메뉴 건너뛰기




Volumn 196, Issue 23, 2014, Pages 4130-4139

Methylamine utilization via the N-methylglutamate pathway in Methylobacterium extorquens PA1 involves a novel flow of carbon through C1 assimilation and dissimilation pathways

Author keywords

[No Author keywords available]

Indexed keywords

4 METHYLGLUTAMIC ACID; AMINE DEHYDROGENASE; BACTERIAL ENZYME; CARBON; FORMALDEHYDE; FORMALDEHYDE ACTIVATING ENZYME; FORMALDEHYDE ACTIVATING ENZYME 2; FORMALDEHYDE ACTIVATING ENZYME 3; GAMMA GLUTAMYLMETHYLAMIDE SYNTHETASE; METHYLAMINE; N METHYLGLUTAMATE; TETRAHYDROFOLIC ACID; UNCLASSIFIED DRUG; GLUTAMIC ACID DERIVATIVE; N-METHYLGLUTAMATE;

EID: 84910017381     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.02026-14     Document Type: Article
Times cited : (27)

References (53)
  • 1
    • 78751591347 scopus 로고    scopus 로고
    • Atmospheric amines. Part I. A review
    • Ge X, Wexler AS, Clegg SL. 2011. Atmospheric amines. Part I. A review. Atmos. Environ. 45:524-546. http://dx.doi.org/10.1016/j.atmosenv.2010.10.012.
    • (2011) Atmos. Environ. , vol.45 , pp. 524-546
    • Ge, X.1    Wexler, A.S.2    Clegg, S.L.3
  • 2
    • 0019998693 scopus 로고
    • Methane production and simultaneous sulphate reduction in anoxic, salt marsh sediments
    • Oremland RS, Marsh LM, Polcin S. 1982. Methane production and simultaneous sulphate reduction in anoxic, salt marsh sediments. Nature 296:143-145. http://dx.doi.org/10.1038/296143a0.
    • (1982) Nature , vol.296 , pp. 143-145
    • Oremland, R.S.1    Marsh, L.M.2    Polcin, S.3
  • 3
    • 77954251726 scopus 로고    scopus 로고
    • γ-Glutamylmethylamide is an essential intermediate in the metabolism of methylamine by Methylocella silvestris
    • Chen Y, Scanlan J, Song L, Crombie A, Rahman MT, Schafer H, Murrell JC. 2010. γ-Glutamylmethylamide is an essential intermediate in the metabolism of methylamine by Methylocella silvestris. Appl. Environ. Microbiol. 76:4350-4357. http://dx.doi.org/10.1128/AEM.00739-10.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 4350-4357
    • Chen, Y.1    Scanlan, J.2    Song, L.3    Crombie, A.4    Rahman, M.T.5    Schafer, H.6    Murrell, J.C.7
  • 4
    • 0036067632 scopus 로고    scopus 로고
    • The origin, composition and rates of organic nitrogen deposition: a missing piece of the nitrogen cycle?
    • NeffJC, Holland EA, Dentener FJ, McDowell WH, Russell KM. 2002. The origin, composition and rates of organic nitrogen deposition: a missing piece of the nitrogen cycle? Biogeochemistry 57-58:99-136. http://dx.doi.org/10.1023/A:1015791622742.
    • (2002) Biogeochemistry , vol.57-58 , pp. 99-136
    • Neff, J.C.1    Holland, E.A.2    Dentener, F.J.3    McDowell, W.H.4    Russell, K.M.5
  • 6
    • 77953623738 scopus 로고    scopus 로고
    • Monomethylamine as a nitrogen source for the nonmethylotrophic bacterium, Agrobacterium tumefaciens
    • Chen Y, McAleer KL, Murrell JC. 2010. Monomethylamine as a nitrogen source for the nonmethylotrophic bacterium, Agrobacterium tumefaciens. Appl. Environ. Microbiol. 76:4102-4104. http://dx.doi.org/10.1128/AEM.00469-10.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 4102-4104
    • Chen, Y.1    McAleer, K.L.2    Murrell, J.C.3
  • 7
    • 84865717815 scopus 로고    scopus 로고
    • Comparative genomics of methylated amine utilization by marine Roseobacter clade bacteria and development of functional gene markers (tmm, gmaS)
    • Chen Y. 2012. Comparative genomics of methylated amine utilization by marine Roseobacter clade bacteria and development of functional gene markers (tmm, gmaS). Environ. Microbiol. 14:2308-2322. http://dx.doi.org/10.1111/j.1462-2920.2012.02765.x.
