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Volumn 46, Issue 48, 2007, Pages 13829-13836

Structural and functional analyses of the human-type corrinoid adenosyltransferase (PduO) from Lactobacillus reuteri

Author keywords

[No Author keywords available]

Indexed keywords

CORRINOID ADENOSYLTRANSFERASE (PDUO); MAGNESIUM IONS; METHYLMALONIC ACIDURIA;

EID: 36849074685     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701622j     Document Type: Article
Times cited : (27)

References (38)
  • 1
    • 36849010883 scopus 로고    scopus 로고
    • Huennekens, F. M., Vitols, K. S., Fujii, K., and Jacobsen, D. W. (1982) Biosynthesis of cobalamin coenzymes, in B12 (Dolphin, D., Ed.) pp 145-168, John Wiley & Sons, Inc., New York.
    • Huennekens, F. M., Vitols, K. S., Fujii, K., and Jacobsen, D. W. (1982) Biosynthesis of cobalamin coenzymes, in B12 (Dolphin, D., Ed.) pp 145-168, John Wiley & Sons, Inc., New York.
  • 2
    • 0014010466 scopus 로고
    • Enzymatic conversion of vitamin B12s to a cobamide coenzyme, α-(5,6- dimethylbenzimidazolyl)deoxy-adenosylcobamide (adenosyl-B12)
    • Vitols, E., Walker, G. A., and Huennekens, F. M. (1966) Enzymatic conversion of vitamin B12s to a cobamide coenzyme, α-(5,6- dimethylbenzimidazolyl)deoxy-adenosylcobamide (adenosyl-B12), J. Biol. Chem. 241, 1455-1461.
    • (1966) J. Biol. Chem , vol.241 , pp. 1455-1461
    • Vitols, E.1    Walker, G.A.2    Huennekens, F.M.3
  • 5
    • 0022430394 scopus 로고
    • 12-dependent rearrangements
    • 12-dependent rearrangements, Science 227, 869-875.
    • (1985) Science , vol.227 , pp. 869-875
    • Halpern, J.1
  • 6
    • 0002162740 scopus 로고    scopus 로고
    • Methylmalonyl-CoA mutase
    • Banerjee, R, Ed, pp, John Wiley & Sons, Inc, New York
    • Banerjee, R., and Chowdhury, S. (1999) Methylmalonyl-CoA mutase, in Chemistry and Biochemistry of B12 (Banerjee, R., Ed.) pp 707-729, John Wiley & Sons, Inc., New York.
    • (1999) Chemistry and Biochemistry of B12 , pp. 707-729
    • Banerjee, R.1    Chowdhury, S.2
  • 7
    • 0003046814 scopus 로고    scopus 로고
    • Glutamate mutase and 2-Methylglutarate mutase
    • Banerjee, R, Ed, pp, John Wiley & Sons, Inc, New York
    • Buckel, W., Bröker, G., Bothe, H., and Pierik, A. (1999) Glutamate mutase and 2-Methylglutarate mutase, in Chemistry and Biochemistry of B12 (Banerjee, R., Ed.) pp 757-782, John Wiley & Sons, Inc., New York.
    • (1999) Chemistry and Biochemistry of B12 , pp. 757-782
    • Buckel, W.1    Bröker, G.2    Bothe, H.3    Pierik, A.4
  • 8
    • 0001916849 scopus 로고    scopus 로고
    • Ethanolamine ammonialyase
    • Banerjee, R, Ed, pp, John Wiley & Sons, Inc, New York
    • Bandarian, V., and Reed, G. H. (1999) Ethanolamine ammonialyase, in Chemistry and Biochemistry of B12 (Banerjee, R., Ed.) pp 811-833, John Wiley & Sons, Inc., New York.
    • (1999) Chemistry and Biochemistry of B12 , pp. 811-833
    • Bandarian, V.1    Reed, G.H.2
  • 9
    • 0001965823 scopus 로고    scopus 로고
    • Diol dehydratase and glycerol dehydratase
    • Banerjee, R, Ed, pp, John Wiley & Sons, Inc, New York
    • Toraya, T. (1999) Diol dehydratase and glycerol dehydratase, in Chemistry and Biochemistry of B12 (Banerjee, R., Ed.) pp 783-809, John Wiley & Sons, Inc., New York.
    • (1999) Chemistry and Biochemistry of B12 , pp. 783-809
    • Toraya, T.1
  • 10
    • 0031849153 scopus 로고    scopus 로고
    • Ribonucleotide reductases and radical reactions
    • Fontecave, M. (1998) Ribonucleotide reductases and radical reactions, Cell. Mol. Life Sci. 54, 684-695.
    • (1998) Cell. Mol. Life Sci , vol.54 , pp. 684-695
    • Fontecave, M.1
  • 11
    • 0002131030 scopus 로고    scopus 로고
    • Ribonucleotide Reductases
    • Banerjee, R, Ed, pp, John Wiley & Sons, Inc, New York
