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Volumn 76, Issue 13, 2010, Pages 4530-4537

γ-Glutamylmethylamide is an essential intermediate in the metabolism of methylamine by Methylocella silvestris

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID PATHWAY; GENE CLUSTERS; GENE HOMOLOGUES; KANAMYCINS; KETOGLUTARATE; KEY ENZYMES; MEMBRANE FRACTION; NITROGEN SOURCES; PROTEOMES; PROTEOMIC ANALYSIS; REVERSE TRANSCRIPTION; SOLE CARBON; SYNTHETASES;

EID: 77954251726     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.00739-10     Document Type: Article
Times cited : (46)

References (42)
  • 2
    • 0017577016 scopus 로고
    • Solubilization, partial purification and properties of N-methylglutamate dehydrogenase from Pseudomonas aminovorans
    • Bamforth, C. W., and P. J. Large. 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
  • 3
    • 0021778428 scopus 로고
    • Bacterial reduction of trimethylamine oxide
    • Barrett, E. L., and H. S. Kwan. 1985. Bacterial reduction of trimethylamine oxide. Annu. Rev. Microbiol. 39:131-149.
    • (1985) Annu. Rev. Microbiol. , vol.39 , pp. 131-149
    • Barrett, E.L.1    Kwan, H.S.2
  • 4
    • 0017344180 scopus 로고
    • Biochemical parameters of glutamine synthetase from Klebsiella aerogenes
    • Bender, R. A., K. A. Janssen, A. D. Resnick, M. Blumenberg, F. Foor, and B. Magasanik. 1977. Biochemical parameters of glutamine synthetase from Klebsiella aerogenes. J. Bacteriol. 129:1001-1009. (Pubitemid 8043921)
    • (1977) Journal of Bacteriology , vol.129 , Issue.2 , pp. 1001-1009
    • Bender, R.A.1    Janssen, K.A.2    Resnick, A.D.3
  • 5
    • 0036366012 scopus 로고    scopus 로고
    • Biomineralization of an organophosphorous pesticide, monocrotophos, by soil bacteria
    • Bhadbhade, B. J., S. S. Sarnaik, and P. P. Kanekar. 2002. Biomineralization of an organophosphorous pesticide, monocrotophos, by soil bacteria. J. Appl. Microbiol. 93:224-234.
    • (2002) J. Appl. Microbiol. , vol.93 , pp. 224-234
    • Bhadbhade, B.J.1    Sarnaik, S.S.2    Kanekar, P.P.3
  • 6
    • 43149110398 scopus 로고    scopus 로고
    • Intracellular organic osmolytes: Function and regulation
    • Burg, M. B., and J. D. Ferraris. 2008. Intracellular organic osmolytes: function and regulation. J. Biol. Chem. 283:7309-7313.
    • (2008) J. Biol. Chem. , vol.283 , pp. 7309-7313
    • Burg, M.B.1    Ferraris, J.D.2
  • 7
    • 0004276267 scopus 로고
    • Burns, E. A., C. A. Streuli, and P. R. Averell (ed.). Wiley Interscience, New York, NY
    • Burns, E. A., C. A. Streuli, and P. R. Averell (ed.). 1970. The analytical chemistry of nitrogen and its compounds. Wiley Interscience, New York, NY.
    • (1970) The Analytical Chemistry of Nitrogen and Its Compounds
  • 9
    • 0028216615 scopus 로고
    • Genetic organization of mau gene cluster in Methylobacterium extorquem AMI: Complete nucleotide sequence and generation and characteristics of mau mutants
    • Chistoserdov, A. Y., L. V. Chistoserdova, W. S. Mclntire, and M. E. Lidstrom. 1994. Genetic organization of mau gene cluster in Methylobacterium extorquem AMI: complete nucleotide sequence and generation and characteristics of mau mutants. J. Bacteriol. 176:4052-4065.
    • (1994) J. Bacteriol. , vol.176 , pp. 4052-4065
    • Chistoserdov, A.Y.1    Chistoserdova, L.V.2    Mclntire, W.S.3    Lidstrom, M.E.4
  • 10
    • 0029143934 scopus 로고
    • Sequence analysis of sarcosine oxidase and nearby genes reveals homologies with key enzymes of folate one-carbon metabolism
    • Chlumsky, L. J., L. Zhang, and M. S. Jorns. 1995. Sequence analysis of sarcosine oxidase and nearby genes reveals homologies with key enzymes of folate one-carbon metabolism. J. Biol. Chem. 270:18252-18259.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18252-18259
    • Chlumsky, L.J.1    Zhang, L.2    Jorns, M.S.3
  • 11
    • 21144452445 scopus 로고    scopus 로고
    • Methylocella species are facultatively methanotrophic
    • Dedysh, S. N., C. Knief, and P. F. Dunfleld. 2005. Methylocella species are facultatively methanotrophic. J. Bacteriol. 187:4665-4670.
