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Volumn 75, Issue 2, 2010, Pages 426-439

Genetics of the glutamate-mediated methylamine utilization pathway in the facultative methylotrophic beta-proteobacterium Methyloversatilis universalis FAM5

Author keywords

[No Author keywords available]

Indexed keywords

FERREDOXIN; GAMMA GLUTAMYLMETHYLAMIDE SYNTHETASE; GLUTAMATE AMMONIA LIGASE; GLUTAMATE SYNTHASE; GLUTAMIC ACID; METHYLAMINE; N METHYLGLUTAMATE DEHYDROGENASE; N METHYLGLUTAMATE SYNTHETASE; OXIDOREDUCTASE; POLYPEPTIDE; PROTEIN GLTB2; SARCOSINE OXIDASE; SYNTHETASE; UNCLASSIFIED DRUG;

EID: 74349122331     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2009.06989.x     Document Type: Article
Times cited : (69)

References (68)
  • 1
    • 0000286509 scopus 로고
    • Amines in blood and urine in relation to liver disease
    • Asatoor, A.M. Kerr, D.N.S. (1961) Amines in blood and urine in relation to liver disease. Clin Chim Acta 6 : 149 156.
    • (1961) Clin Chim Acta , vol.6 , pp. 149-156
    • Asatoor, A.M.1    Kerr, D.N.S.2
  • 2
    • 0017577016 scopus 로고
    • Solubilization, partial purification and properties of N-methylglutamate dehydrogenase from Pseudomonas aminovorans
    • Bamforth, C.W. Large, P.J. (1977a) 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
    • 0017668461 scopus 로고
    • The molecular size of N-methylglutamate dehydrogenase of Pseudomonas aminovorans
    • Bamforth, C.W. Large, P.J. (1977b) 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
  • 4
    • 0018346819 scopus 로고
    • The Isolation of pleiotrophic mutants of Pseudomonas aminovorans deficient in the ability to grow on methylamine and an examination of their enzyme constitution
    • Bamforth, C.W. O'Connor, M.L. (1979) The Isolation of pleiotrophic mutants of Pseudomonas aminovorans deficient in the ability to grow on methylamine and an examination of their enzyme constitution. J Gen Microbiol 110 : 143 149.
    • (1979) J Gen Microbiol , vol.110 , pp. 143-149
    • Bamforth, C.W.1    O'Connor, M.L.2
  • 5
    • 0018856966 scopus 로고
    • N-methylglutamate dehydrogenase, a flavohaemoprotein purified from a new pink trimethylamine-utilizing bacterium
    • Boulton, C.A., Haywood, G.W. Large, P.J. (1980) N-methylglutamate dehydrogenase, a flavohaemoprotein purified from a new pink trimethylamine- utilizing bacterium. J Gen Microbiol 117 : 293 304.
    • (1980) J Gen Microbiol , vol.117 , pp. 293-304
    • Boulton, C.A.1    Haywood, G.W.2    Large, P.J.3
  • 6
    • 0036330578 scopus 로고    scopus 로고
    • Trimethylamine oxide accumulation in marine animals: Relationship to acylglycerol storage
    • Brad, A., Seibel, B.A. Walsh, P.J. (2002) Trimethylamine oxide accumulation in marine animals: relationship to acylglycerol storage. J Exp Biol 205 : 297 306.
    • (2002) J Exp Biol , vol.205 , pp. 297-306
    • Brad, A.1    Seibel, B.A.2    Walsh, P.J.3
  • 7
    • 0028216615 scopus 로고
    • Genetic organization of the mau gene cluster in Methylobacterium extorquens AM1: Complete nucleotide sequence and generation and characteristics of mau mutants
    • Chistoserdov, A.Y., Chistoserdova, L.V., McIntire, W.S. Lidstrom, M.E. (1994) Genetic organization of the mau gene cluster in Methylobacterium extorquens AM1: 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    McIntire, W.S.3    Lidstrom, M.E.4
  • 8
    • 34249812080 scopus 로고    scopus 로고
    • Genome of Methylobacillus flagellatus, molecular basis for obligate methylotrophy, and polyphyletic origin of methylotrophy
    • Chistoserdova, L., Lapidus, A., Han, C., Goodwin, L., Saunders, L., Brettin, T., et al. (2007) Genome of Methylobacillus flagellatus, molecular basis for obligate methylotrophy, and polyphyletic origin of methylotrophy. J Bacteriol 11 : 4020 4027.