    • Fontecave, M., and Mulliez, E. (1999) Ribonucleotide Reductases, in Chemistry and Biochemistry of B12 (Banerjee, R., Ed.) pp 731-756, John Wiley & Sons, Inc., New York.
    • (1999) Chemistry and Biochemistry of B12 , pp. 731-756
    • Fontecave, M.1    Mulliez, E.2
  • 12
    • 0002181615 scopus 로고    scopus 로고
    • Reductive dehalogenases
    • Banerjee, R, Ed, pp, John Wiley & Sons, Inc, New York
    • Wohlfarth, G., and Diekert, G. (1999) Reductive dehalogenases, in Chemistry and Biochemistry of B12 (Banerjee, R., Ed.) pp 871-893, John Wiley & Sons, Inc., New York.
    • (1999) Chemistry and Biochemistry of B12 , pp. 871-893
    • Wohlfarth, G.1    Diekert, G.2
  • 13
    • 0028877843 scopus 로고
    • Purification and initial characterization of the ATP:corrinoid adenosyltransferase encoded by the cobA gene of Salmonella typhimurium
    • Suh, S., and Escalante-Semerena, J. C. (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.1    Escalante-Semerena, J.C.2
  • 14
    • 33745203067 scopus 로고    scopus 로고
    • Purification and initial biochemical characterization of ATP:Cob(1)alamin adenosyltransferase (EutT) enzyme of Salmonella enterica
    • Buan, N. R., and Escalante-Semerena, J. C. (2006) Purification and initial biochemical characterization of ATP:Cob(1)alamin adenosyltransferase (EutT) enzyme of Salmonella enterica, J. Biol. Chem. 281, 16971-16977.
    • (2006) J. Biol. Chem , vol.281 , pp. 16971-16977
    • Buan, N.R.1    Escalante-Semerena, J.C.2
  • 15
    • 9244262460 scopus 로고    scopus 로고
    • Purification and initial characterization of the Salmonella enterica PduO ATP: Cob(I)alamin adenosyltransferase
    • Johnson, C. L., Buszko, M. L., and Bobik, T. A. (2004) Purification and initial characterization of the Salmonella enterica PduO ATP: Cob(I)alamin adenosyltransferase, J. Bacteriol. 186, 7881-7887.
    • (2004) J. Bacteriol , vol.186 , pp. 7881-7887
    • Johnson, C.L.1    Buszko, M.L.2    Bobik, T.A.3
  • 17
    • 0018198219 scopus 로고
    • Mitochondrial metabolism of hydroxocobalamin: Synthesis of adenosylcobalamin by intact rat liver mitochondria
    • Fenton, W. A., and Rosenberg, L. E. (1978) Mitochondrial metabolism of hydroxocobalamin: synthesis of adenosylcobalamin by intact rat liver mitochondria, Arch. Biochem. Biophys. 189, 441-447.
    • (1978) Arch. Biochem. Biophys , vol.189 , pp. 441-447
    • Fenton, W.A.1    Rosenberg, L.E.2
  • 21
    • 34047258871 scopus 로고    scopus 로고
    • Structural characterization of the active site of the PduO-type ATP:Co(I)rrinoid adenosyltransferase from Lactobacillus reuteri
    • St Maurice, M., Mera, P. E., Taranto, M. P., Sesma, F., Escalante-Semerena, J. C., and Rayment, I. (2007) Structural characterization of the active site of the PduO-type ATP:Co(I)rrinoid adenosyltransferase from Lactobacillus reuteri, J. Biol. Chem. 282, 2596-2605.
    • (2007) J. Biol. Chem , vol.282 , pp. 2596-2605
    • St Maurice, M.1    Mera, P.E.2    Taranto, M.P.3    Sesma, F.4    Escalante-Semerena, J.C.5    Rayment, I.6
  • 22
    • 33845937432 scopus 로고    scopus 로고
    • Structure of ATP-bound human ATP:cobalamin adenosyltransferase
    • Schubert, H. L., and Hill, C. P. (2006) Structure of ATP-bound human ATP:cobalamin adenosyltransferase, Biochemistry 45, 15188-15196.
    • (2006) Biochemistry , vol.45 , pp. 15188-15196
    • Schubert, H.L.1    Hill, C.P.2
  • 24
    • 33645113221 scopus 로고    scopus 로고
    • Impact of cblB mutations on the function of ATP:cob(I)alamin adenosyltransferase in disorders of vitamin B12 metabolism
    • Zhang, J., Dobson, C. M., Wu, X., Lerner-Ellis, J., Rosenblatt, D. S., and Gravel, R. A. (2006) Impact of cblB mutations on the function of ATP:cob(I)alamin adenosyltransferase in disorders of vitamin B12 metabolism, Mol. Genet. Metab. 87, 315-322.