    • (2012) Environ. Microbiol. , vol.14 , pp. 2308-2322
    • Chen, Y.1
  • 8
    • 0014231042 scopus 로고
    • Purification and properties of an amine dehydrogenase from Pseudomonas AM1 and its role in growth on methylamine
    • Eady RR, Large PJ. 1968. Purification and properties of an amine dehydrogenase from Pseudomonas AM1 and its role in growth on methylamine. Biochem. J. 106:245-255.
    • (1968) Biochem. J. , vol.106 , pp. 245-255
    • Eady, R.R.1    Large, P.J.2
  • 9
    • 0026072764 scopus 로고
    • Genetic organization of methylamine utilization genes from Methylobacterium extorquens AM1
    • Chistoserdov AY, Tsygankov YD, Lidstrom ML. 1991. Genetic organization of methylamine utilization genes from Methylobacterium extorquens AM1. J. Bacteriol. 173:5901-5908.
    • (1991) J. Bacteriol. , vol.173 , pp. 5901-5908
    • Chistoserdov, A.Y.1    Tsygankov, Y.D.2    Lidstrom, M.L.3
  • 10
    • 0022930678 scopus 로고
    • Methylamine oxidase from Arthrobacter P1. A bacterial copper-quinoprotein amine oxidase
    • Van Iersel J, van der Meek RA, Duine JA. 1986. Methylamine oxidase from Arthrobacter P1. A bacterial copper-quinoprotein amine oxidase. Eur. J. Biochem. 161:415-419.
    • (1986) Eur. J. Biochem. , vol.161 , pp. 415-419
    • Van Iersel, J.1    van der Meek, R.A.2    Duine, J.A.3
  • 11
    • 0028245290 scopus 로고
    • Copper amine oxidase: heterologous expression, purification, and characterization of an active enzyme in Saccharomyces cerevisiae
    • Cai D, Klinman JP. 1994. Copper amine oxidase: heterologous expression, purification, and characterization of an active enzyme in Saccharomyces cerevisiae. Biochemistry 33:7647-7653. http://dx.doi.org/10.1021/bi00190a019.
    • (1994) Biochemistry , vol.33 , pp. 7647-7653
    • Cai, D.1    Klinman, J.P.2
  • 12
    • 0025345360 scopus 로고
    • Characterization of the active site of Arthrobacter P1 methylamine oxidase: evidence for copper-quinone interactions
    • Dooley DM, McIntire WS, McGuirl MA, Cote CE, Bates JL. 1990. Characterization of the active site of Arthrobacter P1 methylamine oxidase: evidence for copper-quinone interactions. J. Am. Chem. Soc. 112:2782-2789. http://dx.doi.org/10.1021/ja00163a047.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 2782-2789
    • Dooley, D.M.1    McIntire, W.S.2    McGuirl, M.A.3    Cote, C.E.4    Bates, J.L.5
  • 13
    • 0014027099 scopus 로고
    • The enzymatic synthesis of N-methylglutamic acid
    • Shaw WV, Tsai L, Stadtman RR. 1966. The enzymatic synthesis of N-methylglutamic acid. J. Biol. Chem. 241:935-945.
    • (1966) J. Biol. Chem. , vol.241 , pp. 935-945
    • Shaw, W.V.1    Tsai, L.2    Stadtman, R.R.3
  • 14
    • 0018346819 scopus 로고
    • The isolation of pleiotropic mutants of Pseudomonas aminovorans deficient in the ability to grow on methylamine and an examination of their enzymic constitution
    • Bamforth CW, O'Connor ML. 1979. The isolation of pleiotropic mutants of Pseudomonas aminovorans deficient in the ability to grow on methylamine and an examination of their enzymic constitution. Microbiology 110:143-149.
