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Volumn 178, Issue 22, 1996, Pages 6599-6607

Sequence and transcript analysis of a novel Methanosarcina barkeri methyltransferase II homolog and its associated corrinoid protein homologous to methionine synthase

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; COBALAMIN; CORRINOID; MESSENGER RNA; METHANOL; METHIONINE SYNTHASE; METHYLTRANSFERASE; TRIMETHYLAMINE; UROPORPHYRINOGEN DECARBOXYLASE;

EID: 0029961504     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.22.6599-6607.1996     Document Type: Article
Times cited : (45)

References (63)
  • 2
    • 0024364303 scopus 로고
    • Cloning and sequence analysis of the Escherichia coli metH gene encoding cobalamin-dependent methionine synthase and isolation of a tryptic fragment containing the cobalamin-binding domain
    • Banerjee, R. V., N. L. Johnston, J. K. Sobeski, P. Datta, and R. G. Matthews. 1989. Cloning and sequence analysis of the Escherichia coli metH gene encoding cobalamin-dependent methionine synthase and isolation of a tryptic fragment containing the cobalamin-binding domain. J. Biol. Chem. 264:13888-13895.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13888-13895
    • Banerjee, R.V.1    Johnston, N.L.2    Sobeski, J.K.3    Datta, P.4    Matthews, R.G.5
  • 3
    • 0026613773 scopus 로고
    • 5-methyl-tetrahydrometh-anopterin:coenzyme M methyltransferase of Methanosarcina strain G1 is an Na -translocating membrane protein
    • 5-methyl-tetrahydrometh-anopterin:coenzyme M methyltransferase of Methanosarcina strain G1 is an Na -translocating membrane protein. J. Bacteriol. 174:7656-7660.
    • (1992) J. Bacteriol. , vol.174 , pp. 7656-7660
    • Becher, B.1    Müller, V.2    Gottschalk, G.3
  • 5
    • 0028097631 scopus 로고
    • Pyruvate - A novel substrate for growth and methane formation in Methanosarcina barkeri
    • Bock, A.-K., A. Prieger-Kraft, and P. Schönheit. 1994. Pyruvate - a novel substrate for growth and methane formation in Methanosarcina barkeri. Arch. Microbiol. 161:33-46.
    • (1994) Arch. Microbiol. , vol.161 , pp. 33-46
    • Bock, A.-K.1    Prieger-Kraft, A.2    Schönheit, P.3
  • 7
  • 8
    • 0028983268 scopus 로고
    • Involvement of the "A" isozyme of methyltransferase II and the 29-kilodalton corrinoid protein in methanogenesis from monomethylamine
    • Burke, S. A., and J. A. Krzycki. 1995. Involvement of the "A" isozyme of methyltransferase II and the 29-kilodalton corrinoid protein in methanogenesis from monomethylamine. J. Bacteriol. 177:4410-4416.
    • (1995) J. Bacteriol. , vol.177 , pp. 4410-4416
    • Burke, S.A.1    Krzycki, J.A.2
  • 9
    • 0026095323 scopus 로고
    • Acetate-dependent methylation of two corrinoid proteins in extracts of Methanosarcina barkeri
    • Cao, X., and J. A. Krzycki. 1991. Acetate-dependent methylation of two corrinoid proteins in extracts of Methanosarcina barkeri. J. Bacteriol. 173:5439-5448.
    • (1991) J. Bacteriol. , vol.173 , pp. 5439-5448
    • Cao, X.1    Krzycki, J.A.2
  • 10
    • 67349114624 scopus 로고
    • Biochemistry of methanogenesis
    • M. Kates, D. J. Kushner, and A. T. Matheson (ed.). Elsevier Science Publishing, Inc., New York
    • Daniels, L. 1993. Biochemistry of methanogenesis, p. 41-112. In M. Kates, D. J. Kushner, and A. T. Matheson (ed.), The biochemistry of Archaea (Archaebacteria). Elsevier Science Publishing, Inc., New York.
