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Volumn 186, Issue 22, 2004, Pages 7635-7644

Evidence that a B12-adenosyl transferase is encoded within the ethanolamine operon of Salmonella enterica

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ADENOSYLCOBALAMIN TRANSFERASE; BACTERIAL PROTEIN; COBALAMIN; COBAMAMIDE; CORRINOID; ETHANOLAMINE; ETHANOLAMINE AMMONIA LYASE; PROPYLENE GLYCOL; TRANSFERASE; UNCLASSIFIED DRUG; COBALAMIN ADENOSYLTRANSFERASE;

EID: 7744221594     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.22.7635-7644.2004     Document Type: Article
Times cited : (48)

References (37)
  • 1
    • 0024331889 scopus 로고
    • Mutations affecting regulation of cobinamide biosynthesis in Salmonella typhimurium
    • Andersson, D. L., and J. R. Roth. 1989. Mutations affecting regulation of cobinamide biosynthesis in Salmonella typhimurium. J. Bacteriol. 171:6726-6733.
    • (1989) J. Bacteriol. , vol.171 , pp. 6726-6733
    • Andersson, D.L.1    Roth, J.R.2
  • 3
    • 0015951814 scopus 로고
    • The mechanism of action of ethanolamine ammonia-lyase, a B12-dependent enzyme
    • Babior, B. M., T. J. Carty, and R. H. Abeles. 1974. The mechanism of action of ethanolamine ammonia-lyase, a B12-dependent enzyme. J. Biol. Chem. 249:1689-1695.
    • (1974) J. Biol. Chem. , vol.249 , pp. 1689-1695
    • Babior, B.M.1    Carty, T.J.2    Abeles, R.H.3
  • 4
    • 0014533015 scopus 로고
    • The mechanism of action of ethanolamine. V. The photolysis of enzyme-bound alkylcobalamins
    • Babior, B. M., H. Kon, and H. Lecar. 1969. The mechanism of action of ethanolamine. V. The photolysis of enzyme-bound alkylcobalamins. Biochemistry 8:2662-2889.
    • (1969) Biochemistry , vol.8 , pp. 2662-2889
    • Babior, B.M.1    Kon, H.2    Lecar, H.3
  • 6
    • 0018173801 scopus 로고
    • 12-dependent ethanolamine ammonia-lyase of Escherichia coli
    • 12-dependent ethanolamine ammonia-lyase of Escherichia coli. Biochem. J. 175:555-563.
    • (1978) Biochem. J. , vol.175 , pp. 555-563
    • Blackwell, C.M.1    Turner, J.M.2
  • 8
    • 0013841423 scopus 로고
    • The clostridial fermentations of choline and ethanolamine. II. Requirement for a cobamide coenzyme by an ethanolamine deaminase
    • Bradbeer, C. 1965. The clostridial fermentations of choline and ethanolamine. II. Requirement for a cobamide coenzyme by an ethanolamine deaminase. J. Biol. Chem. 240:4675-4681.
    • (1965) J. Biol. Chem. , vol.240 , pp. 4675-4681
    • Bradbeer, C.1
  • 9
    • 1542286908 scopus 로고    scopus 로고
    • The eutD gene of Salmonella enterica encodes a protein with phosphotransacetylase enzyme activity
    • Brinsmade, S. R., and J. C. Escalante-Semerena. 2004. The eutD gene of Salmonella enterica encodes a protein with phosphotransacetylase enzyme activity. J. Bacteriol. 186:1890-1892.
    • (2004) J. Bacteriol. , vol.186 , pp. 1890-1892
    • Brinsmade, S.R.1    Escalante-Semerena, J.C.2
  • 11
    • 0025008948 scopus 로고
    • cobA function is required for both de novo cobalamin biosynthesis and assimilation of exogenous corrinoids in Salmonella typhimurium
    • Escalante-Semerena, J. C., S.-J. Suh, and J. R. Roth. 1990. cobA function is required for both de novo cobalamin biosynthesis and assimilation of exogenous corrinoids in Salmonella typhimurium. J. Bacteriol. 172:273-280.