    • (1979) Microbiology , vol.110 , pp. 143-149
    • Bamforth, C.W.1    O'Connor, M.L.2
  • 15
    • 74349122331 scopus 로고    scopus 로고
    • Genetics of the glutamate-mediated methylamine utilization pathway in the facultative methylotrophic betaproteobacteria Methyloversatilis universalis FAM5
    • Latypova E, Yang S, Wang YS, Wang T, Chavkin TA, Hackett M, Schafer H, Kalyuzhnaya MG. 2010. Genetics of the glutamate-mediated methylamine utilization pathway in the facultative methylotrophic betaproteobacteria Methyloversatilis universalis FAM5. Mol. Microbiol. 75:426-439. http://dx.doi.org/10.1111/j.1365-2958.2009.06989.x.
    • (2010) Mol. Microbiol. , vol.75 , pp. 426-439
    • Latypova, E.1    Yang, S.2    Wang, Y.S.3    Wang, T.4    Chavkin, T.A.5    Hackett, M.6    Schafer, H.7    Kalyuzhnaya, M.G.8
  • 16
    • 84877997315 scopus 로고    scopus 로고
    • Elucidation of the role of methylene-tetrahydromethanopterin dehydrogenase MtdA in the tetrahydromethanopterin-dependent oxidation pathway in Methylobacterium extorquens AM1
    • Martinez-Gomez NC, Nguyen S, Lidstrom ME. 2013. Elucidation of the role of methylene-tetrahydromethanopterin dehydrogenase MtdA in the tetrahydromethanopterin-dependent oxidation pathway in Methylobacterium extorquens AM1. J. Bacteriol. 195:2359-2367. http://dx.doi.org/10.1128/JB.00029-13.
    • (2013) J. Bacteriol. , vol.195 , pp. 2359-2367
    • Martinez-Gomez, N.C.1    Nguyen, S.2    Lidstrom, M.E.3
  • 17
    • 84899844313 scopus 로고    scopus 로고
    • Genes of theN-methylglutamate pathway are essential for growth of Methylobacterium extorquens DM4 on monomethylamine
    • Gruffaz C, Muller EEL, Louhichi-Jelail Y, Nelli YR, Guichard G, Bringel F. 2014. Genes of theN-methylglutamate pathway are essential for growth of Methylobacterium extorquens DM4 on monomethylamine. Appl. Environ. Microbiol. 80:3541-3550. http://dx.doi.org/10.1128/AEM.04160-13.
    • (2014) Appl. Environ. Microbiol. , vol.80 , pp. 3541-3550
    • Gruffaz, C.1    Muller, E.E.L.2    Louhichi-Jelail, Y.3    Nelli, Y.R.4    Guichard, G.5    Bringel, F.6
  • 18
    • 0015084936 scopus 로고
    • An N-methylglutamate dehydrogenase from Pseudomonas M.A
    • Hersh LB, Peterson JA, Thompson AA. 1971. An N-methylglutamate dehydrogenase from Pseudomonas M.A. Arch. Biochem. Biophys. 145:115-120. http://dx.doi.org/10.1016/0003-9861(71)90016-6.
    • (1971) Arch. Biochem. Biophys. , vol.145 , pp. 115-120
    • Hersh, L.B.1    Peterson, J.A.2    Thompson, A.A.3
  • 19
    • 0015814087 scopus 로고
    • N-Methylglutamate synthetase. The use of flavin mononucleotide oxidative catalysis
    • Pollock RJ, Hersh LB. 1973. N-Methylglutamate synthetase. The use of flavin mononucleotide oxidative catalysis. J. Biol. Chem. 248:6724-6733.
    • (1973) J. Biol. Chem. , vol.248 , pp. 6724-6733
    • Pollock, R.J.1    Hersh, L.B.2
  • 20
    • 0017577016 scopus 로고
    • Solubilization, partial purification, and properties of N-methylglutamate dehydrogenase from Pseudomonas aminovorans
    • Bamforth CW, Large PJ. 1977. Solubilization, partial purification, and properties of N-methylglutamate dehydrogenase from Pseudomonas aminovorans. Biochem. J. 161:357-370.