    • (1993) The Biochemistry of Archaea (Archaebacteria) , pp. 41-112
    • Daniels, L.1
  • 12
    • 85035177539 scopus 로고    scopus 로고
    • Reconstitution of trimethylamine-dependent CoM methylation with the trimethylamine corrinoid protein (TCP) and the isozymes of methyltransferase II from Methanosarcina barkeri
    • Submitted for publication
    • Ferguson, D. J., and J. A. Krzycki. Reconstitution of trimethylamine-dependent CoM methylation with the trimethylamine corrinoid protein (TCP) and the isozymes of methyltransferase II from Methanosarcina barkeri. J. Bacteriol. Submitted for publication.
    • J. Bacteriol.
    • Ferguson, D.J.1    Krzycki, J.A.2
  • 13
    • 0029864728 scopus 로고    scopus 로고
    • Specific roles of methylcobamide:coenzyme M methyltransferase isozymes in metabolism of methanol and methylamines in Methanosarcina barkeri
    • Ferguson, D. J., J. A. Krzycki, and D. A. Grahame. 1996. Specific roles of methylcobamide:coenzyme M methyltransferase isozymes in metabolism of methanol and methylamines in Methanosarcina barkeri. J. Biol. Chem. 271:5189-5194.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5189-5194
    • Ferguson, D.J.1    Krzycki, J.A.2    Grahame, D.A.3
  • 15
    • 0026801609 scopus 로고
    • Methane from acetate
    • Ferry, J. G. 1992. Methane from acetate. J. Bacteriol. 174:5489-5495.
    • (1992) J. Bacteriol. , vol.174 , pp. 5489-5495
    • Ferry, J.G.1
  • 16
    • 0026608549 scopus 로고
    • Fermentation of methanetbiol and dimethylsulfide by A newly isolated methanogenic bacterium
    • Finster, K., Y. Tanimoto, and F. Bak. 1992. Fermentation of methanetbiol and dimethylsulfide by A newly isolated methanogenic bacterium. Arch. Microbiol. 157:425-430.
    • (1992) Arch. Microbiol. , vol.157 , pp. 425-430
    • Finster, K.1    Tanimoto, Y.2    Bak, F.3
  • 17
    • 0026578588 scopus 로고
    • Uroporphyrinogen decarboxylase in Saccharomyces cerevisiae. hem12 gene sequence and evidence for two conserved glycines essential for enzymatic activity
    • Garey, J. R., R. Labbe-Bois, A. Chelstowska, J. Rytka, L. Harrison, J. Kushner, and P. Labbe. 1993. Uroporphyrinogen decarboxylase in Saccharomyces cerevisiae. hem12 gene sequence and evidence for two conserved glycines essential for enzymatic activity. Eur. J. Biochem. 205:1011-1016.
    • (1993) Eur. J. Biochem. , vol.205 , pp. 1011-1016
    • Garey, J.R.1    Labbe-Bois, R.2    Chelstowska, A.3    Rytka, J.4    Harrison, L.5    Kushner, J.6    Labbe, P.7
  • 18
    • 0028172838 scopus 로고
    • 5-Methyltetrahydromethanopterin:coenzyme M methyltransferase from Methanobacterium thermoautotrophicum, catalytic mechanism and sodium ion dependence
    • 5-Methyltetrahydromethanopterin:coenzyme M methyltransferase from Methanobacterium thermoautotrophicum, catalytic mechanism and sodium ion dependence. Eur. J. Biochem. 226:465-472.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 465-472
    • Gärtner, P.1    Weiss, D.S.2    Harms, U.3    Thauer, R.K.4
  • 19
    • 0024962345 scopus 로고
    • Different isozymes of methylcobalamin:2-mercaptoethanesulfonate methyltransferase predominate in methanol-versus acetate-grown Methanosarcina barkeri
    • Grahame, D. A. 1989. Different isozymes of methylcobalamin:2-mercaptoethanesulfonate methyltransferase predominate in methanol-versus acetate-grown Methanosarcina barkeri. J. Biol. Chem. 264:12890-12894.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12890-12894
    • Grahame, D.A.1
  • 20
    • 0025787641 scopus 로고
    • Catalysis of acetyl-CoA cleavage and tetrahydrosarcinapterin methylation by a carbon monoxide dehydrogenase-corrinoid enzyme complex
    • Grahame, D. A. 1991. Catalysis of acetyl-CoA cleavage and tetrahydrosarcinapterin methylation by a carbon monoxide dehydrogenase-corrinoid enzyme complex. J. Biol. Chem. 266:22227-22233.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22227-22233
    • Grahame, D.A.1
  • 21
    • 0026676696 scopus 로고
    • Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes
    • Hansson, M., and L. Hederstedt. 1992. Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes. J. Bacteriol. 174:8081-8093.
