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Volumn 147, Issue 1, 2010, Pages 83-93

Purification and some properties of wild-type and N-terminal-truncated ethanolamine ammonia-lyase of Escherichia coli

Author keywords

Adenosylcobalamin; Coenzyme B12; Ethanolamine ammonia lyase; Radical enzyme; Truncated enzyme

Indexed keywords

ETHANOLAMINE AMMONIA LYASE;

EID: 75649097075     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvp145     Document Type: Article
Times cited : (17)

References (46)
  • 1
    • 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
  • 2
    • 0013832936 scopus 로고
    • The clostridial fermentations of choline and ethanolamine. I. Preparation and properties of cell-free extracts
    • Bradbeer, C. (1965) The clostridial fermentations of choline and ethanolamine. I. Preparation and properties of cell-free extracts. J. Biol. Chem. 240, 4669-4674
    • (1965) J. Biol. Chem. , vol.240 , pp. 4669-4674
    • Bradbeer, C.1
  • 3
    • 0016593454 scopus 로고
    • 12-dependent enzyme ethanolamine deaminase in Salmonella
    • 12- dependent enzyme ethanolamine deaminase in Salmonella. Nature 95, 150-151
    • (1975) Nature , vol.95 , pp. 150-151
    • Chang, G.W.1    Chang, J.T.2
  • 4
    • 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
  • 5
    • 0022460756 scopus 로고
    • Isolation and genetic characterizations of Bacillus megaterium cobalamin biosynthesis- deficient mutants
    • Wolf, J.B. and Brey, R.N. (1986) Isolation and genetic characterizations of Bacillus megaterium cobalamin biosynthesis- deficient mutants. J. Bacteriol. 166, 51-58
    • (1986) J. Bacteriol. , vol.166 , pp. 51-58
    • Wolf, J.B.1    Brey, R.N.2
  • 6
    • 0024075956 scopus 로고
    • Ethanolamine utilization in Salmonella typhimurium
    • Roof, D.M. and Roth, J.R. (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
  • 7
    • 0027937280 scopus 로고
    • Fermentative degradation of triethanolamine by a homoacetogenic bacterium
    • Frings, J., Wondrak, C., and Schink, B. (1994) Fermentative degradation of triethanolamine by a homoacetogenic bacterium. Arch. Microbiol. 162, 103-107
    • (1994) Arch. Microbiol. , vol.162 , pp. 103-107
    • Frings, J.1    Wondrak, C.2    Schink, B.3
  • 8
    • 0014429479 scopus 로고
    • Ethanolamine deaminase, a cobamide coenzyme-dependent enzyme. I. Purification, assay, and properties of the enzyme
    • Kaplan, B.H. and Stadtman, E.R. (1968) Ethanolamine deaminase, a cobamide coenzyme-dependent enzyme. I. Purification, assay, and properties of the enzyme. J. Biol. Chem. 243, 1787-1793
    • (1968) J. Biol. Chem. , vol.243 , pp. 1787-1793
    • Kaplan, B.H.1    Stadtman, E.R.2
  • 9
    • 0018173801 scopus 로고
    • 12-dependent ethanolamine ammonialyase of Escherichia coli
    • 12-dependent ethanolamine ammonialyase of Escherichia coli. Biochem. J. 175, 555-563
    • (1978) Biochem. J. , vol.175 , pp. 555-563
    • Blackwell, C.M.1    Turner, J.M.2
  • 10
    • 0018295817 scopus 로고
    • Studies on the subunit structure of the adenosylcobalamin- dependent enzyme ethanolamine ammonia-lyase
    • Wallis, O.C., Johnson, A.W., and Lappert, M.F. (1979) Studies on the subunit structure of the adenosylcobalamin- dependent enzyme ethanolamine ammonia-lyase. FEBS Lett. 97, 196-199
    • (1979) FEBS Lett. , vol.97 , pp. 196-199
    • Wallis, O.C.1    Johnson, A.W.2    Lappert, M.F.3
  • 11
    • 0026572107 scopus 로고
    • Overexpression, purification, and some properties of the AdoCbldependent ethanolamine ammonia-lyase from Salmonella typhimurium
    • Faust, L.P. and Babior, B.M. (1992) Overexpression, purification, and some properties of the AdoCbldependent ethanolamine ammonia-lyase from Salmonella typhimurium. Arch. Biochem. Biophys. 294, 50-54