    • (2006) Mol. Genet. Metab , vol.87 , pp. 315-322
    • Zhang, J.1    Dobson, C.M.2    Wu, X.3    Lerner-Ellis, J.4    Rosenblatt, D.S.5    Gravel, R.A.6
  • 25
    • 0033929687 scopus 로고    scopus 로고
    • Reduction of cob(III)alamin to cob(II)alamin in Salmonella enterica Serovar Typhimurium LT2
    • Fonseca, M. V., and Escalante-Semerena, J. C. (2000) Reduction of cob(III)alamin to cob(II)alamin in Salmonella enterica Serovar Typhimurium LT2, J. Bacteriol. 182, 4304-4309.
    • (2000) J. Bacteriol , vol.182 , pp. 4304-4309
    • Fonseca, M.V.1    Escalante-Semerena, J.C.2
  • 26
    • 0038112886 scopus 로고    scopus 로고
    • A Program to Detwin Merohedrally Twinned Data
    • Taylor, H. O., and Leslie, A. G. W. (1998) A Program to Detwin Merohedrally Twinned Data, CCP4 Newsl. 35, 9.
    • (1998) CCP4 Newsl. 35 , pp. 9
    • Taylor, H.O.1    Leslie, A.G.W.2
  • 27
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An Automated Program for Molecular Replacement
    • Vagin, A., and Teplyakov, A. (1997) MOLREP: an Automated Program for Molecular Replacement, J. Appl. Ctystallogr. 30, 1022-1025.
    • (1997) J. Appl. Ctystallogr , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 28
    • 28844461006 scopus 로고    scopus 로고
    • Computer-assisted docking of flavodoxin with the ATP:Co(I)rrinoid adenosyltransferase (CobA) enzyme reveals residues critical for protein-protein interactions but not for catalysis
    • Buan, N. R., and Escalante-Semerena, J. C. (2005) Computer-assisted docking of flavodoxin with the ATP:Co(I)rrinoid adenosyltransferase (CobA) enzyme reveals residues critical for protein-protein interactions but not for catalysis, J. Biol.Chem. 280, 40948-40956.
    • (2005) J. Biol.Chem , vol.280 , pp. 40948-40956
    • Buan, N.R.1    Escalante-Semerena, J.C.2
  • 29
    • 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., Pechonick, E., Park, S. D., Havemann, G. D., Leal, N. A., and Bobik, T. A. (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.1    Pechonick, E.2    Park, S.D.3    Havemann, G.D.4    Leal, N.A.5    Bobik, T.A.6
  • 30
    • 0003518480 scopus 로고
    • John Wiley & Sons, New York
    • Segel, I. H. (1975) Enzyme Kinetics, pp 819-822, John Wiley & Sons, New York.
    • (1975) Enzyme Kinetics , pp. 819-822
    • Segel, I.H.1
  • 31
    • 0027218644 scopus 로고
    • Cloning, sequencing and overexpression of cobA which encodes ATP: Corrinoid adenosyltransferase in Salmonella typhimurium
    • Suh, S. J., and Escalante-Semerena, J. C. (1993) Cloning, sequencing and overexpression of cobA which encodes ATP: corrinoid adenosyltransferase in Salmonella typhimurium, Gene 129, 93-97.
    • (1993) Gene , vol.129 , pp. 93-97
    • Suh, S.J.1    Escalante-Semerena, J.C.2
  • 32
    • 0037031898 scopus 로고    scopus 로고
    • The ATP:co(I)rrinoid adenosyltransferase (CobA) enzyme of Salmonella enterica requires the 2′-OH Group of ATP for function and yields inorganic triphosphate as its reaction byproduct
    • Fonseca, M. V., Buan, N. R., Horswill, A. R., Rayment, I., and Escalante-Semerena, J. C. (2002) The ATP:co(I)rrinoid adenosyltransferase (CobA) enzyme of Salmonella enterica requires the 2′-OH Group of ATP for function and yields inorganic triphosphate as its reaction byproduct, J. Biol. Chem. 277, 33127-33131.
    • (2002) J. Biol. Chem , vol.277 , pp. 33127-33131
    • Fonseca, M.V.1    Buan, N.R.2    Horswill, A.R.3    Rayment, I.4    Escalante-Semerena, J.C.5
  • 33
    • 3543116192 scopus 로고    scopus 로고
    • Spectroscopic and computational studies of Co(2+)corrinoids: Spectral and electronic properties of the biologically relevant base-on and base-off forms of Co(2+)cobalamin
