.6    Metcalf, W.W.7
  • 60
    • 0023101749 scopus 로고
    • Bacterial carbon-phosphorus lyase: Products, rates, and regulation of phosphonic and phosphinic acid metabolism
    • Wackett LP, Shames SL, Venditti CP, Walsh CT. 1987. Bacterial carbon-phosphorus lyase: products, rates, and regulation of phosphonic and phosphinic acid metabolism. J. Bacteriol. 169:710-717. (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
  • 62
    • 79961207559 scopus 로고    scopus 로고
    • Complete genome sequencing of Agrobacterium sp. H13-3, the former Rhizobium lupini H13-3, reveals a tripartite genome consisting of a circular and a linear chromosome and an accessory plasmid but lacking a tumor-inducing Ti-plasmid
    • Wibberg D, Blom J, Jaenicke S, Kollin F, Rupp O, Scharf B, Schneiker-Bekel S, Sczcepanowski R, Goesmann A, Setubal JC, Schmitt R, Puhler A, Schluter A. 2011. Complete genome sequencing of Agrobacterium sp. H13-3, the former Rhizobium lupini H13-3, reveals a tripartite genome consisting of a circular and a linear chromosome and an accessory plasmid but lacking a tumor-inducing Ti-plasmid. J. Biotechnol. 155:50-62. http://dx.doi.org/10.1016/ j.jbiotec.2011.01.010.
    • (2011) J. Biotechnol. , vol.155 , pp. 50-62
    • Wibberg, D.1    Blom, J.2    Jaenicke, S.3    Kollin, F.4    Rupp, O.5    Scharf, B.6    Schneiker-Bekel, S.7    Sczcepanowski, R.8    Goesmann, A.9    Setubal, J.C.10    Schmitt, R.11    Puhler, A.12    Schluter, A.13
  • 65
    • 0025818663 scopus 로고
    • Degradation of the herbicide glyphosate by members of the family Rhizobiaceae
    • Liu CM, McLean PA, Sookdeo CC, Cannon FC. 1991. Degradation of the herbicide glyphosate by members of the family Rhizobiaceae. Appl. Environ. Microbiol. 57:1799-1804.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 1799-1804
    • Liu, C.M.1    McLean, P.A.2    Sookdeo, C.C.3    Cannon, F.C.4
  • 69
    • 40849095973 scopus 로고    scopus 로고
    • Biochemical bases for a widespread tolerance of cyanobacteria to the phosphonate herbicide glyphosate
    • DOI 10.1093/pcp/pcn021
    • Forlani G, Pavan M, Gramek M, Kafarski P, Lipok J. 2008. Biochemical bases for a widespread tolerance of cyanobacteria to the phosphonate herbicide glyphosate. Plant Cell Physiol. 49:443-456. http://dx.doi.org/10.1093/pcp/ pcn021. (Pubitemid 351398316)
    • (2008) Plant and Cell Physiology , vol.49 , Issue.3 , pp. 443-456
    • Forlani, G.1    Pavan, M.2    Gramek, M.3    Kafarski, P.4    Lipok, J.5
  • 71
    • 0036920683 scopus 로고    scopus 로고
    • Detection of novel members, structure-function analysis and evolutionary classification of the 2H phosphoesterase superfamily
    • DOI 10.1093/nar/gkf645
    • Mazumder R, Iyer LM, Vasudevan S, Aravind L. 2002. Detection of novel members, structure-function analysis and evolutionary classification of the 2H phosphoesterase superfamily. Nucleic Acids Res. 30:5229-5243. http://dx.doi.org/10.1093/nar/gkf645. (Pubitemid 36033042)
    • (2002) Nucleic Acids Research , vol.30 , Issue.23 , pp. 5229-5243
    • Mazumder, R.1    Iyer, L.M.2    Vasudevan, S.3    Aravind, L.4
  • 72
    • 0032408864 scopus 로고    scopus 로고
    • The HD domain defines a new superfamily of metal-dependent phosphohydrolases
    • DOI 10.1016/S0968-0004(98)01293-6, PII S0968000498012936
    • Aravind L, Koonin EV. 1998. The HD domain defines a new superfamily of metal-dependent phosphohydrolases. Trends Biochem. Sci. 23:469-472. http://dx.doi.org/10.1016/S0968-0004(98)01293-6. (Pubitemid 29002909)
    • (1998) Trends in Biochemical Sciences , vol.23 , Issue.12 , pp. 469-472
    • Aravind, L.1    Koonin, E.V.2
  • 73
    • 67650743221 scopus 로고    scopus 로고
    • Biosynthesis of phosphonic and phosphinic acid natural products
    • Metcalf WW, van der Donk WA. 2009. Biosynthesis of phosphonic and phosphinic acid natural products. Annu. Rev. Biochem. 78:65-94. http://dx.doi.org/10.1146/annurev.biochem.78.091707.100215.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 65-94
    • Metcalf, W.W.1    Van Der Donk, W.A.2
  • 74
    • 0016194384 scopus 로고
    • The mechanism of action of fosfomycin (phosphonomycin)
    • Kahan FM, Kahan JS, Cassidy PJ, Kropp H. 1974. The mechanism of action of fosfomycin (phosphonomycin). Ann. N. Y. Acad. Sci. 235:364-386. http://dx.doi.org/10.1111/j.1749-6632.1974.tb43277.x.