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 50-54
    • Faust, L.P.1    Babior, B.M.2
  • 12
    • 0014429342 scopus 로고
    • Ethanolamine deaminase, a cobamide coenzyme-dependent enzyme. II. Physical and chemical properties and interaction with cobamides and ethanolamine
    • Kaplan, B.H. and Stadtman, E.R. (1968) Ethanolamine deaminase, a cobamide coenzyme-dependent enzyme. II. Physical and chemical properties and interaction with cobamides and ethanolamine. J. Biol. Chem. 243, 1794-1803
    • (1968) J. Biol. Chem. , vol.243 , pp. 1794-1803
    • Kaplan, B.H.1    Stadtman, E.R.2
  • 13
    • 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 Roth, J.R. (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
  • 14
    • 0032851358 scopus 로고    scopus 로고
    • The 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes five homologues of carboxysome shell proteins
    • Kofoid, E., Rappleye, C., Stojiljkovic, I., and Roth, J. (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
  • 15
    • 0000244215 scopus 로고
    • Ethanolamine ammonia-lyase
    • (Dolphin D., ed.) John Wiley & Sons, New York
    • 12 (Dolphin D., ed.) Vol.2, pp. 263-287, John Wiley & Sons, New York
    • (1982) 12 , vol.2 , pp. 263-287
    • Babior, B.M.1
  • 16
    • 0001916849 scopus 로고    scopus 로고
    • Ethanolamine ammonia-lyase
    • (Banerjee R., ed.) John Wiley & Sons, New York
    • 12 (Banerjee R., ed.), pp. 811-833, John Wiley & Sons, New York
    • (1999) 12 , pp. 811-833
    • Bandarian, V.1    Reed, G.H.2
  • 17
    • 4644229550 scopus 로고    scopus 로고
    • Radical mechanisms in adenosylcobalamin- dependent enzymes
    • Reed, G.H. (2004) Radical mechanisms in adenosylcobalamin- dependent enzymes. Curr. Opin. Chem. Biol. 8, 477-483
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 477-483
    • Reed, G.H.1
  • 18
    • 0017237457 scopus 로고
    • The interaction of adeninylalkylcobalamins with ribonucleotide reductase
    • Sando, G.N., Grant, M.E., and Hogenkamp, H.P.C. (1976) The interaction of adeninylalkylcobalamins with ribonucleotide reductase. Biochim. Biophys. Acta 428, 228-232
    • (1976) Biochim. Biophys. Acta , vol.428 , pp. 228-232
    • Sando, G.N.1    Grant, M.E.2    Hogenkamp, H.P.C.3
  • 19
    • 0026009365 scopus 로고
    • Roles of the D-ribose and 5,6-dimethylbenzimidazole moieties of the nucleotide loop of adenosylcobalamin in manifestation of coenzymic function in the diol dehydrase reaction
    • Toraya, T. and Ishida, A. (1991) Roles of the D-ribose and 5,6-dimethylbenzimidazole moieties of the nucleotide loop of adenosylcobalamin in manifestation of coenzymic function in the diol dehydrase reaction. J. Biol. Chem. 266, 5430-5437
    • (1991) J. Biol. Chem. , vol.266 , pp. 5430-5437
    • Toraya, T.1    Ishida, A.2
  • 20
    • 0032492687 scopus 로고    scopus 로고
    • Evidence for axial coordination of 5,6-dimethylbenzimidazole to the cobalt atom of adenosylcobalamin bound to diol dehydratase
    • Yamanishi, M., Yamada, S., Muguruma, H., Murakami, Y., Tobimatsu, T., Ishida, A., Yamauchi, J., and Toraya, T. (1998) Evidence for axial coordination of 5,6-dimethylbenzimidazole to the cobalt atom of adenosylcobalamin bound to diol dehydratase. Biochemistry 37, 4799-4803
    • (1998) Biochemistry , vol.37 , pp. 4799-4803
    • Yamanishi, M.1    Yamada, S.2    Muguruma, H.3    Murakami, Y.4    Tobimatsu, T.5    Ishida, A.6    Yamauchi, J.7    Toraya, T.8
  • 22
    • 0023669069 scopus 로고
    • The physical map of the whole E. coli chromosome: Application of a new strategy for rapid analysis and sorting of a large genomic library