    • (1977) Biochem. J. , vol.161 , pp. 357-370
    • Bamforth, C.W.1    Large, P.J.2
  • 21
    • 0017668461 scopus 로고
    • The molecular size of N-methylglutamate dehydrogenase of Pseudomonas aminovorans
    • Bamforth CW, Large PJ. 1977. The molecular size of N-methylglutamate dehydrogenase of Pseudomonas aminovorans. Biochem. J. 167:509-512.
    • (1977) Biochem. J. , vol.167 , pp. 509-512
    • Bamforth, C.W.1    Large, P.J.2
  • 22
    • 0014670397 scopus 로고
    • Γ-Glutamylmethylamide. A new intermediate in the metabolism of methylamine
    • Kung H-F, Wagner C. 1969. Γ-Glutamylmethylamide. A new intermediate in the metabolism of methylamine. J. Biol. Chem. 244:4136-4140.
    • (1969) J. Biol. Chem. , vol.244 , pp. 4136-4140
    • Kung, H.-F.1    Wagner, C.2
  • 23
    • 0018856966 scopus 로고
    • N-Methylglutamate dehydrogenase, a flavoprotein purified from a new pink trimethylamineutilizing bacterium
    • Boulton CA, Haywood GW, Large PJ. 1979. N-Methylglutamate dehydrogenase, a flavoprotein purified from a new pink trimethylamineutilizing bacterium. Microbiology 117:293-304.
    • (1979) Microbiology , vol.117 , pp. 293-304
    • Boulton, C.A.1    Haywood, G.W.2    Large, P.J.3
  • 24
    • 0015218329 scopus 로고
    • N-Methylglutamate synthetase. Purification and properties of the enzyme
    • Pollock RJ, Hersh LB. 1971. N-Methylglutamate synthetase. Purification and properties of the enzyme. J. Biol. Chem. 246:4737-4743.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4737-4743
    • Pollock, R.J.1    Hersh, L.B.2
  • 25
    • 84925486525 scopus 로고    scopus 로고
    • Genotypic and phenotypic comparison of facultative methylotrophy between Methylobacterium extorquens strains PA1 and AM1
    • Nayak DD, Marx CJ. 2014. Genotypic and phenotypic comparison of facultative methylotrophy between Methylobacterium extorquens strains PA1 and AM1. PLoS One 9:e107887. http://dx.doi.org/10.1371/journal.pone.0107887.
    • (2014) PLoS One , vol.9
    • Nayak, D.D.1    Marx, C.J.2
  • 26
    • 0345097575 scopus 로고    scopus 로고
    • Formaldehydedetoxifying role of the tetrahydromethanopterin-linked pathway in Methylobacterium extorquens AM1
    • Marx CJ, Chistoserdova L, Lidstrom ME. 2003. Formaldehydedetoxifying role of the tetrahydromethanopterin-linked pathway in Methylobacterium extorquens AM1. J. Bacteriol. 185:7160-7168. http://dx.doi.org/10.1128/JB.185.23.7160-7168.2003.
    • (2003) J. Bacteriol. , vol.185 , pp. 7160-7168
    • Marx, C.J.1    Chistoserdova, L.2    Lidstrom, M.E.3
  • 27
    • 0032479058 scopus 로고    scopus 로고
    • 1 transfer enzymes and coenzymes linking methylotrophic bacteria and methanogenic archaea
    • 1 transfer enzymes and coenzymes linking methylotrophic bacteria and methanogenic archaea. Science 281:99-102. http://dx.doi.org/10.1126/science.281.5373.99.
    • (1998) Science , vol.281 , pp. 99-102
    • Chistoserdova, L.1    Vorholt, J.A.2    Thauer, R.K.3    Lidstrom, M.E.4
  • 28
    • 0037125221 scopus 로고    scopus 로고
    • Generation of formate by the formyltransferase/hydrolase complex (Fhc) from Methylobacterium extorquens AM1
    • Pomper BK, Saurel O, Milon A, Vorholt JA. 2002. Generation of formate by the formyltransferase/hydrolase complex (Fhc) from Methylobacterium extorquens AM1. FEBS Lett. 523:133-137. http://dx.doi.org/10.1016/S0014-5793(02)02962-9.