    • (1974) Ann. N. Y. Acad. Sci. , vol.235 , pp. 364-386
    • Kahan, F.M.1    Kahan, J.S.2    Cassidy, P.J.3    Kropp, H.4
  • 75
  • 76
    • 40849119815 scopus 로고    scopus 로고
    • The chemolithoautotroph Acidithiobacillus ferrooxidans can survive under phosphate-limiting conditions by expressing a C-P lyase operon that allows it to grow on phosphonates
    • DOI 10.1128/AEM.02101-07
    • Vera M, Pagliai F, Guiliani N, Jerez CA. 2008. The chemolithoautotroph Acidithiobacillus ferrooxidans can survive under phosphatelimiting conditions by expressing a C-P lyase operon that allows it to grow on phosphonates. Appl. Environ. Microbiol. 74:1829-1835. http://dx.doi.org/10.1128/AEM.02101-07. (Pubitemid 351400138)
    • (2008) Applied and Environmental Microbiology , vol.74 , Issue.6 , pp. 1829-1835
    • Vera, M.1    Pagliai, F.2    Guiliani, N.3    Jerez, C.A.4
  • 78
    • 30144433545 scopus 로고    scopus 로고
    • Phosphonate utilization by the globally important marine diazotroph Trichodesmium
    • DOI 10.1038/nature04203
    • Dyhrman ST, Chappell PD, Haley ST, Moffett JW, Orchard ED, Waterbury JB, Webb EA. 2006. Phosphonate utilization by the globally important marine diazotroph Trichodesmium. Nature 439:68-71. http://dx.doi.org/10.1038/ nature04203. (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
  • 79
    • 77955622602 scopus 로고    scopus 로고
    • Phosphonate metabolism of Trichodesmium IMS101 and the production greenhouse gases
    • Beversdorf LJ, White AE, Björkman KM, Letelier RM, Karl DM. 2010. Phosphonate metabolism of Trichodesmium IMS101 and the production greenhouse gases. Limnol. Oceanogr. 55:1768-1778. http://dx.doi.org/10.4319/lo.2010.55.4. 1768.
    • (2010) Limnol. Oceanogr. , vol.55 , pp. 1768-1778
    • Beversdorf, L.J.1    White, A.E.2    Björkman, K.M.3    Letelier, R.M.4    Karl, D.M.5
  • 80
    • 80052307978 scopus 로고    scopus 로고
    • Genome sequence of Halorhabdus tiamatea, the first archaeon isolated from a deep-sea anoxic brine lake
    • Antunes A, Alam I, Bajic VB, Stingl U. 2011. Genome sequence of Halorhabdus tiamatea, the first archaeon isolated from a deep-sea anoxic brine lake. J. Bacteriol. 193:4553-4554. http://dx.doi.org/10.1128/JB.05462-11.
