메뉴 건너뛰기




Volumn 264, Issue 1, 1999, Pages 242-249

Properties of the methylcobalamin:H4folate methyltransferase involved in chloromethane utilization by Methylobacteriurn sp. strain CM4

Author keywords

Chloromethane; Dehalogenation; Methylobacterium; Methyltransferase; Tetrahydrofol ate

Indexed keywords

5 METHYLTETRAHYDROFOLATE HOMOCYSTEINE METHYLTRANSFERASE; MECOBALAMIN; METHYL CHLORIDE; PRIMER DNA; PROTEIN METHYLTRANSFERASE; RECOMBINANT PROTEIN;

EID: 0033566374     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00629.x     Document Type: Article
Times cited : (38)

References (29)
  • 1
    • 0030246889 scopus 로고    scopus 로고
    • Isolation and initial characterization of aerobic chloromethane-utilizing bacteria
    • 1. Doronina, N.V., Sokolov, A.P. & Trotsenko, Y.A. (1996) Isolation and initial characterization of aerobic chloromethane-utilizing bacteria. FEMS Microbiol. Lett. 142, 179-183.
    • (1996) FEMS Microbiol. Lett. , vol.142 , pp. 179-183
    • Doronina, N.V.1    Sokolov, A.P.2    Trotsenko, Y.A.3
  • 3
    • 0033551086 scopus 로고    scopus 로고
    • A corrinoid-dependent catabolic pathway for growth of a Methylobacterium strain with chloromethane
    • 3. 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. USA 96, 4615-4620.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 4615-4620
    • Vannelli, T.1    Messmer, M.2    Studer, A.3    Vuilleumier, S.4    Leisinger, T.5
  • 4
    • 0031799184 scopus 로고    scopus 로고
    • Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine
    • 4. Burke, S.A., Lo, S.L. & Krzycki, J.A. (1998) Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine. J. Bacteriol. 180, 3432-3440.
    • (1998) J. Bacteriol. , vol.180 , pp. 3432-3440
    • Burke, S.A.1    Lo, S.L.2    Krzycki, J.A.3
  • 5
    • 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
    • 5. Harms, U. & Thauer, R.K. (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, 653-639.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 653-1639
    • Harms, U.1    Thauer, R.K.2
  • 6
    • 0029864728 scopus 로고    scopus 로고
    • Specific roles of methylcobamide: Coenzyme M methyltransferase isozymes in metabolism of methanol and methylamines in Methanosarcina barkeri
    • 6. Ferguson, D.J. Jr, Krzycki, J.A. & Grahame, D.A. (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., Jr.1    Krzycki, J.A.2    Grahame, D.A.3
  • 7
    • 0031024751 scopus 로고    scopus 로고
    • Methanol: Coenzyme M methyltransferase from Methanosarcina barkeri. Purification, properties and encoding genes of the corrinoid protein MTI
    • 7. Sauer, K., Harms, U. & Thauer, R.K. (1997) Methanol: coenzyme M methyltransferase from Methanosarcina barkeri. Purification, properties and encoding genes of the corrinoid protein MTI. Eur. J. Biochem. 243, 670-677.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 670-677
    • Sauer, K.1    Harms, U.2    Thauer, R.K.3
  • 8
    • 0032080155 scopus 로고    scopus 로고
    • O-demethylase from Acetobacterium dehalogenans: Substrate specificity and function of the participating proteins
    • 8. Kaufmann, F., Wohlfarth, G. & Diekert, G. (1998) O-demethylase from Acetobacterium dehalogenans: substrate specificity and function of the participating proteins. Eur. J. Biochem. 253, 706-711.
    • (1998) Eur. J. Biochem. , vol.253 , pp. 706-711
    • Kaufmann, F.1    Wohlfarth, G.2    Diekert, G.3
  • 9
    • 0031679835 scopus 로고    scopus 로고
    • The NADP-dependent methylene tetrahydromethanopterin dehydrogenase in Methylobacterium extorquens AMI
    • 9. Vorholt, J.A., Chistoserdova, L., Lidstrom, M.E. & Thauer, R.K. (1998) The NADP-dependent methylene tetrahydromethanopterin dehydrogenase in Methylobacterium extorquens AMI. J. Bacteriol. 180, 5351 -5356.
    • (1998) J. Bacteriol. , vol.180 , pp. 5351-5356
    • Vorholt, J.A.1    Chistoserdova, L.2    Lidstrom, M.E.3    Thauer, R.K.4
  • 13
    • 0025045678 scopus 로고
    • Purification and properties of a NADH-dependent 5,10-methylenetetrahydrofolate reductase from Peptostreptococcus productus
    • 13. Wohlfarth, G., Geerligs, G. & Diekert, G. (1990) Purification and properties of a NADH-dependent 5,10-methylenetetrahydrofolate reductase from Peptostreptococcus productus. Eur. J. Biochem. 192, 411-417.
    • (1990) Eur. J. Biochem. , vol.192 , pp. 411-417
    • Wohlfarth, G.1    Geerligs, G.2    Diekert, G.3
  • 14
    • 0028670448 scopus 로고
    • O-demethylation by the homoacetogenic anaerobe Holophaga foetida studied by a new photometric methylation assay using electrochemically produced cob(I)alamin
    • 14. Kreft, J.U. & Schink, B. (1994) O-demethylation by the homoacetogenic anaerobe Holophaga foetida studied by a new photometric methylation assay using electrochemically produced cob(I)alamin. Eur. J. Biochem. 226, 945-951.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 945-951