    • (1990) J. Bacteriol. , vol.172 , pp. 273-280
    • Escalante-Semerena, J.C.1    Suh, S.-J.2    Roth, J.R.3
  • 12
    • 0026572107 scopus 로고
    • Over expression, purification, and some properties of the Ado Cbl-dependent ethanolamine ammonia-lyase from Salmonella typhimurium
    • Faust, L. R., and B. M. Babior. 1992. Over expression, purification, and some properties of the Ado Cbl-dependent ethanolamine ammonia-lyase from Salmonella typhimurium. Arch. Biochem. Biophys. 294:50-54.
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 50-54
    • Faust, L.R.1    Babior, B.M.2
  • 13
    • 0042389658 scopus 로고    scopus 로고
    • 12-dependent degradation of 1,2-propanediol in Salmonella enterica serovar Typhimurium LT2
    • 12-dependent degradation of 1,2-propanediol in Salmonella enterica serovar Typhimurium LT2. J. Bacteriol. 185:5086-5095.
    • (2003) J. Bacteriol. , vol.185 , pp. 5086-5095
    • Havemann, G.D.1    Bobik, T.A.2
  • 14
    • 0036178889 scopus 로고    scopus 로고
    • 12-dependent degradation of 1,2-propanediol in Salmonella enterica serovar Typhimurium LT2
    • 12-dependent degradation of 1,2-propanediol in Salmonella enterica serovar Typhimurium LT2. J. Bacteriol. 184:1253-1261.
    • (2002) J. Bacteriol. , vol.184 , pp. 1253-1261
    • Havemann, G.D.1    Sampson, E.M.2    Bobik, T.A.3
  • 16
    • 0017139869 scopus 로고
    • Coenzyme B12 dependent reactions. Part IV. Observations on the purification of ethanolamine ammonia-lyase
    • Joblin, K., A. Johnson, M. Lappert, and O. Wallis. 1976. Coenzyme B12 dependent reactions. Part IV. Observations on the purification of ethanolamine ammonia-lyase. Biochim. Biophys. Acta 452:262-270.
    • (1976) Biochim. Biophys. Acta , vol.452 , pp. 262-270
    • Joblin, K.1    Johnson, A.2    Lappert, M.3    Wallis, O.4
  • 17
    • 0035110798 scopus 로고    scopus 로고
    • Functional genomic, biochemical, and genetic characterization of the Salmonella pduO gene, an ATP:cob(I)alamin adenosyltransferase gene
    • Johnson, C. L. V. J., E. Pechonick, S. D. Park, G. D. Havemann, N. A. Leal, and T. A. Bobik. 2001. Functional genomic, biochemical, and genetic characterization of the Salmonella pduO gene, an ATP:cob(I)alamin adenosyltransferase gene. J. Bacteriol. 183:1577-1584.
    • (2001) J. Bacteriol. , vol.183 , pp. 1577-1584
    • Johnson, C.L.V.J.1    Pechonick, E.2    Park, S.D.3    Havemann, G.D.4    Leal, N.A.5    Bobik, T.A.6
  • 18
    • 0021255243 scopus 로고
    • A model for common control of enzymes of ethanolamine metabolism in Escherichia coli
    • Jones, P. W., and J. M. Turner. 1984. A model for common control of enzymes of ethanolamine metabolism in Escherichia coli. J. Gen. Microbiol. 130:849-860.
    • (1984) J. Gen. Microbiol. , vol.130 , pp. 849-860
    • Jones, P.W.1    Turner, J.M.2
  • 19
    • 0032851358 scopus 로고    scopus 로고
    • The 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes five homologues of carboxysome shell proteins
    • Kofoid, E., C. Rappleye, I. Stojiljkovic, and J. Roth. 1999. The 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes five homologues of carboxysome shell proteins. J. Bacteriol. 181:5317-5329.
    • (1999) J. Bacteriol. , vol.181 , pp. 5317-5329
    • Kofoid, E.1    Rappleye, C.2    Stojiljkovic, I.3    Roth, J.4
  • 20
    • 0028970502 scopus 로고
    • 12) biosynthetic genes of Escherichia coli
    • 12) biosynthetic genes of Escherichia coli. J. Bacteriol. 177:6371-6380.