    • (2011) J. Bacteriol. , vol.193 , pp. 4553-4554
    • Antunes, A.1    Alam, I.2    Bajic, V.B.3    Stingl, U.4
  • 83
    • 0017410535 scopus 로고
    • Aldolase like imine formation in the mechanism of action of phosphonoacetaldehyde hydrolase
    • La Nauze JM, Coggins JR, Dixon HB. 1977. Aldolase-like imine formation in the mechanism of action of phosphonoacetaldehyde hydrolase. Biochem. J. 165:409-411. (Pubitemid 8154802)
    • (1977) Biochemical Journal , vol.165 , Issue.2 , pp. 409-411
    • La, N.J.M.1    Coggins, J.R.2    Dixon, H.B.F.3
  • 84
    • 0036063913 scopus 로고    scopus 로고
    • The 2-aminoethylphosphonate-specific transaminase of the 2-aminoethylphosphonate degradation pathway
    • DOI 10.1128/JB.184.15.4134-4140.2002
    • Kim AD, Baker AS, Dunaway-Mariano D, Metcalf WW, Wanner BL, Martin BM. 2002. The 2-aminoethylphosphonate-specific transaminase of the 2-aminoethylphosphonate degradation pathway. J. Bacteriol. 184:4134-4140. http://dx.doi.org/10.1128/JB.184.15.4134-4140.2002. (Pubitemid 34774293)
    • (2002) Journal of Bacteriology , vol.184 , Issue.15 , pp. 4134-4140
    • Kim, A.D.1    Baker, A.S.2    Dunaway-Mariano, D.3    Metcalf, W.W.4    Wanner, B.L.5    Martin, B.M.6
  • 85
    • 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 AS, Ciocci MJ, Metcalf WW, Kim J, Babbitt PC, Wanner BL, Martin BM, Dunaway-Mariano D. 1998. 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. http://dx.doi.org/10.1021/ bi972677d. (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
  • 86
    • 0028791603 scopus 로고
    • The purification and properties of phosphonoacetate hydrolase, a novel carbon-phosphorus bond-cleavage enzyme from Pseudomonas fluorescens 23F
    • McGrath JW, Wisdom GB, McMullan G, Larkin MJ, Quinn JP. 1995. The purification and properties of phosphonoacetate hydrolase, a novel carbon-phosphorus bond-cleavage enzyme from Pseudomonas fluorescens 23F. Eur. J. Biochem. 234:225-230. http://dx.doi.org/10.1111/j.1432-1033.1995.225-c.x.
    • (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
  • 87
    • 0028123662 scopus 로고
    • In vitro characterization of a phosphate starvation-independent carbon- phosphorus bond cleavage activity in Pseudomonas fluorescens 23F
    • McMullan G, Quinn JP. 1994. In vitro characterization of a phosphate starvation-independent carbon-phosphorus bond cleavage activity in Pseudomonas fluorescens 23F. J. Bacteriol. 176:320-324. (Pubitemid 24034047)
    • (1994) Journal of Bacteriology , vol.176 , Issue.2 , pp. 320-324
    • McMullan, G.1    Quinn, J.P.2
  • 88
    • 0035031803 scopus 로고    scopus 로고
    • Structural and functional analysis of the phosphonoacetate hydrolase (phnA) gene region in Pseudomonas fluorescens 23F
    • DOI 10.1128/JB.183.11.3268-3275.2001
    • Kulakova AN, Kulakov LA, Akulenko NV, Ksenzenko VN, Hamilton JT, Quinn JP. 2001. Structural and functional analysis of the phosphonoacetate hydrolase (phnA) gene region in Pseudomonas fluorescens 23F. J. Bacteriol. 183:3268-3275. http://dx.doi.org/10.1128/JB.183.11.3268-3275.2001. (Pubitemid 32448589)
    • (2001) Journal of Bacteriology , vol.183 , Issue.11 , 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
  • 89
    • 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 AN, Wisdom GB, Kulakov LA, Quinn JP. 2003. The purification and characterization of phosphonopyruvate hydrolase, a novel carbonphosphorus bond cleavage enzyme from Variovorax sp Pal2. J. Biol. Chem. 278:23426-23431. http://dx.doi.org/10.1074/jbc.M301871200. (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
  • 90
    • 80055084842 scopus 로고    scopus 로고
    • Structural and mechanistic insights into C-P bond hydrolysis by phosphonoacetate hydrolase
    • Agarwal V, Borisova SA, Metcalf WW, van der Donk WA, Nair SK. 2011. Structural and mechanistic insights into C-P bond hydrolysis by phosphonoacetate hydrolase. Chem. Biol. 18:1230-1240. http://dx.doi.org/10.1016/j.chembiol.2011. 07.019.