    • Stich, T. A., Buan, N. R., and Brunold, T. C. (2004) Spectroscopic and computational studies of Co(2+)corrinoids: spectral and electronic properties of the biologically relevant base-on and base-off forms of Co(2+)cobalamin, J. Am. Chem. Soc. 126, 9735-9749.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 9735-9749
    • Stich, T.A.1    Buan, N.R.2    Brunold, T.C.3
  • 34
    • 19744367518 scopus 로고    scopus 로고
    • Spectroscopic evidence for the formation of a four-coordinate Co(2+)cobalamin species upon binding to the human ATP:Cobalamin adenosyltransferase
    • Stich, T. A., Yamanishi, M., Banerjee, R., and Brunold, T. C. (2005) Spectroscopic evidence for the formation of a four-coordinate Co(2+)cobalamin species upon binding to the human ATP:Cobalamin adenosyltransferase, J. Am. Chem. Soc. 127, 7660-7661.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 7660-7661
    • Stich, T.A.1    Yamanishi, M.2    Banerjee, R.3    Brunold, T.C.4
  • 35
    • 20944441368 scopus 로고    scopus 로고
    • Spectroscopic and computational studies of the ATP: Corrinoid adenosyltransferase (CobA) from Salmonella enterica: Insights into the mechanism of adenosylcobalamin biosynthesis
    • Stich, T. A., Buan, N. R., Escalante-Semerena, J. C., and Brunold, T. C. (2005) Spectroscopic and computational studies of the ATP: Corrinoid adenosyltransferase (CobA) from Salmonella enterica: Insights into the mechanism of adenosylcobalamin biosynthesis, J. Am. Chem. Soc. 127, 8710-8719.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 8710-8719
    • Stich, T.A.1    Buan, N.R.2    Escalante-Semerena, J.C.3    Brunold, T.C.4
  • 36
    • 0035933729 scopus 로고    scopus 로고
    • Structural evidence for entropic contribution of salt bridge formation to a protein antigen-antibody interaction: The case of hen lysozyme-HyHEL-10 Fv complex
    • Shiroishi, M., Yokota, A., Tsumoto, K., Kondo, H., Nishimiya, Y., Horii, K., Matsushima, M., Ogasahara, K., Yutani, K., and Kumagai, I. (2001) Structural evidence for entropic contribution of salt bridge formation to a protein antigen-antibody interaction: the case of hen lysozyme-HyHEL-10 Fv complex, J. Biol. Chem. 276, 23042-23050.
    • (2001) J. Biol. Chem , vol.276 , pp. 23042-23050
    • Shiroishi, M.1    Yokota, A.2    Tsumoto, K.3    Kondo, H.4    Nishimiya, Y.5    Horii, K.6    Matsushima, M.7    Ogasahara, K.8    Yutani, K.9    Kumagai, I.10
  • 37
    • 0030459404 scopus 로고    scopus 로고
    • Role of salt bridge formation in antigen-antibody interaction. Entropic contribution to the complex between hen egg white lysozyme and its monoclonal antibody HyHEL10
    • Tsumoto, K., Ogasahara, K., Ueda, Y., Watanabe, K., Yutani, K., and Kumagai, I. (1996) Role of salt bridge formation in antigen-antibody interaction. Entropic contribution to the complex between hen egg white lysozyme and its monoclonal antibody HyHEL10, J. Biol. Chem. 271, 32612-32616.
    • (1996) J. Biol. Chem , vol.271 , pp. 32612-32616
    • Tsumoto, K.1    Ogasahara, K.2    Ueda, Y.3    Watanabe, K.4    Yutani, K.5    Kumagai, I.6
  • 38
    • 0035895343 scopus 로고    scopus 로고
    • Three-dimensional structure of ATP:corrinoid adenosyltransferase from Salmonella typhimurium in its free state, complexed with MgATP, or complexed with hydroxycobalamin and MgATP
    • Bauer, C. B., Fonseca, M. V., Holden, H. M., Thoden, J. B., Thompson, T. B., Escalante-Semerena, J. C., and Rayment, I. (2001) Three-dimensional structure of ATP:corrinoid adenosyltransferase from Salmonella typhimurium in its free state, complexed with MgATP, or complexed with hydroxycobalamin and MgATP, Biochemistry 40, 361-374.
    • (2001) Biochemistry , vol.40 , pp. 361-374
    • Bauer, C.B.1    Fonseca, M.V.2    Holden, H.M.3    Thoden, J.B.4    Thompson, T.B.5    Escalante-Semerena, J.C.6    Rayment, I.7


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