    • (1992) J. Bacteriol. , vol.174 , pp. 8081-8093
    • Hansson, M.1    Hederstedt, L.2
  • 22
    • 0029671414 scopus 로고    scopus 로고
    • Methylcobalamin:coenzyme M methyltransferase isoenzymes MtaA and MtbA from Methanosarcina barkeri. Cloning, sequencing and differential transcription of the encoding genes and functional overexpression of the mtaA gene in Escherichia coli
    • Harms, U., and R. K. Thauer. 1996. Methylcobalamin:coenzyme M methyltransferase isoenzymes MtaA and MtbA from Methanosarcina barkeri. Cloning, sequencing and differential transcription of the encoding genes and functional overexpression of the mtaA gene in Escherichia coli. Eur. J. Biochem. 235:653-659.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 653-659
    • Harms, U.1    Thauer, R.K.2
  • 23
    • 0028988304 scopus 로고
    • 5-methyltetrahydromethanopterin:coenzyme M methyltransferase complex from Methanobacterium thermoautotrophicum is composed of eight different subunits
    • 5-methyltetrahydromethanopterin:coenzyme M methyltransferase complex from Methanobacterium thermoautotrophicum is composed of eight different subunits. Eur. J. Biochem. 228:640-648.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 640-648
    • Harms, U.1    Weiss, D.S.2    Gärtner, P.3    Linder, D.4    Thauer, R.K.5
  • 24
    • 0026343173 scopus 로고
    • Control regions of an archael gene: A TATA box and an initiator element promote cell-free transcription of the tRNA(val) gene of Methanococcus vannielii
    • Hausner, W., G. Frey, and M. Thomm. 1991. Control regions of an archael gene: a TATA box and an initiator element promote cell-free transcription of the tRNA(val) gene of Methanococcus vannielii. J. Mol. Biol. 222:495-508.
    • (1991) J. Mol. Biol. , vol.222 , pp. 495-508
    • Hausner, W.1    Frey, G.2    Thomm, M.3
  • 25
    • 0021253525 scopus 로고
    • Unidirectional digestion with exonuclease III creates targeted break points for DNA sequencing
    • Henikoff, S. 1984. Unidirectional digestion with exonuclease III creates targeted break points for DNA sequencing. Gene 28:351-359.
    • (1984) Gene , vol.28 , pp. 351-359
    • Henikoff, S.1
  • 26
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • Henikoff, S., and J. G. Henikoff. 1992. Amino acid substitution matrices from protein blocks. Proc. Natl. Acad. Sci. USA 89:10915-10919.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10915-10919
    • Henikoff, S.1    Henikoff, J.G.2
  • 27
    • 0028306092 scopus 로고
    • mRNAs in the methanogenic archaeon Methanococcus vannielii: Numbers, halt-lives, and processing
    • Hennigan, A. N., and J. N. Reeve. 1994. mRNAs in the methanogenic archaeon Methanococcus vannielii: numbers, halt-lives, and processing. Mol. Microbiol. 11:655-670.
    • (1994) Mol. Microbiol. , vol.11 , pp. 655-670
    • Hennigan, A.N.1    Reeve, J.N.2
  • 28
    • 0025675856 scopus 로고
    • High efficiency transformation of Escherichia coli with plasmids
    • Inoue, H., H. Nojima, and H. Okayama. 1990. High efficiency transformation of Escherichia coli with plasmids. Gene 96:23-28.