    • Kreft, J.U.1    Schink, B.2
  • 15
    • 0027377502 scopus 로고
    • Methyl chloride metabolism of strictly anaerobic, methyl chloride-utilizing homoacetogen strain MC
    • 15. Messmer, M., Wohlfarth, G. & Diekert, G. (1993) Methyl chloride metabolism of strictly anaerobic, methyl chloride-utilizing homoacetogen strain MC. Arch. Microbiol. 160, 383-387.
    • (1993) Arch. Microbiol. , vol.160 , pp. 383-387
    • Messmer, M.1    Wohlfarth, G.2    Diekert, G.3
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 16. Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 17
    • 0032479058 scopus 로고    scopus 로고
    • C1 transfer enzymes and coenzymes linking methylotrophic bacteria and methanogenic Archaea
    • 17. Chistoserdova, L., Vorholt, J.A., Thauer, R.K. & Lidstrom, M.E. (1998) C1 transfer enzymes and coenzymes linking methylotrophic bacteria and methanogenic Archaea. Science 281, 99-102.
    • (1998) Science , vol.281 , pp. 99-102
    • Chistoserdova, L.1    Vorholt, J.A.2    Thauer, R.K.3    Lidstrom, M.E.4
  • 18
    • 0022388672 scopus 로고
    • Methyl transfer from methylcobalamin to thiols. A reinvestigation
    • 18. Hogenkamp, H.P.C., Bratt, G.T. & Sun, S. (1985) Methyl transfer from methylcobalamin to thiols. A reinvestigation. Biochemistry 24, 6428-6432.
    • (1985) Biochemistry , vol.24 , pp. 6428-6432
    • Hogenkamp, H.P.C.1    Bratt, G.T.2    Sun, S.3
  • 19
    • 0029744528 scopus 로고    scopus 로고
    • Methylcobamide: Coenzyme M methyltransferase isoenzymes from Methanosarcina barkeri
    • 19. LeClerc, G.M. & Grahame, D.A. (1996) Methylcobamide: coenzyme M methyltransferase isoenzymes from Methanosarcina barkeri. J. Biol. Chem. 271, 18725-18731.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18725-18731
    • LeClerc, G.M.1    Grahame, D.A.2
  • 20
    • 0032919372 scopus 로고    scopus 로고
    • Recent improvements of the ProDom database of protein domain families
    • 20. Corpet, F., Gouzy, J. & Kahn, D. (1999) Recent improvements of the ProDom database of protein domain families. Nucleic Acids Res. 27, 263-267.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 263-267
    • Corpet, F.1    Gouzy, J.2    Kahn, D.3
  • 21
    • 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
  • 22
    • 0001961089 scopus 로고    scopus 로고
    • EPR spectroscopic evidence that in the energy conserving methyltransferase complex from methanogenic archea a histidine residue is ligated to the cobamide-cobalt
    • Kräutler, B., Arigoni, D. & Golding, B.T., eds. Wiley-VCH, Weinheim
    • 12-Proteins (Kräutler, B., Arigoni, D. & Golding, B.T., eds), pp. 157-165. Wiley-VCH, Weinheim.
    • (1998) 12-Proteins , pp. 157-165
    • Harms, U.1    Thauer, R.K.2
  • 24
    • 0030829339 scopus 로고    scopus 로고
    • Cobalamin-dependent methionine synthase is a modular protein with distinct regions for binding homocysteine, methyltetrahydrofolate, cobalamin and adenosylmethionine
    • 24. Goulding, C.W., Postigo, D. & Matthews, R.G. (1997) Cobalamin-dependent methionine synthase is a modular protein with distinct regions for binding homocysteine, methyltetrahydrofolate, cobalamin and adenosylmethionine. Biochemistry 36, 8082-8091.
    • (1997) Biochemistry , vol.36 , pp. 8082-8091
    • Goulding, C.W.1    Postigo, D.2    Matthews, R.G.3
  • 25
    • 0028075318 scopus 로고
    • The reductive acetyl coenzyme A pathway: Sequence and heterologous expression of active methyltetrahydrofolate: Corrinoid/iron-sulfur protein methyltransferase from Clostridium thermoaceticum
    • 25. Roberts, D.L., Zhao, S., Doukov, T. & Ragsdale, S.W. (1994) The reductive acetyl coenzyme A pathway: sequence and heterologous expression of active methyltetrahydrofolate: corrinoid/iron-sulfur protein methyltransferase from Clostridium thermoaceticum. J. Bacteriol. 176, 6127-6130.
    • (1994) J. Bacteriol. , vol.176 , pp. 6127-6130
    • Roberts, D.L.1    Zhao, S.2    Doukov, T.3    Ragsdale, S.W.4
  • 26
    • 0028846885 scopus 로고
    • Mechanistic studies of the methyltransferase from Clostridium thermoaceticum: Origin of the pH dependence of the methyl group transfer from methyltetrahydrofolate to the corrinoid/iron-sulfur protein
    • 26. Zhao, S., Roberts, D.L. & Ragsdale, S.W. (1995) Mechanistic studies of the methyltransferase from Clostridium thermoaceticum: origin of the pH dependence of the methyl group transfer from methyltetrahydrofolate to the corrinoid/iron-sulfur protein. Biochemistry 34, 15075-15083.
    • (1995) Biochemistry , vol.34 , pp. 15075-15083
    • Zhao, S.1    Roberts, D.L.2    Ragsdale, S.W.3
  • 27
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.