    • (2002) FEBS Lett. , vol.523 , pp. 133-137
    • Pomper, B.K.1    Saurel, O.2    Milon, A.3    Vorholt, J.A.4
  • 29
    • 0344235395 scopus 로고    scopus 로고
    • Purification of the formate-tetrahydrofolate ligase from Methylobacterium extorquens AM1 and demonstration of its requirement for methylotrophic growth
    • Marx CJ, Laukel M, Vorholt JA, Lidstrom ME. 2003. Purification of the formate-tetrahydrofolate ligase from Methylobacterium extorquens AM1 and demonstration of its requirement for methylotrophic growth. J. Bacteriol. 185:7169-7175. http://dx.doi.org/10.1128/JB.185.24.7169-7175.2003.
    • (2003) J. Bacteriol. , vol.185 , pp. 7169-7175
    • Marx, C.J.1    Laukel, M.2    Vorholt, J.A.3    Lidstrom, M.E.4
  • 30
    • 14544294928 scopus 로고    scopus 로고
    • Flux analysis uncovers key role of functional redundancy in formaldehyde metabolism
    • Marx CJ, Van Dien SJ, Lidstrom ME. 2005. Flux analysis uncovers key role of functional redundancy in formaldehyde metabolism. PLoS Biol. 3:e16. http://dx.doi.org/10.1371/journal.pbio.0030016.
    • (2005) PLoS Biol. , vol.3
    • Marx, C.J.1    Van Dien, S.J.2    Lidstrom, M.E.3
  • 31
    • 47249109471 scopus 로고    scopus 로고
    • Formate as the main branch point for methylotrophic metabolism in Methylobacterium extorquens AM1
    • Crowther GJ, Kosaly G, Lidstrom ME. 2008. Formate as the main branch point for methylotrophic metabolism in Methylobacterium extorquens AM1. J. Bacteriol. 190:5057-5062. http://dx.doi.org/10.1128/JB.00228-08.
    • (2008) J. Bacteriol. , vol.190 , pp. 5057-5062
    • Crowther, G.J.1    Kosaly, G.2    Lidstrom, M.E.3
  • 32
    • 0037967152 scopus 로고    scopus 로고
    • Methylotrophy in Methylobacterium extorquensAM1from a genomic point of view
    • Chistoserdova L, Chen SW, Lapidus A, Lidstrom ME. 2003. Methylotrophy in Methylobacterium extorquensAM1from a genomic point of view. J. Bacteriol. 185:2980-2987. http://dx.doi.org/10.1128/JB.185.10.2980-2987.2003.
    • (2003) J. Bacteriol. , vol.185 , pp. 2980-2987
    • Chistoserdova, L.1    Chen, S.W.2    Lapidus, A.3    Lidstrom, M.E.4
  • 33
    • 0011143461 scopus 로고
    • The metabolism of one-carbon compounds in microorganisms
    • Quayle JR. 1972. The metabolism of one-carbon compounds in microorganisms. Adv. Microb. Physiol. 7:119-203. http://dx.doi.org/10.1016/S0065-2911(08)60078-8.
    • (1972) Adv. Microb. Physiol. , vol.7 , pp. 119-203
    • Quayle, J.R.1
  • 34
    • 0033551086 scopus 로고    scopus 로고
    • A corrinoid-dependent catabolic pathway for growth of a Methylobacterium strain with chloromethane
    • Vannelli T, Messmer M, Studer A, Vuilleumier S, Leisinger T. 1999. A corrinoid-dependent catabolic pathway for growth of a Methylobacterium strain with chloromethane. Proc. Natl. Acad. Sci. U. S. A. 96:4615-4620. http://dx.doi.org/10.1073/pnas.96.8.4615.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 4615-4620
    • Vannelli, T.1    Messmer, M.2    Studer, A.3    Vuilleumier, S.4    Leisinger, T.5
  • 36
    • 77956881314 scopus 로고    scopus 로고
    • Competitiveness of diverse Methylobacterium strains in the phyllosphere of Arabidopsis thaliana and identification of representative models, including M. extorquens PA1
    • Knief C, Frances L, Vorholt JA. 2010. Competitiveness of diverse Methylobacterium strains in the phyllosphere of Arabidopsis thaliana and identification of representative models, including M. extorquens PA1. Microb. Ecol. 60:440-452. http://dx.doi.org/10.1007/s00248-010-9725-3.