    • (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
  • 91
    • 0032551751 scopus 로고    scopus 로고
    • In vitro cleavage of the carbon-phosphorus bond of phosphonopyruvate by cell extracts of an environmental Burkholderia cepacia isolate
    • DOI 10.1006/bbrc.1998.8962
    • Ternan NG, Quinn JP. 1998. In vitro cleavage of the carbon-phosphorus bond of phosphonopyruvate by cell extracts of an environmental Burkholderia cepacia isolate. Biochem. Biophys. Res. Commun. 248:378-381. http://dx.doi.org/10.1006/bbrc.1998.8962. (Pubitemid 28386430)
    • (1998) Biochemical and Biophysical Research Communications , vol.248 , Issue.2 , pp. 378-381
    • Ternan, N.G.1    Quinn, J.P.2
  • 92
    • 0023785036 scopus 로고
    • Catalysis and thermodynamics of the phosphoenolpyruvate/phosphonopyruvate rearrangement. Entry into the phosphonate class of naturally occurring organophosphorus compounds
    • Bowman E, McQueney M, Barry RJ, Dunaway-Mariano D. 1988. Catalysis and thermodynamics of the phosphoenolpyruvate/phosphonopyruvate rearrangement. Entry into the phosphonate class of naturally occurring organophosphorus compounds. J. Am. Chem. Soc. 110:5575-5576.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 5575-5576
    • Bowman, E.1    McQueney, M.2    Barry, R.J.3    Dunaway-Mariano, D.4
  • 93
    • 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 AN, Kulakov LA, Villarreal-Chiu JF, Gilbert JA, McGrath JW, Quinn JP. 2009. 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. http://dx.doi.org/10.1111/ j.1574-6968.2008.01477.x.
    • (2009) FEMS Microbiol. Lett. , vol.292 , pp. 100-106
    • Kulakova, A.N.1    Kulakov, L.A.2    Villarreal-Chiu, J.F.3    Gilbert, J.A.4    McGrath, J.W.5    Quinn, J.P.6
  • 94
    • 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 GW, Delong EF. 2010. Widespread known and novel phosphonate utilization pathways in marine bacteria revealed by functional screening and metagenomic analyses. Environ. Microbiol. 12:222-238. http://dx.doi.org/10.1111/j.1462-2920.2009.02062.x.
    • (2010) Environ. Microbiol. , vol.12 , pp. 222-238
    • Martinez, A.1    Tyson, G.W.2    Delong, E.F.3
  • 95
    • 84861395902 scopus 로고    scopus 로고
    • PhnY and PhnZ comprise a new oxidative pathway for enzymatic cleavage of a carbon-phosphorus bond
    • McSorley FR, Wyatt PB, Martinez A, DeLong EF, Hove-Jensen B, Zechel DL. 2012. PhnY and PhnZ comprise a new oxidative pathway for enzymatic cleavage of a carbon-phosphorus bond. J. Am. Chem. Soc. 134:8364-8367. http://dx.doi.org/10. 1021/ja302072f.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 8364-8367
    • McSorley, F.R.1    Wyatt, P.B.2    Martinez, A.3    DeLong, E.F.4    Hove-Jensen, B.5    Zechel, D.L.6
  • 96
    • 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 JP, Kulakova AN, Cooley NA, McGrath JW. 2007. New ways to break an old bond: the bacterial carbon-phosphorus hydrolases and their role in biogeochemical phosphorus cycling. Environ. Microbiol. 9:2392-2400. http://dx.doi.org/10.1111/j.1462-2920.2007.01397.x. (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
  • 97
    • 84878016894 scopus 로고    scopus 로고
    • Organophosphonates revealed: New insights into the microbial metabolism of ancient molecules
    • McGrath JW, Chin JP, Quinn JP. 2013. Organophosphonates revealed: new insights into the microbial metabolism of ancient molecules. Nat. Rev. Microbiol. 11:412-419. http://dx.doi.org/10.1038/nrmicro3011.