    • (2005) J. Bacteriol. , vol.187 , pp. 4665-4670
    • Dedysh, S.N.1    Knief, C.2    Dunfleld, P.F.3
  • 12
    • 19944393048 scopus 로고
    • A new sensitive and specific test for the detection of aldehydes: Formation of 6-mercapto-3-substituted-striazolo [4,3-b]-s-tetrazines
    • Dickinson, R. G., and N. W. Jacobsen. 1970. A new sensitive and specific test for the detection of aldehydes: formation of 6-mercapto-3-substituted- striazolo [4,3-b]-s-tetrazines. Chem. Commun. (Camb.) 24:1719-1721.
    • (1970) Chem. Commun. (Camb.) , vol.24 , pp. 1719-1721
    • Dickinson, R.G.1    Jacobsen, N.W.2
  • 13
    • 0141614747 scopus 로고    scopus 로고
    • Methylocella silvestris sp. nov., A novel methanotrophic bacterium isolated from an acidic forest cambisol
    • Dunfield, P. F., V. N. Khmelenina, N. E. Suzina, Y. A. Trotsenko, and S. N. Dedysh. 2003. Methylocella silvestris sp. nov., a novel methanotrophic bacterium isolated from an acidic forest cambisol. Int. J. Syst. Evol. Microbiol. 53:1231-1239.
    • (2003) Int. J. Syst. Evol. Microbiol. , vol.53 , pp. 1231-1239
    • Dunfield, P.F.1    Khmelenina, V.N.2    Suzina, N.E.3    Trotsenko, Y.A.4    Dedysh, S.N.5
  • 16
    • 0015084936 scopus 로고
    • An N-methyl glutamate dehydrogenase from Pseudomonas M.A.
    • Hersh, L. B., J. A. Peterson, and A. A. Thompson. 1971. An N-methyl glutamate dehydrogenase from Pseudomonas M.A. Arch. Biochem. Biophys. 145:115-120.
    • (1971) Arch. Biochem. Biophys. , vol.145 , pp. 115-120
    • Hersh, L.B.1    Peterson, J.A.2    Thompson, A.A.3
  • 17
    • 0023217278 scopus 로고
    • Purification and properties of methylamine dehydrogenase from Paracoccus denitrificans
    • Husain, M., and V. L. Davidson. 1987. Purification and properties of methylamine dehydrogenase from Paracoccus denitrificans. J. Bacteriol. 169: 1712-1717.
    • (1987) J. Bacteriol. , vol.169 , pp. 1712-1717
    • Husain, M.1    Davidson, V.L.2
  • 18
    • 0025924637 scopus 로고
    • 15N NMR studies of methylamine metabolism in Pseudomonas species MA
    • 15N NMR studies of methylamine metabolism in Pseudomonas species MA J. Biol. Chem. 266: 11705-11713.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11705-11713
    • Jones, J.G.1    Bellion, E.2
  • 20
    • 0001198456 scopus 로고
    • Study of odorous compounds produced by putrefaction of foods
    • Kamiya, A., and O. Youki. 1984. Study of odorous compounds produced by putrefaction of foods. J. Chromatogr. A 292:383-391.
    • (1984) J. Chromatogr. A , vol.292 , pp. 383-391
    • Kamiya, A.1    Youki, O.2
  • 21
    • 0022345420 scopus 로고
    • Biodegradation of N-nitrosodimethylamine in aqueous and soil systems
    • Kaplan, D. L., and A. M. Kaplan. 1985. Biodegradation of N-nitrosodimethylamine in aqueous and soil systems. Appl. Environ. Microbiol. 50: 1077-1086.
    • (1985) Appl. Environ. Microbiol. , vol.50 , pp. 1077-1086
    • Kaplan, D.L.1    Kaplan, A.M.2
  • 22
    • 0031716490 scopus 로고    scopus 로고
    • Electroporation of pink-pigmented methylotrophic bacteria
    • Kim, C., and T. K. Wood. 1998. Electroporation of pink-pigmented methylotrophic bacteria. Appl. Biochem. Biotechnol. 73:81-88.