    • (2010) Microb. Ecol. , vol.60 , pp. 440-452
    • Knief, C.1    Frances, L.2    Vorholt, J.A.3
  • 38
    • 70349538975 scopus 로고    scopus 로고
    • The expanding world of methylotrophic metabolism
    • Chistoserdova L, Kalyuzhnaya MG, Lidstrom ME. 2009. The expanding world of methylotrophic metabolism. Annu. Rev. Microbiol. 63:477-499. http://dx.doi.org/10.1146/annurev.micro.091208.073600.
    • (2009) Annu. Rev. Microbiol. , vol.63 , pp. 477-499
    • Chistoserdova, L.1    Kalyuzhnaya, M.G.2    Lidstrom, M.E.3
  • 39
    • 84876965085 scopus 로고    scopus 로고
    • Development of an optimized medium, strain, and highthroughput culturing methods for Methylobacterium extorquens
    • Delaney NF, Kaczmarek ME, Ward LM, Swanson PK, Lee M-C, Marx CJ. 2013. Development of an optimized medium, strain, and highthroughput culturing methods for Methylobacterium extorquens. PLoS One 8:e62957. http://dx.doi.org/10.1371/journal.pone.0062957.
    • (2013) PLoS One , vol.8
    • Delaney, N.F.1    Kaczmarek, M.E.2    Ward, L.M.3    Swanson, P.K.4    Lee, M.-C.5    Marx, C.J.6
  • 40
    • 84873601673 scopus 로고    scopus 로고
    • Good codons, bad transcript: large reductions in gene expression and fitness arising from synonymous mutations in a key enzyme
    • Agashe D, Martinez-Gomez NC, Drummond DA, Marx CJ. 2013. Good codons, bad transcript: large reductions in gene expression and fitness arising from synonymous mutations in a key enzyme. Mol. Biol. Evol. 30:549-560. http://dx.doi.org/10.1093/molbev/mss273.
    • (2013) Mol. Biol. Evol. , vol.30 , pp. 549-560
    • Agashe, D.1    Martinez-Gomez, N.C.2    Drummond, D.A.3    Marx, C.J.4
  • 41
    • 84878305954 scopus 로고    scopus 로고
    • Clarity: an open-source manager for laboratory automation
    • Delaney NF, Rojas Echenique JI, Marx CJ. 2013. Clarity: an open-source manager for laboratory automation. J. Lab Autom. 18:171-177. http://dx.doi.org/10.1177/2211068212460237.
    • (2013) J. Lab Autom. , vol.18 , pp. 171-177
    • Delaney, N.F.1    Rojas Echenique, J.I.2    Marx, C.J.3
  • 42
    • 1342346609 scopus 로고    scopus 로고
    • Characterization of two methanopterin biosynthesis mutants of Methylobacterium extorquens AM1 by use of a tetrahydromethanopterin bioassay
    • Rasche ME, Havemann SA, Rosenzvaig M. 2004. Characterization of two methanopterin biosynthesis mutants of Methylobacterium extorquens AM1 by use of a tetrahydromethanopterin bioassay. J. Bacteriol. 186: 1565-1570. http://dx.doi.org/10.1128/JB.186.5.1565-1570.2004.
    • (2004) J. Bacteriol. , vol.186 , pp. 1565-1570
    • Rasche, M.E.1    Havemann, S.A.2    Rosenzvaig, M.3
  • 43
    • 0037023907 scopus 로고    scopus 로고
    • Stoichiometric model for evaluating the metabolic capacities of the facultative methylotroph Methylobacterium extorquens AM1, with applications to reconstruction of C3 and C4 metabolism
    • Van Dien SJ, Lidstrom ME. 2002. Stoichiometric model for evaluating the metabolic capacities of the facultative methylotroph Methylobacterium extorquens AM1, with applications to reconstruction of C3 and C4 metabolism. Biotechnol. Bioeng. 78:296-312. http://dx.doi.org/10.1002/bit.10200.