    • (2007) J Bacteriol , vol.11 , pp. 4020-4027
    • Chistoserdova, L.1    Lapidus, A.2    Han, C.3    Goodwin, L.4    Saunders, L.5    Brettin, T.6
  • 9
    • 0029143934 scopus 로고
    • Sequence analysis of sarcosine oxidase and nearby genes reveals homologies with key enzymes of folate one-carbon metabolism
    • Chlumsky, L.J., Zhang, L. Jorns, M.S. (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
  • 10
    • 5444228842 scopus 로고    scopus 로고
    • Methylobacillus pratensis sp. nov., a novel non-pigmented, aerobic, obligately methylotrophic bacterium isolated from meadow grass
    • Doronina, N.V., Trotsenko, Y.A., Kolganova, T.V., Tourova, T.P. Salkinoja-Salonen, M.S. (2004) Methylobacillus pratensis sp. nov., a novel non-pigmented, aerobic, obligately methylotrophic bacterium isolated from meadow grass. Int J Syst Evol Microbiol 54 : 1453 1457.
    • (2004) Int J Syst Evol Microbiol , vol.54 , pp. 1453-1457
    • Doronina, N.V.1    Trotsenko, Y.A.2    Kolganova, T.V.3    Tourova, T.P.4    Salkinoja-Salonen, M.S.5
  • 11
    • 0014231042 scopus 로고
    • Purification and properties of an amine dehydrogenase from Pseudomonas AM1 and its role in growth on methylamine
    • Eady, R.R. Large, P.J. (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
  • 12
    • 0015154434 scopus 로고
    • Microbial oxidation of amines. Partial purification of a mixed-function secondary-amine oxidase system from Pseudomonas aminovorans that contains an enzymically active cytochrome-P-420-type haemoprotein
    • Eady, R.R., Jarmant, T.R. Large, P.J. (1971) Microbial oxidation of amines. Partial purification of a mixed-function secondary-amine oxidase system from Pseudomonas aminovorans that contains an enzymically active cytochrome-P-420-type haemoprotein. Biochem J 125 : 449 459.
    • (1971) Biochem J , vol.125 , pp. 449-459
    • Eady, R.R.1    Jarmant, T.R.2    Large, P.J.3
  • 13
    • 33845530709 scopus 로고    scopus 로고
    • Burkholderia phymatum is a highly effective nitrogen-fixing symbiont of Mimosa spp. and fixes nitrogen ex planta
    • Elliott, G.N., Chen, W.M., Chou, J.H., Wang, H.C., Sheu, S.Y., Perin, L., et al. (2007) Burkholderia phymatum is a highly effective nitrogen-fixing symbiont of Mimosa spp. and fixes nitrogen ex planta. New Phytol 173 : 168 180.
    • (2007) New Phytol , vol.173 , pp. 168-180
    • Elliott, G.N.1    Chen, W.M.2    Chou, J.H.3    Wang, H.C.4    Sheu, S.Y.5    Perin, L.6
  • 14
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass-spectral data of peptides with amino-acid-sequences in a protein database
    • Eng, J.K., McCormack, A.L. Yates, J.R. (1994) An approach to correlate tandem mass-spectral data of peptides with amino-acid-sequences in a protein database. J Am Soc Mass Spectrom 5 : 976 989.
    • (1994) J Am Soc Mass Spectrom , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.3
  • 15
    • 0035826615 scopus 로고    scopus 로고
    • Organization of the multiple coenzymes and subunits and role of the covalent flavin link in the complex heterotetrameric sarcosine oxidase
    • Eschenbrenner, M., Chlumsky, L.J., Khanna, P., Strasser, F. Jorns, M.S. (2001) Organization of the multiple coenzymes and subunits and role of the covalent flavin link in the complex heterotetrameric sarcosine oxidase. Biochemistry 40 : 5352 5367.
