메뉴 건너뛰기




Volumn 164, Issue 1, 2009, Pages 1-8

Sleeping beauty mutase (sbm) is expressed and interacts with ygfd in Escherichia coli

Author keywords

Cobalamin; Methylmalonyl CoA mutase; Sbm; Vitamin B12; YgfD

Indexed keywords

BIOCHEMISTRY; FLOW INTERACTIONS; PROTEINS;

EID: 58149359198     PISSN: 09445013     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.micres.2008.08.006     Document Type: Article
Times cited : (22)

References (17)
  • 1
    • 0035813109 scopus 로고    scopus 로고
    • Identification of the human methylmalonyl-CoA racemase gene based on the analysis of prokaryotic gene arrangements. Implications for decoding the human genome
    • Bobik T.A., and Rasche M.E. Identification of the human methylmalonyl-CoA racemase gene based on the analysis of prokaryotic gene arrangements. Implications for decoding the human genome. J Biol Chem 276 (2001) 37194-37198
    • (2001) J Biol Chem , vol.276 , pp. 37194-37198
    • Bobik, T.A.1    Rasche, M.E.2
  • 2
    • 0037161282 scopus 로고    scopus 로고
    • Metabolic engineering of a methylmalonyl-CoA mutase-epimerase pathway for complex polyketide biosynthesis in Escherichia coli
    • Dayem L.C., Carney J.R., Santi D.V., Pfeifer B.A., Khosla C., and Kealey J.T. Metabolic engineering of a methylmalonyl-CoA mutase-epimerase pathway for complex polyketide biosynthesis in Escherichia coli. Biochemistry 41 (2002) 5193-5201
    • (2002) Biochemistry , vol.41 , pp. 5193-5201
    • Dayem, L.C.1    Carney, J.R.2    Santi, D.V.3    Pfeifer, B.A.4    Khosla, C.5    Kealey, J.T.6
  • 3
    • 0037180440 scopus 로고    scopus 로고
    • Identification of the gene responsible for the cblA complementation group of vitamin B12-responsive methylmalonic acidemia based on analysis of prokaryotic gene arrangements
    • Dobson C.M., Wai T., Leclerc D., Wilson A., Wu X., Dore C., et al. Identification of the gene responsible for the cblA complementation group of vitamin B12-responsive methylmalonic acidemia based on analysis of prokaryotic gene arrangements. Proc Natl Acad Sci USA 99 (2002) 15554-15559
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 15554-15559
    • Dobson, C.M.1    Wai, T.2    Leclerc, D.3    Wilson, A.4    Wu, X.5    Dore, C.6
  • 4
    • 58149353207 scopus 로고
    • The purification and properties of a factor containing vitamin B12 concerned in the synthesis of methionine by Escherichia coli
    • Foster M.A., Jones K.M., and Woods D.D. The purification and properties of a factor containing vitamin B12 concerned in the synthesis of methionine by Escherichia coli. Biochem J 80 (1961) 519-531
    • (1961) Biochem J , vol.80 , pp. 519-531
    • Foster, M.A.1    Jones, K.M.2    Woods, D.D.3
  • 5
    • 0013770829 scopus 로고
    • Two enzymic mechanisms for the methylation of homocysteine by extracts of Escherichia coli
    • Foster M.A., Tejerina G., Guest J.R., and Woods D.D. Two enzymic mechanisms for the methylation of homocysteine by extracts of Escherichia coli. Biochem J 92 (1964) 476-488
    • (1964) Biochem J , vol.92 , pp. 476-488
    • Foster, M.A.1    Tejerina, G.2    Guest, J.R.3    Woods, D.D.4
  • 7
    • 0013770818 scopus 로고
    • Transfer of the methyl group from N5-methyltetrahydrofolates to homocysteine in Escherichia coli
    • Guest J.R., Friedman S., Foster M.A., Tejerina G., and Woods D.D. Transfer of the methyl group from N5-methyltetrahydrofolates to homocysteine in Escherichia coli. Biochem J 92 (1964) 497-504
    • (1964) Biochem J , vol.92 , pp. 497-504
    • Guest, J.R.1    Friedman, S.2    Foster, M.A.3    Tejerina, G.4    Woods, D.D.5
  • 8
    • 0034712657 scopus 로고    scopus 로고
    • Discovering new enzymes and metabolic pathways: conversion of succinate to propionate by Escherichia coli
    • Haller T., Buckel T., Retey J., and Gerlt J.A. Discovering new enzymes and metabolic pathways: conversion of succinate to propionate by Escherichia coli. Biochemistry 39 (2000) 4622-4629
    • (2000) Biochemistry , vol.39 , pp. 4622-4629
    • Haller, T.1    Buckel, T.2    Retey, J.3    Gerlt, J.A.4
  • 9
    • 0019833645 scopus 로고