    • (1990) Gene , vol.96 , pp. 23-28
    • Inoue, H.1    Nojima, H.2    Okayama, H.3
  • 29
    • 0026503633 scopus 로고
    • Isolation of a 5-hydroxybenzimidazolyl cobamide-containing enzyme involved in the methyltetrahydromethanopterin: Coenzyme M methyltransferase reaction in Methanobacterium thermoautoirophicum
    • Kengen, S. W. M., P. J. H. Daas, E. F. G. Duits, J. T. Keltjens, C. van der Drift, and G. D. Vogels. 1992. Isolation of a 5-hydroxybenzimidazolyl cobamide-containing enzyme involved in the methyltetrahydromethanopterin: coenzyme M methyltransferase reaction in Methanobacterium thermoautoirophicum. Biochim. Biophys. Acta 1118:249-260.
    • (1992) Biochim. Biophys. Acta , vol.1118 , pp. 249-260
    • Kengen, S.W.M.1    Daas, P.J.H.2    Duits, E.F.G.3    Keltjens, J.T.4    Van der Drift, C.5    Vogels, G.D.6
  • 30
    • 0026679249 scopus 로고
    • Nucleotide sequence of the Synechococcus sp. PCC7942 hemE gene encoding the homologue of mammalian uroporphyrinogen decarboxylase
    • Kiel, J., A. A. M. Ten Berge, and G. Venema. 1992. Nucleotide sequence of the Synechococcus sp. PCC7942 hemE gene encoding the homologue of mammalian uroporphyrinogen decarboxylase. DNA Seq. 2:415-418.
    • (1992) DNA Seq. , vol.2 , pp. 415-418
    • Kiel, J.1    Ten Berge, A.A.M.2    Venema, G.3
  • 31
    • 0028587252 scopus 로고
    • Simple methods for preparation of plasmid DNA yielding long and accurate sequence data
    • Kovalenko, S. A., M. Tanaka, and T. Ozawa. 1994. Simple methods for preparation of plasmid DNA yielding long and accurate sequence data. Nucleic Acids Res. 22:5771-5772.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5771-5772
    • Kovalenko, S.A.1    Tanaka, M.2    Ozawa, T.3
  • 32
    • 0027952994 scopus 로고
    • Differential in vitro methylation and synthesis of the 480-kilodalton corrinoid protein in Methanosarcina barkeri grown on different substrates
    • Kremer, J., S. Burchfield, C. Frazier, and J. Krzycki. 1994. Differential in vitro methylation and synthesis of the 480-kilodalton corrinoid protein in Methanosarcina barkeri grown on different substrates. J. Bacteriol. 176:253-255.
    • (1994) J. Bacteriol. , vol.176 , pp. 253-255
    • Kremer, J.1    Burchfield, S.2    Frazier, C.3    Krzycki, J.4
  • 33
    • 0027305651 scopus 로고
    • Isolation of two novel corrinoid proteins from acetate-grown Methanosarcina barkeri
    • Kremer, J. D., X. Cao, and J. Krzycki. 1993. Isolation of two novel corrinoid proteins from acetate-grown Methanosarcina barkeri. J. Bacteriol. 175:4824-4833.
    • (1993) J. Bacteriol. , vol.175 , pp. 4824-4833
    • Kremer, J.D.1    Cao, X.2    Krzycki, J.3
  • 34
    • 0028430175 scopus 로고
    • Identification of a light-responsive region of the nuclear gene encoding the B subunit of chloroplast glyceraldehyde 3-phosphate dehydrogenase from Arabidopsis thaliana
    • Kwon, H.-B., S.-C. Park, H.-P. Peng, H. M. Goodman, J. Dewdney, and M.-C. Shih. 1994. Identification of a light-responsive region of the nuclear gene encoding the B subunit of chloroplast glyceraldehyde 3-phosphate dehydrogenase from Arabidopsis thaliana. Plant Physiol. 105:357-367.