    • (2001) Biochemistry , vol.40 , pp. 5352-5367
    • Eschenbrenner, M.1    Chlumsky, L.J.2    Khanna, P.3    Strasser, F.4    Jorns, M.S.5
  • 16
    • 0030791125 scopus 로고    scopus 로고
    • Organization of methylamine utilization genes (mau) in 'Methylobacillus flagellatum' KT and analysis of mau mutants
    • Gak, E.R., Tsygankov, Y.D. Chistoserdov, A.Y. (1997) Organization of methylamine utilization genes (mau) in 'Methylobacillus flagellatum' KT and analysis of mau mutants. Microbiology 143 : 1827 1835.
    • (1997) Microbiology , vol.143 , pp. 1827-1835
    • Gak, E.R.1    Tsygankov, Y.D.2    Chistoserdov, A.Y.3
  • 17
    • 0015084936 scopus 로고
    • An N-methyl glutamate dehydrogenase from Pseudomonas M.A
    • Hersh, L.B., Peterson, J.A. Thompson, A.A. (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
  • 18
    • 0015335694 scopus 로고
    • N-methyl glutamate dehydrogenase: Kinetic studies on the solubilized enzyme
    • Hersh, L.B., Stark, M.J., Worthen, S. Fiero, M.K. (1972) N-methyl glutamate dehydrogenase: kinetic studies on the solubilized enzyme. Arch Biochem Biophys 150 : 219 226.
    • (1972) Arch Biochem Biophys , vol.150 , pp. 219-226
    • Hersh, L.B.1    Stark, M.J.2    Worthen, S.3    Fiero, M.K.4
  • 19
    • 0025924637 scopus 로고
    • 15N NMR studies of methylamine metabolism in Pseudomonas species
    • 15N NMR studies of methylamine metabolism in Pseudomonas species. J Biol Chem 266 : 11705 11713.
    • (1991) J Biol Chem , vol.266 , pp. 11705-11713
    • Jones, J.G.1    Bellion, E.2
  • 20
    • 33751257179 scopus 로고    scopus 로고
    • Methyloversatilis universalis gen. nov., sp. nov., a novel taxon within the Betaproteobacteria represented by three methylotrophic isolates
    • Kalyuzhnaya, M.G., De Marco, P., Bowerman, S., Pacheco, C.C., Lara, J.C., Lidstrom, M.E. Chistoserdova, L. (2006) Methyloversatilis universalis gen. nov., sp. nov., a novel taxon within the Betaproteobacteria represented by three methylotrophic isolates. Int J Syst Evol Microbiol 56 : 2517 2522.
    • (2006) Int J Syst Evol Microbiol , vol.56 , pp. 2517-2522
    • Kalyuzhnaya, M.G.1    De Marco, P.2    Bowerman, S.3    Pacheco, C.C.4    Lara, J.C.5    Lidstrom, M.E.6    Chistoserdova, L.7
  • 21
    • 51349161191 scopus 로고    scopus 로고
    • High-resolution metagenomics targets specific functional types in complex microbial communities
    • Kalyuzhnaya, M.G., Lapidus, A., Ivanova, N., Copeland, A.C., McHardy, A.C., Szeto, E., et al. (2008) High-resolution metagenomics targets specific functional types in complex microbial communities. Nat Biotechnol 26 : 1029 1034.
    • (2008) Nat Biotechnol , vol.26 , pp. 1029-1034
    • Kalyuzhnaya, M.G.1    Lapidus, A.2    Ivanova, N.3    Copeland, A.C.4    McHardy, A.C.5    Szeto, E.6
  • 22
    • 0022526771 scopus 로고
    • Stimulation of methanogenesis by aldicarb and several other N-methyl carbamate pesticides
    • Kiene, R.P. Capone, D.G. (1986) Stimulation of methanogenesis by aldicarb and several other N-methyl carbamate pesticides. Appl Environ Microbiol 51 : 1247 1251.