    • (2013) Nat. Rev. Microbiol. , vol.11 , pp. 412-419
    • McGrath, J.W.1    Chin, J.P.2    Quinn, J.P.3
  • 99
    • 0043031049 scopus 로고    scopus 로고
    • Structural basis of Synercid (quinupristin-dalfopristin) resistance in gram-positive bacterial pathogens
    • DOI 10.1074/jbc.M303766200
    • Kehoe LE, Snidwongse J, Courvalin P, Rafferty JB, Murray IA. 2003. Structural basis of synercid (quinupristin-dalfopristin) resistance in Gram-positive bacterial pathogens. J. Biol. Chem. 278:29963-29970. http://dx.doi.org/10.1074/jbc.M303766200. (Pubitemid 36962385)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.32 , pp. 29963-29970
    • Kehoe, L.E.1    Snidwongse, J.2    Courvalin, P.3    Rafferty, J.B.4    Murray, I.A.5
  • 100
    • 0028031940 scopus 로고
    • The novel hexapeptide motif found in the acyltransferases LpxA and LpxD of lipid A biosynthesis is conserved in various bacteria
    • DOI 10.1016/0014-5793(94)80211-4
    • Vuorio R, Harkonen T, Tolvanen M, Vaara M. 1994. The novel hexapeptide motif found in the acyltransferases LpxA and LpxD of lipid A biosynthesis is conserved in various bacteria. FEBS Lett. 337:289-292. http://dx.doi.org/10. 1016/0014-5793(94)80211-4. (Pubitemid 24034789)
    • (1994) FEBS Letters , vol.337 , Issue.3 , pp. 289-292
    • Vuorio, R.1
  • 101
    • 33644695376 scopus 로고    scopus 로고
    • Functional annotation and kinetic characterization of PhnO from Salmonella enterica
    • DOI 10.1021/bi052297p
    • Errey JC, Blanchard JS. 2006. Functional annotation and kinetic characterization of PhnO from Salmonella enterica. Biochemistry 45:3033-3039. http://dx.doi.org/10.1021/bi052297p. (Pubitemid 43334551)
    • (2006) Biochemistry , vol.45 , Issue.9 , pp. 3033-3039
    • Errey, J.C.1    Blanchard, J.S.2
  • 102
    • 0029088436 scopus 로고
    • Glyphosate-degrading isolates from environmental samples: Occurrence and pathways of degradation
    • Dick RE, Quinn JP. 1995. Glyphosate-degrading isolates from environmental samples: occurrence and pathways of degradation. Appl. Microbiol. Biotechnol. 43:545-550. http://dx.doi.org/10.1007/BF00218464.
    • (1995) Appl. Microbiol. Biotechnol. , vol.43 , pp. 545-550
    • Dick, R.E.1    Quinn, J.P.2
  • 104
    • 0023645491 scopus 로고
    • Degradation of glyphosate by Pseudomonas sp. PG2982 via a sarcosine intermediate
    • Kishore GM, Jacob GS. 1987. Degradation of glyphosate by Pseudomonas sp. PG2982 via a sarcosine intermediate. J. Biol. Chem. 262:12164-12168.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12164-12168
    • Kishore, G.M.1    Jacob, G.S.2
  • 105
    • 0022972154 scopus 로고
    • Glyphosate catabolism by Pseudomonas sp. strain PG2982
    • Shinabarger DL, Braymer HD. 1986. Glyphosate catabolism by Pseudomonas sp. strain PG2982. J. Bacteriol. 168:702-707. (Pubitemid 17172759)
    • (1986) Journal of Bacteriology , vol.168 , Issue.2 , pp. 702-707
    • Shinabarger, D.L.1    Braymer, H.D.2
  • 106
    • 0023176821 scopus 로고
    • Metabolism of glyphosate in an Arthrobacter sp. GLP-1
    • DOI 10.1111/j.1432-1033.1987.tb11437.x
    • Pipke R, Amrhein N, Jacob GS, Schaefer J, Kishore GM. 1987. Metabolism of glyphosate in an Arthrobacter sp. GLP-1. Eur. J. Biochem. 165:267-273. http://dx.doi.org/10.1111/j.1432-1033.1987.tb11437.x. (Pubitemid 17092963)
    • (1987) European Journal of Biochemistry , vol.165 , Issue.2 , pp. 267-273
    • Pipke, R.1    Amrhein, N.2    Jacob, G.S.3
  • 108
    • 0026290535 scopus 로고
    • In vivo utilization of N-(phosphonomethyl)-anilines and related substances by Pseudomonas spec. GS
    • Albrecht B, Weidhase R, Stock M, Weidhase RA. 1991. In vivo utilization of N-(phosphonomethyl)-anilines and related substances by Pseudomonas spec. GS. J. Basic Microbiol. 31:403-411. http://dx.doi.org/10.1002/jobm.3620310602.