    • (1998) Appl. Biochem. Biotechnol. , vol.73 , pp. 81-88
    • Kim, C.1    Wood, T.K.2
  • 24
    • 0346162408 scopus 로고
    • Purification and characterization of -y-glutamylmethylamide synthetase from Methylophaga sp. AA-30
    • Kimura, T., I. Sugahara, K. Hanai, and Y. Tonomura. 1992. Purification and characterization of -y-glutamylmethylamide synthetase from Methylophaga sp. AA-30. Biosci. Biotechnol. Biochem. 56:708-711.
    • (1992) Biosci. Biotechnol. Biochem. , vol.56 , pp. 708-711
    • Kimura, T.1    Sugahara, I.2    Hanai, K.3    Tonomura, Y.4
  • 25
    • 85007800996 scopus 로고
    • Purification and characterization of a new -γ-glutamylmethylamide- dissimilating enzyme system from Methylophaga sp. AA-30
    • Kimura, T., I. Sugahara, K. Hanai, and Y. Tonomura. 1995. Purification and characterization of a new -γ-glutamylmethylamide-dissimilating enzyme system from Methylophaga sp. AA-30. Biosci. Biotechnol. Biochem. 59:648-655.
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 648-655
    • Kimura, T.1    Sugahara, I.2    Hanai, K.3    Tonomura, Y.4
  • 26
    • 0014670397 scopus 로고
    • γ-Glutamylmethylamide: A new intermediate in the metabolism of methylamine
    • Kung, H.-F., and C. Wagner. 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
  • 27
    • 74349122331 scopus 로고    scopus 로고
    • Genetics of the glutamate-mediated methylamine utilization pathway in the facultative methylotrophic beta-proteobacterium Methyloversatilis universalis FAM5
    • Latypova, E., S. Yang, Y.-S. Wang, T. Wang, T. A. Chavkin, M. Hackett, H. Schäfer, and M. G. Kalyuzhnaya. 2010. Genetics of the glutamate-mediated methylamine utilization pathway in the facultative methylotrophic beta-proteobacterium Methyloversatilis universalis FAM5. Mol. Microbiol. 75:426-439.
    • (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    Schäfer, H.7    Kalyuzhnaya, M.G.8
  • 28
    • 0017402139 scopus 로고
    • The demonstration of two discrete enzymes catalyzing the synthesis of glutamine and γ-glutamylmethylamide in Pseudomonas MS
    • Levitch, M. E. 1976. The demonstration of two discrete enzymes catalyzing the synthesis of glutamine and γ-glutamylmethylamide in Pseudomonas MS. Biochem. Biophys. Res. Commun. 76:609-614.
    • (1976) Biochem. Biophys. Res. Commun. , vol.76 , pp. 609-614
    • Levitch, M.E.1
  • 29
    • 0028849860 scopus 로고
    • Discovery of the ammonium substrate site on glutamine synthetase, a third cation binding site
    • Liaw, S.-H., I. Kuo, and D. Eisenberg. 1995. Discovery of the ammonium substrate site on glutamine synthetase, a third cation binding site. Protein Sci. 4:2358-2365.
    • (1995) Protein Sci. , vol.4 , pp. 2358-2365
    • Liaw, S.-H.1    Kuo, I.2    Eisenberg, D.3
  • 30
    • 0006662305 scopus 로고
    • Preparation of γ -alkylamides of glutamic acid
    • Lichtenstein, N. 1942. Preparation of γ -alkylamides of glutamic acid. J. Am. Chem. Soc. 65:1021-1022.
    • (1942) J. Am. Chem. Soc. , vol.65 , pp. 1021-1022
    • Lichtenstein, N.1
  • 31
    • 41349083576 scopus 로고    scopus 로고
    • Metabolic, phylogenetic and ecological diversity of the methanogenic Archaea
    • Liu, Y., and W. B. Whitman. 2008. Metabolic, phylogenetic and ecological diversity of the methanogenic Archaea. Ann. N. Y. Acad. Sci. 1125:171-189.