    • (1986) Appl Environ Microbiol , vol.51 , pp. 1247-1251
    • Kiene, R.P.1    Capone, D.G.2
  • 23
    • 0346162408 scopus 로고
    • Purification and characterization of γ-glutamylmethylamide synthetase from Methylophaga sp. AA-30
    • Kimura, T., Sugahara, I., Hanai, K. Tonomura, Y. (1992) Purification and characterization of γ-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
  • 24
    • 85007800996 scopus 로고
    • Purification and characterization of the new γ-glutamylmethylamide dissimilating enzyme system from Methylophaga sp. AA-30
    • Kimura, T., Sugahara, I., Hanai, K. Asahi, T. (1995) Purification and characterization of the 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    Asahi, T.4
  • 25
    • 0000000443 scopus 로고
    • Metabolism of acetate, methanol, and methylated amines in intertidal sediments of Lowes Cove, Maine
    • King, G.M., Klug, M.J. Lovley, D.R. (1983) Metabolism of acetate, methanol, and methylated amines in intertidal sediments of Lowes Cove, Maine. Appl Environ Microbiol 45 : 1848 1853.
    • (1983) Appl Environ Microbiol , vol.45 , pp. 1848-1853
    • King, G.M.1    Klug, M.J.2    Lovley, D.R.3
  • 26
    • 74349130747 scopus 로고
    • Metabolic conversion of N-methyl carbon of γ-glutamylmethylamide to caffeine in tea plants
    • Konishi, S., Ozasa, M. Takahashi, E. (1972) Metabolic conversion of N-methyl carbon of γ-glutamylmethylamide to caffeine in tea plants. Plant Cell Physiol 13 : 365 375.
    • (1972) Plant Cell Physiol , vol.13 , pp. 365-375
    • Konishi, S.1    Ozasa, M.2    Takahashi, E.3
  • 27
    • 0014670397 scopus 로고
    • Gamma-glutamylmethylamide. A new intermediate in the metabolism of methylamine
    • Kung, H.F. Wagner, C. (1969) Gamma-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
  • 28
    • 0014738495 scopus 로고
    • Oxidation of C1-compounds by Pseudomonas sp. MS
    • Kung, H.F. Wagner, C. (1970) Oxidation of C1-compounds by Pseudomonas sp. MS. Biochem J 116 : 357 365.
    • (1970) Biochem J , vol.116 , pp. 357-365
    • Kung, H.F.1    Wagner, C.2
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 : 680 685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 33750583876 scopus 로고    scopus 로고
    • The copper-containing amine oxidase from Arthrobacter globiformis: Refinement at 1.55 and 2.20 A resolution in two crystal forms
    • Langley, D.B., Duff, A.P., Freeman, H.C. Guss, J.M. (2006) The copper-containing amine oxidase from Arthrobacter globiformis: refinement at 1.55 and 2.20 A resolution in two crystal forms. Acta Crystallogr 62 : 1052 1057.
    • (2006) Acta Crystallogr , vol.62 , pp. 1052-1057
    • Langley, D.B.1    Duff, A.P.2    Freeman, H.C.3    Guss, J.M.4
  • 32
    • 0000842682 scopus 로고
    • Amino acid and amine biogeo-chemistry in marine particulate material and sediments
    • In. Blackburn, T.H. Sorensen, J. eds). Chichester. John Wiley & Sons. pp.
    • Lee, C. (1988) Amino acid and amine biogeo-chemistry in marine particulate material and sediments. In Nitrogen Cycling in Coastal Marine Environments. Blackburn, T.H. Sorensen, J. (eds). Chichester : John Wiley & Sons, pp. 125 141.
    • (1988) Nitrogen Cycling in Coastal Marine Environments. , pp. 125-141
    • Lee, C.1
  • 33
    • 0016800405 scopus 로고
    • Purification and characterization of N-methylalanine dehydrogenase
    • Lin, M.C. Wagner, C. (1975) Purification and characterization of N-methylalanine dehydrogenase. J Biol Chem 250 : 3746 3751.
    • (1975) J Biol Chem , vol.250 , pp. 3746-3751
    • Lin, M.C.1    Wagner, C.2
  • 34
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • 3rd
    • Liu, H., Sadygov, R.G. Yates, J.R. 3rd (2004) A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal Chem 76 : 4193 4201.
    • (2004) Anal Chem , vol.76 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates, J.R.3
  • 35
    • 0016916262 scopus 로고
    • Primary metabolic pathways of methylated amines in Hyphomicrobium vulgare
    • English translation).