    • Kohara, Y., Akiyama, K., and Isono, K. (1987) The physical map of the whole E. coli chromosome: application of a new strategy for rapid analysis and sorting of a large genomic library. Cell 50, 495-508
    • (1987) Cell , vol.50 , pp. 495-508
    • Kohara, Y.1    Akiyama, K.2    Isono, K.3
  • 23
    • 17844373301 scopus 로고    scopus 로고
    • The N-terminal regions of b and g subunits lower the solubility of adenosylcobalamin-dependent diol dehydratase
    • Tobimatsu, T., Kawata, M., and Toraya, T. (2005) The N-terminal regions of b and g subunits lower the solubility of adenosylcobalamin-dependent diol dehydratase. Biosci. Biotechnol. Biochem. 69, 455-462
    • (2005) Biosci. Biotechnol. Biochem. , vol.69 , pp. 455-462
    • Tobimatsu, T.1    Kawata, M.2    Toraya, T.3
  • 24
    • 4944253783 scopus 로고    scopus 로고
    • Identification of a reactivating factor for adenosylcobalamin- dependent ethanolamine ammonia lyase
    • Mori, K., Bando, R., Hieda, N., and Toraya, T. (2004) Identification of a reactivating factor for adenosylcobalamin- dependent ethanolamine ammonia lyase. J. Bacteriol. 186, 6845-6854
    • (2004) J. Bacteriol. , vol.186 , pp. 6845-6854
    • Mori, K.1    Bando, R.2    Hieda, N.3    Toraya, T.4
  • 25
    • 0017626312 scopus 로고
    • Studies on the mechanism of the adenosylcobalamin-dependent diol dehydrase reaction by the use of analogs of the coenzyme
    • Toraya, T., Ushio, K., Fukui, S., and Hogenkamp, H.P.C. (1977) Studies on the mechanism of the adenosylcobalamin-dependent diol dehydrase reaction by the use of analogs of the coenzyme. J. Biol. Chem. 252, 963-970
    • (1977) J. Biol. Chem. , vol.252 , pp. 963-970
    • Toraya, T.1    Ushio, K.2    Fukui, S.3    Hogenkamp, H.P.C.4
  • 27
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S.C. and von Hippel, P.H. (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182, 319-326
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 28
    • 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
  • 29
    • 0014448405 scopus 로고
    • The binding of cobamides to ethanolamine deaminase
    • Babior, B.M. and Li, T.K. (1969) The binding of cobamides to ethanolamine deaminase. Biochemistry 8, 154-160
    • (1969) Biochemistry , vol.8 , pp. 154-160
    • Babior, B.M.1    Li, T.K.2
  • 30
    • 0019071337 scopus 로고
    • The number of functional active sites per molecule of the adenosylcobalamin-dependent enzyme, ethanolamine ammonia-lyase, as determined by a kinetic method
    • Hollaway, M.R., Johnson, A.W., Lappert, M.F., and Wallis, O.C. (1980) The number of functional active sites per molecule of the adenosylcobalamin- dependent enzyme, ethanolamine ammonia-lyase, as determined by a kinetic method. Eur. J. Biochem. 111, 177-188
    • (1980) Eur. J. Biochem. , vol.111 , pp. 177-188
    • Hollaway, M.R.1    Johnson, A.W.2    Lappert, M.F.3    Wallis, O.C.4
  • 31
    • 0033592455 scopus 로고    scopus 로고
    • Hydrazine cation radical in the active site of ethanolamine ammonia-lyase: Mechanism-based inactivation by hydroxyethylhydrazine
    • Bandarian, V. and Reed, G.H. (1999) Hydrazine cation radical in the active site of ethanolamine ammonia-lyase: mechanism-based inactivation by hydroxyethylhydrazine. Biochemistry 38, 12394-12402
    • (1999) Biochemistry , vol.38 , pp. 12394-12402
    • Bandarian, V.1    Reed, G.H.2
  • 32
    • 0019324012 scopus 로고
    • The mechanism of action of ethanolamine ammonia-lyase, an adenosylcobalamindependent enzyme. Evidence that carbon-cobalt bond cleavage is driven in part by conformational alterations of the corrin ring
    • Krouwer, J.S., Holmquist, B., Kipnes, R.S., and Babior, B.M. (1980) The mechanism of action of ethanolamine ammonia-lyase, an adenosylcobalamindependent enzyme. Evidence that carbon-cobalt bond cleavage is driven in part by conformational alterations of the corrin ring. Biochim. Biophys. Acta 612, 153-159