    • (2008) Ann. N. Y. Acad. Sci. , vol.1125 , pp. 171-189
    • Liu, Y.1    Whitman, W.B.2
  • 32
    • 0016916262 scopus 로고
    • Primary metabolic pathways of methylated amines in Hyphomicrobium vulgare
    • In Russian
    • Loginova, N. V., V. N. Shishkina, and Y. A. Trotsenko. 1976. Primary metabolic pathways of methylated amines in Hyphomicrobium vulgare. Mikrobiologiia 45:41-47. (In Russian.)
    • (1976) Mikrobiologiia , vol.45 , pp. 41-47
    • Loginova, N.V.1    Shishkina, V.N.2    Trotsenko, Y.A.3
  • 33
    • 0036841380 scopus 로고    scopus 로고
    • Broad-host-range cre-lox system for antibiotic marker recycling in gram-negative bacteria
    • Marx, C. J., and M. E. Lidstrom. 2002. Broad-host-range cre-lox system for antibiotic marker recycling in gram-negative bacteria. Biotechniques 33: 1062-1067.
    • (2002) Biotechniques , vol.33 , pp. 1062-1067
    • Marx, C.J.1    Lidstrom, M.E.2
  • 34
    • 0015218329 scopus 로고
    • N-methylglutamate synthetase: Purification and properties of the enzyme
    • Pollock, R. J., and L. B. Hersh. 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
  • 35
    • 18944374389 scopus 로고    scopus 로고
    • Evidence for the presence of a CmuA methyltransferase pathway in novel marine methyl halide-oxidising bacteria
    • Schäfer, H., I. R. McDonald, P. D. Nightingale, and J. C. Murrell. 2005. Evidence for the presence of a CmuA methyltransferase pathway in novel marine methyl halide-oxidising bacteria. Environ. Microbiol. 7:839-852.
    • (2005) Environ. Microbiol. , vol.7 , pp. 839-852
    • Schäfer, H.1    McDonald, I.R.2    Nightingale, P.D.3    Murrell, J.C.4
  • 36
    • 0014027099 scopus 로고
    • The enzymatic synthesis of N-methylglutamic acid
    • Shaw, W. V., L. Tsai, and E. R. Stadtman. 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, E.R.3
  • 37
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular evolutionary genetics analysis (MEGA) software version 4.0
    • Tamura, K., J. Dudley, M. Nei, and S. Kumar. 2007. MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24:1596-1599.
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 39
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL-X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., T. J. Gibson, F. Plewniak, F. Jeanmougin, and D. G. Higgins. 1997. The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25:4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 40
    • 33847178321 scopus 로고    scopus 로고
    • Characterization of theanine-forming enzyme from Methylovorus mays no. 9 in respect to utilization of theanine production
    • Yamamoto, S., M. Wakayama, and T. Tachiki. 2007. Characterization of theanine-forming enzyme from Methylovorus mays no. 9 in respect to utilization of theanine production. Biosci. Biotechnol. Biochem. 71:545-552.
    • (2007) Biosci. Biotechnol. Biochem. , vol.71 , pp. 545-552
    • Yamamoto, S.1    Wakayama, M.2    Tachiki, T.3
  • 41
    • 38549120647 scopus 로고    scopus 로고
    • Cloning and expression of Methylovorus mays no. 9 gene encoding gamma-glutamylmethylamide synthetase: An enzyme usable in theanine formation by coupling with the alcoholic fermentation system of baker's yeast
    • Yamamoto, S., M. Wakayama, and T. Tachiki. 2008. Cloning and expression of Methylovorus mays no. 9 gene encoding gamma-glutamylmethylamide synthetase: an enzyme usable in theanine formation by coupling with the alcoholic fermentation system of baker's yeast. Biosci. Biotechnol. Biochem. 72:101-109.
    • (2008) Biosci. Biotechnol. Biochem. , vol.72 , pp. 101-109
    • Yamamoto, S.1    Wakayama, M.2    Tachiki, T.3
  • 42
    • 0027254762 scopus 로고
    • Cloning, sequencing, expression and regulation of structural gene for the copper/topa quininecontaining methylamine oxidase from Arthrobacter strain P1, a gram-positive facultative methylotroph
    • Zhang, X., J. H. Fuller, and W. S. McIntire. 1993. Cloning, sequencing, expression and regulation of structural gene for the copper/topa quininecontaining methylamine oxidase from Arthrobacter strain P1, a gram-positive facultative methylotroph. J. Bacteriol. 175:5617-5627.
    • (1993) J. Bacteriol. , vol.175 , pp. 5617-5627
    • Zhang, X.1    Fuller, J.H.2    McIntire, W.S.3


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