    • (1994) Plant Physiol. , vol.105 , pp. 357-367
    • Kwon, H.-B.1    Park, S.-C.2    Peng, H.-P.3    Goodman, H.M.4    Dewdney, J.5    Shih, M.-C.6
  • 35
    • 0029744528 scopus 로고    scopus 로고
    • Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri: Physicochemical characterization, cloning, sequence analysis, and heterologous gene expression
    • LeClerc, G. M., and D. A. Grahame. 1996. Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri: physicochemical characterization, cloning, sequence analysis, and heterologous gene expression. J. Biol. Chem. 271:18725-18731.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18725-18731
    • LeClerc, G.M.1    Grahame, D.A.2
  • 36
    • 0029004286 scopus 로고
    • 5-methyltetrahydromethanopterin:coenzyme M methyltransferase from Methanosarcina mazei Göl
    • 5-methyltetrahydromethanopterin:coenzyme M methyltransferase from Methanosarcina mazei Göl. J. Bacteriol. 177:2245-2250.
    • (1995) J. Bacteriol. , vol.177 , pp. 2245-2250
    • Lu, W.-P.1    Becher, B.2    Gottschalk, G.3    Ragsdale, S.W.4
  • 37
    • 0026701740 scopus 로고
    • Cloning and sequencing of glutamate mutase component S from Clostridium tetanamorphum
    • Marsh, E. N. G., and D. E. Holloway. 1992. Cloning and sequencing of glutamate mutase component S from Clostridium tetanamorphum. FEBS Lett. 310:167-170.
    • (1992) FEBS Lett. , vol.310 , pp. 167-170
    • Marsh, E.N.G.1    Holloway, D.E.2
  • 38
    • 0027513016 scopus 로고
    • Identification of a complex operator for galP1, the glucose-sensitive, galactose-dependent promoter of the Streptomyces galactose operon
    • Mattern, S. G., M. E. Brawner, and J. Westpheling. 1993. Identification of a complex operator for galP1, the glucose-sensitive, galactose-dependent promoter of the Streptomyces galactose operon. J. Bacteriol. 175:1213-1220.
    • (1993) J. Bacteriol. , vol.175 , pp. 1213-1220
    • Mattern, S.G.1    Brawner, M.E.2    Westpheling, J.3
  • 39
    • 0030058857 scopus 로고    scopus 로고
    • Characterization of the cdhD and cdhE genes encoding subunits of the corrinoid/iron-sulfur enzyme of the CO dehydrogenase complex from Methanosarcina thermophila
    • Maupin-Furlow, J., and J. G. Ferry. 1996. Characterization of the cdhD and cdhE genes encoding subunits of the corrinoid/iron-sulfur enzyme of the CO dehydrogenase complex from Methanosarcina thermophila. J. Bacteriol. 178:340-346.
    • (1996) J. Bacteriol. , vol.178 , pp. 340-346
    • Maupin-Furlow, J.1    Ferry, J.G.2
  • 40
    • 0025984345 scopus 로고
    • A generally applicable technique for the extraction of restrictable DNA from methanogenic bacteria
    • Meakin, S. A., J. H. Nash, W. D. Murray, K. J. Kennedy, and G. D. Sprott. 1991. A generally applicable technique for the extraction of restrictable DNA from methanogenic bacteria. J. Microbiol. Methods 14:119-126.
    • (1991) J. Microbiol. Methods , vol.14 , pp. 119-126
    • Meakin, S.A.1    Nash, J.H.2    Murray, W.D.3    Kennedy, K.J.4    Sprott, G.D.5
  • 41
    • 0024040211 scopus 로고
    • Conservation of structure in the human gene encoding argininosuccinate synthetase and the argG genes of the archaebacteria Methanosarcina barkeri MS and Methanococcus vannielii
    • Morris, C. J., and J. N. Reeve. 1988. Conservation of structure in the human gene encoding argininosuccinate synthetase and the argG genes of the archaebacteria Methanosarcina barkeri MS and Methanococcus vannielii. J. Bacteriol. 170:3125-3130.