    • (1991) J. Basic Microbiol. , vol.31 , pp. 403-411
    • Albrecht, B.1    Weidhase, R.2    Stock, M.3    Weidhase, R.A.4
  • 110
    • 0023892971 scopus 로고
    • Degradation of the phosphonate herbicide glyphosate by Arthrobacter atrocyaneus ATCC 13752
    • Pipke R, Amrhein N. 1988. Degradation of the phosphonate herbicide glyphosate by Arthrobacter atrocyaneus ATCC 13752. Appl. Environ. Microbiol. 54:1293-1296.
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 1293-1296
    • Pipke, R.1    Amrhein, N.2
  • 111
    • 0000861077 scopus 로고
    • Carbon-phosphorus bond cleavage by Gram-positive and Gram-negative soil bacteria
    • Quinn JP, Peden JMM, Dick RE. 1989. Carbon-phosphorus bond cleavage by Gram-positive and Gram-negative soil bacteria. Appl. Microbiol. Biotechnol. 31:283-287.
    • (1989) Appl. Microbiol. Biotechnol. , vol.31 , pp. 283-287
    • Quinn, J.P.1    Peden, J.M.M.2    Dick, R.E.3
  • 113
    • 0036208901 scopus 로고    scopus 로고
    • Organophosphonate utilization by the thermophile Geobacillus caldoxylosilyticus T20
    • DOI 10.1128/AEM.68.4.2081-2084.2002
    • Obojska A, Ternan NG, Lejczak B, Kafarski P, McMullan G. 2002. Organophosphonate utilization by the thermophile Geobacillus caldoxylosilyticus T20. Appl. Environ. Microbiol. 68:2081-2084. http://dx.doi.org/10.1128/AEM.68.4. 2081-2084.2002. (Pubitemid 34280027)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.4 , pp. 2081-2084
    • Obojska, A.1    Ternan, N.G.2    Lejczak, B.3    Kafarski, P.4    McMullan, G.5
  • 114
    • 0003338719 scopus 로고    scopus 로고
    • Phosphorus assimilation and control of the phosphate regulon
    • Neidhardt FC, Curtis R, III, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE (ed), 2nd ed. ASM Press, Washington, DC
    • Wanner BL. 1996. Phosphorus assimilation and control of the phosphate regulon, p 1357-1381. In Neidhardt FC, Curtis R, III, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE (ed), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. ASM Press, Washington, DC.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , pp. 1357-1381
    • Wanner, B.L.1
  • 116
    • 84880888853 scopus 로고    scopus 로고
    • Directional RNA-seq reveals highly complex condition-dependent transcriptomes in E. coli K12 through accurate full-length transcripts assembling
    • Li S, Dong X, Su Z. 2013. Directional RNA-seq reveals highly complex condition-dependent transcriptomes in E. coli K12 through accurate full-length transcripts assembling. BMC Genomics 14:520. http://dx.doi.org/10.1186/1471- 2164-14-520.