    • (1980) Biochim. Biophys. Acta , vol.612 , pp. 153-159
    • Krouwer, J.S.1    Holmquist, B.2    Kipnes, R.S.3    Babior, B.M.4
  • 33
    • 0016244339 scopus 로고
    • 12-dependent enzyme. The participation of paramagnetic species in the catalytic deamination of 2-aminopropanol
    • 12-dependent enzyme. The participation of paramagnetic species in the catalytic deamination of 2-aminopropanol. J. Biol. Chem. 249, 4537-4544
    • (1974) J. Biol. Chem. , vol.249 , pp. 4537-4544
    • Babior, B.M.1    Moss, T.H.2    Orme-Johnson, W.H.3    Beinert, H.4
  • 35
    • 54849439082 scopus 로고    scopus 로고
    • Identification of the substrate radical intermediate derived from ethanolamine during catalysis by ethanolamine ammonia-lyase
    • Bender, G., Poyner, R.R., and Reed, G.H. (2008) Identification of the substrate radical intermediate derived from ethanolamine during catalysis by ethanolamine ammonia-lyase. Biochemistry 47, 11360-11366
    • (2008) Biochemistry , vol.47 , pp. 11360-11366
    • Bender, G.1    Poyner, R.R.2    Reed, G.H.3
  • 36
    • 0037047017 scopus 로고    scopus 로고
    • 12-dependent ethanolamine ammonia-lyase catalyzed reaction of S-2- aminopropanol
    • 12-dependent ethanolamine ammonia-lyase catalyzed reaction of S-2- aminopropanol. Biochemistry 41, 8580-8588
    • (2002) Biochemistry , vol.41 , pp. 8580-8588
    • Bandarian, V.1    Reed, G.H.2
  • 38
    • 0017609160 scopus 로고
    • EPR determination of the Co(II)-free radical magnetic geometry of the "doublet" species arising in a coenzyme B-12-enzyme reaction
    • Buettner, G.R. and Coffman, R.E. (1977) EPR determination of the Co(II)-free radical magnetic geometry of the "doublet" species arising in a coenzyme B-12-enzyme reaction. Biochim. Biophys. Acta 480, 495-505
    • (1977) Biochim. Biophys. Acta , vol.480 , pp. 495-505
    • Buettner, G.R.1    Coffman, R.E.2
  • 44
    • 0033613217 scopus 로고    scopus 로고
    • Identification of dimethylbenzimidazole axial coordination and characterization of 14N superhyperfine and nuclear quadrupole coupling in cob(II)alamin bound to ethanolamine deaminase in a catalytically-engaged substrate radical-cobalt(II) biradical state
    • Ke, S.-C., Torrent, M., Museav, D.G., Morokuma, K., and Warncke, K. (1999) Identification of dimethylbenzimidazole axial coordination and characterization of 14N superhyperfine and nuclear quadrupole coupling in cob(II)alamin bound to ethanolamine deaminase in a catalytically-engaged substrate radical-cobalt(II) biradical state. Biochemistry 38, 12681-12689
    • (1999) Biochemistry , vol.38 , pp. 12681-12689
    • Ke, S.-C.1    Torrent, M.2    Museav, D.G.3    Morokuma, K.4    Warncke, K.5
  • 45
    • 0015951814 scopus 로고
    • 12-dependent enzyme. The reversible formation of 50-deoxyadenosine from adenosylcobalamin during the catalytic process
    • 12-dependent enzyme. The reversible formation of 50-deoxyadenosine from adenosylcobalamin during the catalytic process. 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
  • 46
    • 0017576520 scopus 로고
    • Inactivation of ethanolamine ammonia-lyase by 5,50-dithiobis(2- nitrobenzoic acid). Further evidence for the involvement of sulfhydryl groups in adenosylcobalamin-dependent rearrangements
    • Mauck, L. and Babior, B.M. (1977) Inactivation of ethanolamine ammonia-lyase by 5,50-dithiobis(2- nitrobenzoic acid). Further evidence for the involvement of sulfhydryl groups in adenosylcobalamin-dependent rearrangements. Biochim. Biophys. Acta. 480, 489-494
    • (1977) Biochim. Biophys. Acta. , vol.480 , pp. 489-494
    • Mauck, L.1    Babior, B.M.2


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