    • (1988) J. Bacteriol. , vol.170 , pp. 3125-3130
    • Morris, C.J.1    Reeve, J.N.2
  • 42
    • 0027525607 scopus 로고
    • Cloning and sequencing of the hemE gene encoding uroporphyrinogen III decarboxylase (UPD) from Escherichia coli K-12
    • Nishimura, K., T. Nakayashiki, and H. Inokuchi. 1993. Cloning and sequencing of the hemE gene encoding uroporphyrinogen III decarboxylase (UPD) from Escherichia coli K-12. Gene 133:109-113.
    • (1993) Gene , vol.133 , pp. 109-113
    • Nishimura, K.1    Nakayashiki, T.2    Inokuchi, H.3
  • 43
    • 0028593509 scopus 로고
    • Protein superfamilies and domain superfolds
    • Orengo, C. A., D. T. Jones, and J. M. Thornton. 1994. Protein superfamilies and domain superfolds. Nature (London) 372:631-634.
    • (1994) Nature (London) , vol.372 , pp. 631-634
    • Orengo, C.A.1    Jones, D.T.2    Thornton, J.M.3
  • 44
    • 0028908091 scopus 로고
    • In vivo definition of an archael promoter
    • Palmer, J. R., and C. J. Daniels. 1995. In vivo definition of an archael promoter. J. Bacteriol. 177:1844-1849.
    • (1995) J. Bacteriol. , vol.177 , pp. 1844-1849
    • Palmer, J.R.1    Daniels, C.J.2
  • 45
    • 0027993193 scopus 로고
    • 5-methyltetrahydromethanopterin:coenzyme M methyltransferase in Methanobacterium thermoautotrophicum ΔH
    • 5-methyltetrahydromethanopterin:coenzyme M methyltransferase in Methanobacterium thermoautotrophicum ΔH. J. Bacteriol. 176:6384-6391.
    • (1994) J. Bacteriol. , vol.176 , pp. 6384-6391
    • Pihl, T.D.1    Sharma, S.2    Reeve, J.N.3
  • 46
    • 0020494046 scopus 로고
    • Corrinoids from Methanosarcina barkeri: Structure of the α-ligand
    • Pol, A., C. van der Drift, and G. D. Vogels. 1982. Corrinoids from Methanosarcina barkeri: structure of the α-ligand. Biochem. Biophys. Res. Commun. 108:731-737.
    • (1982) Biochem. Biophys. Res. Commun. , vol.108 , pp. 731-737
    • Pol, A.1    Van der Drift, C.2    Vogels, G.D.3
  • 47
    • 0026732105 scopus 로고
    • Molecular biology of methanogens
    • Reeve, J. N. 1992. Molecular biology of methanogens. Annu. Rev. Microbiol. 46:165-191.
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 165-191
    • Reeve, J.N.1
  • 48
    • 0026063256 scopus 로고
    • Isolation of chromosomal DNA from a methanogenic Archaebactcria using a french pressure cell press
    • Rinker, A. G., Jr., and D. R. Evans. 1991. Isolation of chromosomal DNA from a methanogenic Archaebactcria using a french pressure cell press. BioTechniques 11:612-613.
    • (1991) BioTechniques , vol.11 , pp. 612-613
    • Rinker Jr., A.G.1    Evans, D.R.2
  • 50
    • 0028922177 scopus 로고
    • Transcriptional regulation of the phosphotransacetylase-encoding and acetate kinase-encoding genes (pta and ack) from Methanosarcina thermophila
    • Singh-Wissmann, K., and J. G. Ferry. 1995. Transcriptional regulation of the phosphotransacetylase-encoding and acetate kinase-encoding genes (pta and ack) from Methanosarcina thermophila. J. Bacteriol. 177:1699-1702.
    • (1995) J. Bacteriol. , vol.177 , pp. 1699-1702
    • Singh-Wissmann, K.1    Ferry, J.G.2
  • 51
    • 0019887799 scopus 로고
    • Identification of common molecular subsequences
    • Smith, T. F., and M. S. Waterman. 1981. Identification of common molecular subsequences. J. Mol. Biol. 147:195-197.