    • (2013) BMC Genomics , vol.14 , pp. 520
    • Li, S.1    Dong, X.2    Su, Z.3
  • 117
    • 4344707142 scopus 로고    scopus 로고
    • The htx and ptx operons of Pseudomonas stutzeri WM88 are new members of the Pho regulon
    • DOI 10.1128/JB.186.17.5876-5882.2004
    • White AK, Metcalf WW. 2004. The htx and ptx operons of Pseudomonas stutzeri WM88 are new members of the Pho regulon. J. Bacteriol. 186:5876-5882. http://dx.doi.org/10.1128/JB.186.17.5876-5882.2004. (Pubitemid 39128661)
    • (2004) Journal of Bacteriology , vol.186 , Issue.17 , pp. 5876-5882
    • White, A.K.1    Metcalf, W.W.2
  • 118
    • 33744797980 scopus 로고    scopus 로고
    • Genome prediction of PhoB regulated promoters in Sinorhizobium meliloti and twelve proteobacteria
    • DOI 10.1093/nar/gkl365
    • Yuan ZC, Zaheer R, Morton R, Finan TM. 2006. Genome prediction of PhoB regulated promoters in Sinorhizobium meliloti and twelve proteobacteria. Nucleic Acids Res. 34:2686-2697. http://dx.doi.org/10.1093/nar/gkl365. (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
  • 119
    • 0031941653 scopus 로고    scopus 로고
    • Regulation of phosphate assimilation in Rhizobium (Sinorhizobium) meliloti
    • Bardin SD, Finan TM. 1998. Regulation of phosphate assimilation in Rhizobium (Sinorhizobium) meliloti. Genetics 148:1689-1700. (Pubitemid 28180697)
    • (1998) Genetics , vol.148 , Issue.4 , pp. 1689-1700
    • Bardin, S.D.1    Finan, T.M.2
  • 120
    • 4544275338 scopus 로고    scopus 로고
    • Global transcriptional analysis of the phosphate starvation response in Sinorhizobium meliloti strains 1021 and 2011
    • DOI 10.1007/s00438-004-1030-8
    • Krol E, Becker A. 2004. Global transcriptional analysis of the phosphate starvation response in Sinorhizobium meliloti strains 1021 and 2011. Mol. Genet. Genomics 272:1-17. http://dx.doi.org/10.1007/s00438-004-1030-8. (Pubitemid 39222581)
    • (2004) Molecular Genetics and Genomics , vol.272 , Issue.1 , pp. 1-17
    • Krol, E.1    Becker, A.2
  • 121
    • 0025905579 scopus 로고
    • A new family of bacterial regulatory proteins
    • Haydon DJ, Guest JR. 1991. A new family of bacterial regulatory proteins. FEMS Microbiol. Lett. 79:291-295. http://dx.doi.org/10.1111/j.1574-6968.1991. tb04544.x.
    • (1991) FEMS Microbiol. Lett. , vol.79 , pp. 291-295
    • Haydon, D.J.1    Guest, J.R.2
  • 122
    • 0038664315 scopus 로고    scopus 로고
    • HutC/FarR-like bacterial transcription factors of the GntR family contain a small molecule-binding domain of the chorismate lyase fold
    • DOI 10.1016/S0378-1097(03)00242-8
    • Aravind L, Anantharaman V. 2003. HutC/FarR-like bacterial transcription factors of the GntR family contain a small molecule-binding domain of the chorismate lyase fold. FEMS Microbiol. Lett. 222:17-23. http://dx.doi.org/10. 1016/S0378-1097(03)00242-8. (Pubitemid 36577347)
    • (2003) FEMS Microbiology Letters , vol.222 , Issue.1 , pp. 17-23
    • Aravind, L.1    Anantharaman, V.2
  • 124
    • 84875836888 scopus 로고    scopus 로고
    • Genome-wide transcriptional responses of Escherichia coli to glyphosate, a potent inhibitor of the shikimate pathway enzyme 5-enolpyruvylshikimate-3- phosphate synthase
    • Lu W, Li L, Chen M, Zhou Z, Zhang W, Ping S, Yan Y, Wang J, Lin M. 2013. Genome-wide transcriptional responses of Escherichia coli to glyphosate, a potent inhibitor of the shikimate pathway enzyme 5-enolpyruvylshikimate-3- phosphate synthase. Mol. Biosyst. 9:522-530. http://dx.doi.org/10.1039/ c2mb25374g.