    • (2002) Biotechnol. Bioeng. , vol.78 , pp. 296-312
    • Van Dien, S.J.1    Lidstrom, M.E.2
  • 44
    • 58849089274 scopus 로고    scopus 로고
    • Development of a broad-host-range sacB-based vector for unmarked allelic exchange
    • Marx CJ. 2008. Development of a broad-host-range sacB-based vector for unmarked allelic exchange. BMC Res. Notes 1:1. http://dx.doi.org/10.1186/1756-0500-1-1.
    • (2008) BMC Res. Notes , vol.1 , pp. 1
    • Marx, C.J.1
  • 46
    • 0001289754 scopus 로고
    • The biological control of chemical factors in the environment
    • Redfield AC. 1958. The biological control of chemical factors in the environment. Am. Sci. 46:205-221.
    • (1958) Am. Sci. , vol.46 , pp. 205-221
    • Redfield, A.C.1
  • 47
    • 0034460957 scopus 로고    scopus 로고
    • Novel formaldehyde-activating enzyme in Methylobacterium extorquens AM1
    • Vorholt JA, Marx CJ, Lidstrom ME, Thauer RK. 2000. Novel formaldehyde-activating enzyme in Methylobacterium extorquens AM1. J. Bacteriol. 182:6645-6650. http://dx.doi.org/10.1128/JB.182.23.6645-6650.2000.
    • (2000) J. Bacteriol. , vol.182 , pp. 6645-6650
    • Vorholt, J.A.1    Marx, C.J.2    Lidstrom, M.E.3    Thauer, R.K.4
  • 48
    • 0028172819 scopus 로고
    • Genetics of the serine cycle in Methylobacterium extorquens AM1: cloning, sequence, mutation and physiological effect of glyA, the gene for serine hydroxymethyltransferase
    • Chistoserdova L, Lidstrom ME. 1994. Genetics of the serine cycle in Methylobacterium extorquens AM1: cloning, sequence, mutation and physiological effect of glyA, the gene for serine hydroxymethyltransferase. J. Bacteriol. 176:6759-6762.
    • (1994) J. Bacteriol. , vol.176 , pp. 6759-6762
    • Chistoserdova, L.1    Lidstrom, M.E.2
  • 50
    • 17144399884 scopus 로고    scopus 로고
    • 1 carrier tetrahydromethanopterin. Structure of the tetrahydromethanopterindependent formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1
    • 1 carrier tetrahydromethanopterin. Structure of the tetrahydromethanopterindependent formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1. J. Biol. Chem. 280:13712-13719. http://dx.doi.org/10.1074/jbc.M412320200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 13712-13719
    • Acharya, P.1    Goenrich, M.2    Hagemeier, C.H.3    Demmer, U.4    Vorholt, J.A.5    Thauer, R.K.6    Ermler, U.7
  • 51
    • 84885119847 scopus 로고    scopus 로고
    • Comparative transcriptomics in three Methylophilaceae species uncover different strategies for environmental adaptation
    • Vorobev A, Beck DAC, Kalyuzhnaya MG, Lidstrom ME, Chistoserdova L. 2013. Comparative transcriptomics in three Methylophilaceae species uncover different strategies for environmental adaptation. PeerJ 1:e115. http://dx.doi.org/10.7717/peerj.115.
    • (2013) PeerJ , vol.1
    • Vorobev, A.1    Beck, D.A.C.2    Kalyuzhnaya, M.G.3    Lidstrom, M.E.4    Chistoserdova, L.5
  • 52
    • 79961061069 scopus 로고    scopus 로고
    • Methylotrophy in a lake: from metagenomics to single-organism physiology
    • Chistoserdova L. 2011. Methylotrophy in a lake: from metagenomics to single-organism physiology. Appl. Environ. Microbiol. 77:4705-4711. http://dx.doi.org/10.1128/AEM.00314-11.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 4705-4711
    • Chistoserdova, L.1
  • 53
    • 0000527903 scopus 로고
    • Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans
    • Figurski DH, Helinski DR. 1979. Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans. Proc. Natl. Acad. Sci. U. S. A. 76:1648-1652. http://dx.doi.org/10.1073/pnas.76.4.1648.
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 1648-1652
    • Figurski, D.H.1    Helinski, D.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.