    • (1981) J. Mol. Biol. , vol.147 , pp. 195-197
    • Smith, T.F.1    Waterman, M.S.2
  • 52
    • 0028218683 scopus 로고
    • The modular arrangement of proteins as inferred from analysis of homology
    • Sonnhammer, E. L., and D. Kahn. 1994. The modular arrangement of proteins as inferred from analysis of homology. Protein Sci. 3:482-492.
    • (1994) Protein Sci. , vol.3 , pp. 482-492
    • Sonnhammer, E.L.1    Kahn, D.2
  • 53
    • 0027504341 scopus 로고
    • 5-methyltetrahydromethanopterin:coenzyme M methyltransferase from Methanobacterium thermoautotrophicum
    • 5-methyltetrahydromethanopterin:coenzyme M methyltransferase from Methanobacterium thermoautotrophicum. Eur. J. Biochem. 217:115-121.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 115-121
    • Stupperich, E.1    Juza, A.2    Hoppert, M.3    Mayer, F.4
  • 54
    • 85035182499 scopus 로고    scopus 로고
    • Manuscript in preparation
    • Tallant, T., and J. Krzycki. Manuscript in preparation.
    • Tallant, T.1    Krzycki, J.2
  • 55
    • 0029935034 scopus 로고    scopus 로고
    • Coenzyme M methylase activity of the 480-kilodalton corrinoid protein from Methanosarcina barkeri
    • Tallant, T. C., and J. A. Krzycki. 1996. Coenzyme M methylase activity of the 480-kilodalton corrinoid protein from Methanosarcina barkeri. J. Bacteriol. 178:1295-1301.
    • (1996) J. Bacteriol. , vol.178 , pp. 1295-1301
    • Tallant, T.C.1    Krzycki, J.A.2
  • 56
    • 0027946485 scopus 로고
    • Anaerobic degradation of tetramethylammonium by a newly isolated marine methanogen
    • Tanaka, K. 1994. Anaerobic degradation of tetramethylammonium by a newly isolated marine methanogen. J. Ferment. Bioeng. 78:386-388.
    • (1994) J. Ferment. Bioeng. , vol.78 , pp. 386-388
    • Tanaka, K.1
  • 57
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 59
    • 0021684111 scopus 로고
    • Purification and properties of methanol:5-hydroxybenzimidazolylcobamide methyltransferase from Methanosarcina barkeri
    • van der Meijden, P., B. W. te Brömmelstroet, C. M. Poirot, C. van der Drift, and G. D. Vogels. 1984. Purification and properties of methanol:5-hydroxybenzimidazolylcobamide methyltransferase from Methanosarcina barkeri. J. Bacteriol. 160:629-635.
    • (1984) J. Bacteriol. , vol.160 , pp. 629-635
    • Van der Meijden, P.1    Te Brömmelstroet, B.W.2    Poirot, C.M.3    Van der Drift, C.4    Vogels, G.D.5
  • 60
    • 0028587832 scopus 로고
    • 5-methyltetrahydromethanopterin:coenzyme M methyltransferase studied with cob(I)alamin as methyl acceptor and methylcob(III)alamin as methyl donor
    • 5-methyltetrahydromethanopterin:coenzyme M methyltransferase studied with cob(I)alamin as methyl acceptor and methylcob(III)alamin as methyl donor. Eur. J. Biochem. 226:799-809.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 799-809
    • Weiss, D.S.1    Gärtner, P.2    Thauer, R.K.3
  • 62
    • 0027157321 scopus 로고
    • Function of methylcobalamin:coenzyme M methyltransferase isoenzyme II in Methanosarcina barkeri
    • Yeliseev, A., P. Gärtner, U. Harms, D. Linder, and R. K. Thauer. 1993. Function of methylcobalamin:coenzyme M methyltransferase isoenzyme II in Methanosarcina barkeri. Arch. Microbiol. 159:530-536.
    • (1993) Arch. Microbiol. , vol.159 , pp. 530-536
    • Yeliseev, A.1    Gärtner, P.2    Harms, U.3    Linder, D.4    Thauer, R.K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.