    • (1995) J. Bacteriol. , vol.177 , pp. 6371-6380
    • Lawrence, J.G.1    Roth, J.R.2
  • 21
  • 22
    • 0031464312 scopus 로고    scopus 로고
    • Characterization, sequencing, and expression of the genes encoding a reactivating factor for glycerol-inactivated adenosylcobalamin-dependent diol dehydratase
    • Mori, K., T. Tobimatsu, T. Hara, and T. Toraya. 1997. Characterization, sequencing, and expression of the genes encoding a reactivating factor for glycerol-inactivated adenosylcobalamin-dependent diol dehydratase. J. Biol. Chem. 272:32034-32041.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32034-32041
    • Mori, K.1    Tobimatsu, T.2    Hara, T.3    Toraya, T.4
  • 24
    • 0035094993 scopus 로고    scopus 로고
    • 12-dependent anaerobic growth of Salmonella enterica serovar Typhimurium on ethanolamine or 1,2-propanediol
    • 12-dependent anaerobic growth of Salmonella enterica serovar Typhimurium on ethanolamine or 1,2-propanediol. J. Bacteriol. 183:2463-2475.
    • (2001) J. Bacteriol. , vol.183 , pp. 2463-2475
    • Price-Carter, M.1    Tingey, J.2    Bobik, T.A.3    Roth, J.R.4
  • 25
    • 0030885156 scopus 로고    scopus 로고
    • A Tn10 derivative (T-POP) for isolation of insertions with conditional (tetracycline-dependent) phenotypes
    • Rappleye, C. A., and J. R. Roth. 1997. A Tn10 derivative (T-POP) for isolation of insertions with conditional (tetracycline-dependent) phenotypes. J. Bacteriol. 179:5827-5834.
    • (1997) J. Bacteriol. , vol.179 , pp. 5827-5834
    • Rappleye, C.A.1    Roth, J.R.2
  • 26
    • 0017839245 scopus 로고
    • Cluster of genes controlling proline degradation in Salmonella typhimurium
    • Ratzkin, B., and J. Roth. 1978. Cluster of genes controlling proline degradation in Salmonella typhimurium. J. Bacteriol. 133:744-754.
    • (1978) J. Bacteriol. , vol.133 , pp. 744-754
    • Ratzkin, B.1    Roth, J.2
  • 27
    • 0026657140 scopus 로고
    • Autogenous regulation of ethanolamine utilization by a transcriptional activator of the eut operon in Salmonella typhimurium
    • Roof, D. M., and J. R. Roth. 1992. Autogenous regulation of ethanolamine utilization by a transcriptional activator of the eut operon in Salmonella typhimurium. J. Bacteriol. 174:6634-6643.
    • (1992) J. Bacteriol. , vol.174 , pp. 6634-6643
    • Roof, D.M.1    Roth, J.R.2
  • 28
    • 0024075956 scopus 로고
    • Ethanolamine utilization in Salmonella typhimurium
    • Roof, D. M., and J. R. Roth. 1988. Ethanolamine utilization in Salmonella typhimurium. J. Bacteriol. 170:3855-3863.
    • (1988) J. Bacteriol. , vol.170 , pp. 3855-3863
    • Roof, D.M.1    Roth, J.R.2
  • 29
    • 0024393078 scopus 로고
    • 12-dependent ethanolamine utilization in Salmonella typhimurium
    • 12-dependent ethanolamine utilization in Salmonella typhimurium. J. Bacteriol. 171:3316-3323.
    • (1989) J. Bacteriol. , vol.171 , pp. 3316-3323
    • Roof, D.M.1    Roth, J.R.2
  • 30
    • 0029658689 scopus 로고    scopus 로고
    • Cobalamin (coenzyme B12): Synthesis and biological significance
    • Roth, J. R., J. G. Lawrence, and T. A. Bobik. 1996. Cobalamin (coenzyme B12): synthesis and biological significance. Annu. Rev. Microbiol. 50:137-181.