    • Loginova, N.V., Shishkina, V.N. Trotsenko, Yu.A. (1974) Primary metabolic pathways of methylated amines in Hyphomicrobium vulgare (English translation). Mikrobiologiya 45 : 41 47.
    • (1974) Mikrobiologiya , vol.45 , pp. 41-47
    • Loginova, N.V.1    Shishkina, V.N.2    Trotsenko, Y.A.3
  • 37
    • 0036841380 scopus 로고    scopus 로고
    • Broad-host-range cre-lox system for antibiotic marker recycling in gram-negative bacteria
    • Marx, C.J. Lidstrom, M.E. (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
  • 38
    • 0017848707 scopus 로고
    • Aerobic and anaerobic metabolism of trimethylamine, dimethylamine and methylamine in Hyphomicrobium X
    • Meiberg, J.B.M. Harder, W. (1978) Aerobic and anaerobic metabolism of trimethylamine, dimethylamine and methylamine in Hyphomicrobium X. J Gen Microbiol 106 : 265 276.
    • (1978) J Gen Microbiol , vol.106 , pp. 265-276
    • Meiberg, J.B.M.1    Harder, W.2
  • 39
    • 19544371964 scopus 로고    scopus 로고
    • Labrys methylaminiphilus sp. nov., a novel facultatively methylotrophic bacterium from a freshwater lake sediment
    • Miller, J.A., Kalyuzhnaya, M.G., Noyes, E., Lara, J.C., Lidstrom, M.E. Chistoserdova, L. (2005) Labrys methylaminiphilus sp. nov., a novel facultatively methylotrophic bacterium from a freshwater lake sediment. Int J Syst Evol Microbiol 55 : 1247 1253.
    • (2005) Int J Syst Evol Microbiol , vol.55 , pp. 1247-1253
    • Miller, J.A.1    Kalyuzhnaya, M.G.2    Noyes, E.3    Lara, J.C.4    Lidstrom, M.E.5    Chistoserdova, L.6
  • 41
    • 77049138167 scopus 로고
    • The colorimetric estimation of formaldehyde by means of the Hantzsch reaction
    • Nash, T. (1953) The colorimetric estimation of formaldehyde by means of the Hantzsch reaction. Biochemical J 55 : 416 421.
    • (1953) Biochemical J , vol.55 , pp. 416-421
    • Nash, T.1
  • 42
    • 0036067632 scopus 로고    scopus 로고
    • The origin, composition and rates of organic nitrogen deposition: A missing piece of the nitrogen cycle?
    • Neff, J.C., Holland, E.A., Dentener, F.J., McDowell, W.H. Russell, K.M. (2002) The origin, composition and rates of organic nitrogen deposition: a missing piece of the nitrogen cycle? Biogeochemistry 57/58 : 99 136.
    • (2002) Biogeochemistry , vol.5758 , pp. 99-136
    • Neff, J.C.1    Holland, E.A.2    Dentener, F.J.3    McDowell, W.H.4    Russell, K.M.5
  • 43
    • 0009680426 scopus 로고
    • Glutamine synthetase of pea leaves
    • O'Neal, D. Joy, K.W. (1974) Glutamine synthetase of pea leaves. Plant Physiol 54 : 773 779.
    • (1974) Plant Physiol , vol.54 , pp. 773-779
    • O'Neal, D.1    Joy, K.W.2
  • 44
    • 0019998693 scopus 로고
    • Methane production and simultaneous sulphate reduction in anoxic, salt marsh sediments
    • Oremland, R.S., Marsh, L.M. Polcin, S. (1982) Methane production and simultaneous sulphate reduction in anoxic, salt marsh sediments. Nature 296 : 143 145.
    • (1982) Nature , vol.296 , pp. 143-145
    • Oremland, R.S.1    Marsh, L.M.2    Polcin, S.3
  • 45
    • 0025695947 scopus 로고
    • Formation and breakdown of glycine betaine and trimethylamine in hypersaline environments
    • Oren, A. (1990) Formation and breakdown of glycine betaine and trimethylamine in hypersaline environments. Antonie Van Leeuwenhoek 58 : 291 298.