    • (2013) Mol. Biosyst. , vol.9 , pp. 522-530
    • Lu, W.1    Li, L.2    Chen, M.3    Zhou, Z.4    Zhang, W.5    Ping, S.6    Yan, Y.7    Wang, J.8    Lin, M.9
  • 125
    • 33749602970 scopus 로고    scopus 로고
    • Time-dependent proteome alterations under osmotic stress during aerobic and anaerobic growth in Escherichia coli
    • DOI 10.1128/JB.00508-06
    • Weber A, Kogl SA, Jung K. 2006. Time-dependent proteome alterations under osmotic stress during aerobic and anaerobic growth in Escherichia coli. J. Bacteriol. 188:7165-7175. http://dx.doi.org/10.1128/JB.00508-06. (Pubitemid 44547621)
    • (2006) Journal of Bacteriology , vol.188 , Issue.20 , pp. 7165-7175
    • Weber, A.1    Kogl, S.A.2    Jung, K.3
  • 127
    • 0034161474 scopus 로고    scopus 로고
    • Macromolecular interactions: Tracing the roots
    • DOI 10.1016/S0968-0004(00)01550-4, PII S0968000400015504
    • Srere PA. 2000. Macromolecular interactions: tracing the roots. Trends Biochem. Sci. 25:150-153. http://dx.doi.org/10.1016/S0968-0004(00)01550-4. (Pubitemid 30122429)
    • (2000) Trends in Biochemical Sciences , vol.25 , Issue.3 , pp. 150-153
    • Srere, P.A.1
  • 128
    • 84864057701 scopus 로고    scopus 로고
    • Membrane transport metabolons
    • Moraes TF, Reithmeier RA. 2012. Membrane transport metabolons. Biochim. Biophys. Acta 1818:2687-2706. http://dx.doi.org/10.1016/j.bbamem.2012.06.007.
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 2687-2706
    • Moraes, T.F.1    Reithmeier, R.A.2
  • 129
    • 27744503104 scopus 로고    scopus 로고
    • The evolution of microbial phosphonate degradative pathways
    • DOI 10.1007/s00239-004-0349-4
    • Huang J, Su Z, Xu Y. 2005. The evolution of microbial phosphonate degradative pathways. J. Mol. Evol. 61:682-690. http://dx.doi.org/10.1007/ s00239-004-0349-4. (Pubitemid 41598613)
    • (2005) Journal of Molecular Evolution , vol.61 , Issue.5 , pp. 682-690
    • Huang, J.1    Su, Z.2    Xu, Y.3
  • 131
    • 0029744179 scopus 로고    scopus 로고
    • A phosphate transport system is required for symbiotic nitrogen fixation by Rhizobium meliloti
    • Bardin S, Dan S, Osteras M, Finan TM. 1996. A phosphate transport system is required for symbiotic nitrogen fixation by Rhizobium meliloti. J. Bacteriol. 178:4540-4547. (Pubitemid 26262240)
    • (1996) Journal of Bacteriology , vol.178 , Issue.15 , pp. 4540-4547
    • Bardin, S.1    Dan, S.2    Osteras, M.3    Finan, T.M.4
  • 133
    • 79961140679 scopus 로고    scopus 로고
    • Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic pathogen and symbiont of several eukaryotic hosts
    • Chain PS, Lang DM, Comerci DJ, Malfatti SA, Vergez LM, Shin M, Ugalde RA, Garcia E, Tolmasky ME. 2011. Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic pathogen and symbiont of several eukaryotic hosts. J. Bacteriol. 193:4274-4275. http://dx.doi.org/10.1128/JB.05335-11.
    • (2011) J. Bacteriol. , vol.193 , pp. 4274-4275
    • Chain, P.S.1    Lang, D.M.2    Comerci, D.J.3    Malfatti, S.A.4    Vergez, L.M.5    Shin, M.6    Ugalde, R.A.7    Garcia, E.8    Tolmasky, M.E.9
  • 140
    • 0023598123 scopus 로고
    • Chemical and mutagenic analysis of aminomethylphosphonate biodegradation
    • Avila LZ, Loo SH, Frost JW. 1987. Chemical and mutagenic analysis of aminomethylphosphonate biodegradation. J. Am. Chem. Soc. 109:6758-6764. http://dx.doi.org/10.1021/ja00256a033. (Pubitemid 18036600)
    • (1987) Journal of the American Chemical Society , vol.109 , Issue.22 , pp. 6758-6764
    • Avila, L.Z.1    Loo, S.H.2    Frost, J.W.3


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