    • (1996) Annu. Rev. Microbiol. , vol.50 , pp. 137-181
    • Roth, J.R.1    Lawrence, J.G.2    Bobik, T.A.3
  • 31
    • 0017165177 scopus 로고
    • 12-dependent ethanolamine ammonia-lyase in Escherichia coli and Klebsiella aerogenes
    • 12-dependent ethanolamine ammonia-lyase in Escherichia coli and Klebsiella aerogenes. J. Gen. Microbiol. 95:173-176.
    • (1976) J. Gen. Microbiol. , vol.95 , pp. 173-176
    • Scarlett, F.A.1    Turner, J.M.2
  • 32
    • 0028262935 scopus 로고
    • A rationale for autoinduction of a transcriptional activator: Ethanolamine ammonia-lyase (EutBC) and the operon activator (EutR) compete for adenosyl-cobalamin in Salmonella typhimurium
    • Sheppard, D. E., and J. R. Roth. 1994. A rationale for autoinduction of a transcriptional activator: ethanolamine ammonia-lyase (EutBC) and the operon activator (EutR) compete for adenosyl-cobalamin in Salmonella typhimurium. J. Bacteriol. 176:1287-1296.
    • (1994) J. Bacteriol. , vol.176 , pp. 1287-1296
    • Sheppard, D.E.1    Roth, J.R.2
  • 33
    • 0028944586 scopus 로고
    • Ethanolamine utilization in Salmonella typhimurium: Nucleotide sequence, protein expression, and mutational analysis of the cchA cchB eutJ eutG eutH gene cluster
    • Stojiljkovic, I., A. J. Bäumler, and F. Heffron. 1995. Ethanolamine utilization in Salmonella typhimurium: nucleotide sequence, protein expression, and mutational analysis of the cchA cchB eutJ eutG eutH gene cluster. J. Bacteriol. 177:1357-1366.
    • (1995) J. Bacteriol. , vol.177 , pp. 1357-1366
    • Stojiljkovic, I.1    Bäumler, A.J.2    Heffron, F.3
  • 34
    • 0028877843 scopus 로고
    • Purification and initial characterization of the ATP:corrinoid adenosyltransferase encoded by the cobA gene of Salmonella typhimurium
    • Suh, S.-J., and J. C. Escalante-Semerena. 1995. Purification and initial characterization of the ATP:corrinoid adenosyltransferase encoded by the cobA gene of Salmonella typhimurium. J. Bacteriol. 177:921-925.
    • (1995) J. Bacteriol. , vol.177 , pp. 921-925
    • Suh, S.-J.1    Escalante-Semerena, J.C.2
  • 35
    • 0033024922 scopus 로고    scopus 로고
    • Identification and expression of the genes encoding a reactivating factor for adenosylcobalamin-dependent glycerol dehydratase
    • Tobimatsu, T., H. Kajiura, M. Yunoki, M. Azuma, and T. Toraya. 1999. Identification and expression of the genes encoding a reactivating factor for adenosylcobalamin-dependent glycerol dehydratase. J. Bacteriol. 181:4110-4113.
    • (1999) J. Bacteriol. , vol.181 , pp. 4110-4113
    • Tobimatsu, T.1    Kajiura, H.2    Yunoki, M.3    Azuma, M.4    Toraya, T.5
  • 36
    • 0033525074 scopus 로고    scopus 로고
    • A reactivating factor for coenzyme B12-dependent diol dehydratase
    • Toraya, T., and K. Mori. 1999. A reactivating factor for coenzyme B12-dependent diol dehydratase. J. Biol. Chem. 274:3372-3377.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3372-3377
    • Toraya, T.1    Mori, K.2
  • 37
    • 0021681568 scopus 로고
    • New Tn10 derivatives for transposon mutagenesis and for construction of lacZ operon fusions by transposition
    • Way, J. C., M. A. Davis, D. Morisato, D. E. Roberts, and N. Kleckner. 1984. New Tn10 derivatives for transposon mutagenesis and for construction of lacZ operon fusions by transposition. Gene 32:369-379.
    • (1984) Gene , vol.32 , pp. 369-379
    • Way, J.C.1    Davis, M.A.2    Morisato, D.3    Roberts, D.E.4    Kleckner, N.5


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