    • Specific-purpose plasmid cloning vectors. I. Low copy number, temperature-sensitive, mobilization-defective pSC101-derived containment vectors
    • Hashimoto-Gotoh T., Franklin F.C., Nordheim A., and Timmis K.N. Specific-purpose plasmid cloning vectors. I. Low copy number, temperature-sensitive, mobilization-defective pSC101-derived containment vectors. Gene 16 (1981) 227-235
    • (1981) Gene , vol.16 , pp. 227-235
    • Hashimoto-Gotoh, T.1    Franklin, F.C.2    Nordheim, A.3    Timmis, K.N.4
  • 10
    • 1842791547 scopus 로고    scopus 로고
    • MeaB is a component of the methylmalonyl-CoA mutase complex required for protection of the enzyme from inactivation
    • Korotkova N., and Lidstrom M.E. MeaB is a component of the methylmalonyl-CoA mutase complex required for protection of the enzyme from inactivation. J Biol Chem 279 (2004) 13652-13658
    • (2004) J Biol Chem , vol.279 , pp. 13652-13658
    • Korotkova, N.1    Lidstrom, M.E.2
  • 11
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • Leipe D.D., Wolf Y.I., Koonin E.V., and Aravind L. Classification and evolution of P-loop GTPases and related ATPases. J Mol Biol 317 (2002) 41-72
    • (2002) J Mol Biol , vol.317 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 12
    • 0024674238 scopus 로고
    • Subunit interactions in Propionibacterium shermanii methylmalonyl-CoA mutase studied by analytical ultracentrifugation
    • Marsh E.N., Harding S.E., and Leadlay P.F. Subunit interactions in Propionibacterium shermanii methylmalonyl-CoA mutase studied by analytical ultracentrifugation. Biochem J 260 (1989) 353-358
    • (1989) Biochem J , vol.260 , pp. 353-358
    • Marsh, E.N.1    Harding, S.E.2    Leadlay, P.F.3
  • 13
    • 0042158578 scopus 로고    scopus 로고
    • Purification and characterization of homodimeric methylmalonyl-CoA mutase from Sinorhizobium meliloti
    • Miyamoto E., Watanabe F., Charles T.C., Yamaji R., Inui H., and Nakano Y. Purification and characterization of homodimeric methylmalonyl-CoA mutase from Sinorhizobium meliloti. Arch Microbiol 180 (2003) 151-154
    • (2003) Arch Microbiol , vol.180 , pp. 151-154
    • Miyamoto, E.1    Watanabe, F.2    Charles, T.C.3    Yamaji, R.4    Inui, H.5    Nakano, Y.6
  • 14
    • 33745805484 scopus 로고    scopus 로고
    • Energetics of interaction between the G-protein chaperone, MeaB, and B12-dependent methylmalonyl-CoA mutase
    • Padovani D., Labunska T., and Banerjee R. Energetics of interaction between the G-protein chaperone, MeaB, and B12-dependent methylmalonyl-CoA mutase. J Biol Chem 281 (2006) 17838-17844
    • (2006) J Biol Chem , vol.281 , pp. 17838-17844
    • Padovani, D.1    Labunska, T.2    Banerjee, R.3
  • 15
    • 0026806201 scopus 로고
    • Physical map location of the new Escherichia coli gene sbm
    • Roy I., and Leadlay P.F. Physical map location of the new Escherichia coli gene sbm. J Bacteriol 174 (1992) 5763-5764
    • (1992) J Bacteriol , vol.174 , pp. 5763-5764
    • Roy, I.1    Leadlay, P.F.2
  • 16
    • 0344867896 scopus 로고    scopus 로고
    • High efficiency gene replacement in Salmonella enteritidis: chimeric fimbrins containing a T-cell epitope from Leishmania major
    • White A.P., Collinson S.K., Burian J., Clouthier S.C., Banser P.A., and Kay W.W. High efficiency gene replacement in Salmonella enteritidis: chimeric fimbrins containing a T-cell epitope from Leishmania major. Vaccine 17 (1999) 2150-2161
    • (1999) Vaccine , vol.17 , pp. 2150-2161
    • White, A.P.1    Collinson, S.K.2    Burian, J.3    Clouthier, S.C.4    Banser, P.A.5    Kay, W.W.6
  • 17
    • 34247241655 scopus 로고    scopus 로고
    • An efficient system for markerless gene replacement applicable in a wide variety of enterobacterial species
    • White A.P., len-Vercoe E., Jones B.W., DeVinney R., Kay W.W., and Surette M.G. An efficient system for markerless gene replacement applicable in a wide variety of enterobacterial species. Can J Microbiol 53 (2007) 56-62
    • (2007) Can J Microbiol , vol.53 , pp. 56-62
    • White, A.P.1    len-Vercoe, E.2    Jones, B.W.3    DeVinney, R.4    Kay, W.W.5    Surette, M.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.