    • (1990) Antonie Van Leeuwenhoek , vol.58 , pp. 291-298
    • Oren, A.1
  • 46
    • 29444457740 scopus 로고    scopus 로고
    • Treatment of waste gas containing monomethylamine in a biofilter enriched with Pseudomonas mendocina
    • Pandey, R.A., Gangane, R., Mudliak, S.N. Rajvaidya, A.S. (2006) Treatment of waste gas containing monomethylamine in a biofilter enriched with Pseudomonas mendocina. Waste Manag (Oxford) 26 : 233 244.
    • (2006) Waste Manag (Oxford) , vol.26 , pp. 233-244
    • Pandey, R.A.1    Gangane, R.2    Mudliak, S.N.3    Rajvaidya, A.S.4
  • 47
    • 0037277179 scopus 로고    scopus 로고
    • Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: The yeast proteome
    • Peng, J., Elias, J.E., Thoreen, C.C., Licklider, L.J. Gygi, S.P. (2003) Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: the yeast proteome. J Proteome Res 2 : 43 50.
    • (2003) J Proteome Res , vol.2 , pp. 43-50
    • Peng, J.1    Elias, J.E.2    Thoreen, C.C.3    Licklider, L.J.4    Gygi, S.P.5
  • 48
    • 0015218329 scopus 로고
    • N-methylglutamate synthetase. Purification and properties of the enzyme
    • Pollock, R.J. Hersh, L.B. (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
  • 49
    • 0015814087 scopus 로고
    • N-methylglutamate synthetase. the use of flavin mononucleotide in oxidative catalysis
    • Pollock, R.J. Hersh, L.B. (1973) N-methylglutamate synthetase. The use of flavin mononucleotide in 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
  • 51
    • 0014027099 scopus 로고
    • The enzymatic synthesis of N-methylglutamic acid
    • Shaw, W.V., Tsai, L. Stadtman, E.R. (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
  • 52
    • 0029927505 scopus 로고    scopus 로고
    • Mass Spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O. Mann, M. (1996) Mass Spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal Chem 68 : 850 858.
    • (1996) Anal Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 54
    • 0342652977 scopus 로고
    • Growth determination and medium analysis
    • In. Pollard, J.W. Walker, J.M. eds). Clifton. Humana Press. Vol. 6, pp.
    • Stepan-Sarkissian, G. Grey, D. (1990) Growth determination and medium analysis. In Methods in Molecular Biology, Plant Cell and Tissue Culture. Pollard, J.W. Walker, J.M. (eds). Clifton : Humana Press, Vol. 6, pp. 13 28 182 : 50 69.
    • (1990) Methods in Molecular Biology, Plant Cell and Tissue Culture. , vol.182 , pp. 13-28
    • Stepan-Sarkissian, G.1    Grey, D.2
  • 56
    • 0036393898 scopus 로고    scopus 로고
    • DTASelect and Contrast: Tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb, D.L., McDonald, W.H. Yates, J.R. (2002) DTASelect and Contrast: tools for assembling and comparing protein identifications from shotgun proteomics. J Proteome Res 1 : 21 26.
    • (2002) J Proteome Res , vol.1 , pp. 21-26
    • Tabb, D.L.1    McDonald, W.H.2    Yates, J.R.3
  • 59
    • 0032951727 scopus 로고    scopus 로고
    • Glutamate synthase: A complex iron-sulfur flavoprotein
    • Vanoni, M.A. Curti, B. (1999) Glutamate synthase: a complex iron-sulfur flavoprotein. Cell Mol Life Sci 55 : 617 638.
    • (1999) Cell Mol Life Sci , vol.55 , pp. 617-638
    • Vanoni, M.A.1    Curti, B.2
  • 60
    • 0031172645 scopus 로고    scopus 로고
    • Folate utilization by monomeric versus heterotetrameric sarcosine oxidases
    • Wagner, M.A. Jorns, S.M. (1997) Folate utilization by monomeric versus heterotetrameric sarcosine oxidases. Arch Biochem Biophys 342 : 176 181.
    • (1997) Arch Biochem Biophys , vol.342 , pp. 176-181
    • Wagner, M.A.1    Jorns, S.M.2
  • 61
    • 0034254672 scopus 로고    scopus 로고
    • Monomeric sarcosine oxidase: 2. Kinetic studies with sarcosine, alternate substrates, and a substrate analogue
    • Wagner, M.A. Jorns, S.M. (2000) Monomeric sarcosine oxidase: 2. Kinetic studies with sarcosine, alternate substrates, and a substrate analogue. Biochemistry 39 : 8825 8829.
    • (2000) Biochemistry , vol.39 , pp. 8825-8829
    • Wagner, M.A.1    Jorns, S.M.2
  • 62
    • 0033609040 scopus 로고    scopus 로고
    • Structure of the flavocoenzyme of two homologous amine oxidases: Monomeric sarcosine oxidase and N-methyltryptophan oxidase
    • Wagner, M.A., Khanna, P. Jorns, M.S. (1997) Structure of the flavocoenzyme of two homologous amine oxidases: monomeric sarcosine oxidase and N-methyltryptophan oxidase. Biochemistry 38 : 5588 5595.
    • (1997) Biochemistry , vol.38 , pp. 5588-5595
    • Wagner, M.A.1    Khanna, P.2    Jorns, M.S.3
  • 63
    • 33646927488 scopus 로고    scopus 로고
    • Quantitative proteomics of the archaeon Methanococcus maripaludis validated by microarray analysis and real time PCR
    • Xia, Q., Hendrickson, E.L., Zhang, Y., Wang, T., Taub, F., Moore, B.C., et al. (2006) Quantitative proteomics of the archaeon Methanococcus maripaludis validated by microarray analysis and real time PCR. Mol Cell Proteomics 5 : 868 881.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 868-881
    • Xia, Q.1    Hendrickson, E.L.2    Zhang, Y.3    Wang, T.4    Taub, F.5    Moore, B.C.6
  • 64
    • 33847178321 scopus 로고    scopus 로고
    • Characterization of theanine-forming enzyme from Methylovorus mays no. 9 in respect to utilization of theanine production
    • Yamamoto, S., Wakayama, M. Tachiki, T. (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
  • 65
    • 38549120647 scopus 로고    scopus 로고
    • Cloning and expression of Methylovorus mays No. 9 gene encoding γ-glutamylmethylamide synthetase: An enzyme usable in theanine formation by coupling with the alcoholic fermentation system of Baker's yeast
    • Yamamoto, S., Wakayama, M. Tachiki, T. (2008) Cloning and expression of Methylovorus mays No. 9 gene encoding γ-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
  • 66
    • 62249104385 scopus 로고    scopus 로고
    • Liquid chromatography-tandem quadrupole mass spectrometry and comprehensive two-dimensional gas chromatography-time-of-flight mass spectrometry measurement of targeted metabolites of Methylobacterium extorquens AM1 grown on two different carbon sources
    • Yang, S., Sadilek, M., Synovec, R.E. Lidstrom, M.E. (2009) Liquid chromatography-tandem quadrupole mass spectrometry and comprehensive two-dimensional gas chromatography-time-of-flight mass spectrometry measurement of targeted metabolites of Methylobacterium extorquens AM1 grown on two different carbon sources. J Chromatogr 1216 : 3280 3289.
    • (2009) J Chromatogr , vol.1216 , pp. 3280-3289
    • Yang, S.1    Sadilek, M.2    Synovec, R.E.3    Lidstrom, M.E.4
  • 67
    • 0031894048 scopus 로고    scopus 로고
    • Impairment of methylamine clearance in uremic patients and its nephropathological implications
    • Yu, P.H. Dyck, R.F. (1998) Impairment of methylamine clearance in uremic patients and its nephropathological implications. Clin Nephrol 49 : 299 302.
    • (1998) Clin Nephrol , vol.49 , pp. 299-302
    • Yu, P.H.1    Dyck, R.F.2
  • 68
    • 0027254762 scopus 로고
    • Cloning, sequencing, expression, and regulation of the structural gene for the copper/topa quinone-containing methylamine oxidase from Arthrobacter strain P1, a gram-positive facultative methylotroph
    • Zhang, X., Fuller, J.H. McIntire, W.S. (1993) Cloning, sequencing, expression, and regulation of the structural gene for the copper/topa quinone-containing 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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