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Volumn 43, Issue 33, 2004, Pages 10619-10627

Mechanism of cobyrinic acid a,c-diamide synthetase from Salmonella typhimurium LT2

Author keywords

[No Author keywords available]

Indexed keywords

ACIDS; ADENOSINETRIPHOSPHATE; AMMONIA; BIOSYNTHESIS; CATALYSIS; HYDROLYSIS; ISOTOPES; MONOMERS; PROTEINS; SYNTHESIS (CHEMICAL); VITAMINS;

EID: 4143095851     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048972x     Document Type: Article
Times cited : (25)

References (31)
  • 5
    • 0032190037 scopus 로고    scopus 로고
    • 12) biosynthesis: Functional characterization of the Bacillus megaterium cbi genes required to convert uroporphyrinogen III into cobyrinic acid a,c-diamide
    • 12) biosynthesis: Functional characterization of the Bacillus megaterium cbi genes required to convert uroporphyrinogen III into cobyrinic acid a,c-diamide, Biochem. J. 335, 167-173.
    • (1998) Biochem. J. , vol.335 , pp. 167-173
    • Raux, E.1    Lanois, A.2    Rambach, A.3    Warren, M.J.4    Thermes, C.5
  • 8
    • 0025155625 scopus 로고
    • Purification and characterization of cobyrinic acid a,c-diamide synthase from Pseudomonas denitrificans
    • Debussche, L., Thibaut, D., Cameron, B., Crouzet, J., and Blanche, F. J. (1990) Purification and characterization of cobyrinic acid a,c-diamide synthase from Pseudomonas denitrificans, J. Bacteriol. 172, 6239-6244.
    • (1990) J. Bacteriol. , vol.172 , pp. 6239-6244
    • Debussche, L.1    Thibaut, D.2    Cameron, B.3    Crouzet, J.4    Blanche, F.J.5
  • 9
    • 0034333084 scopus 로고    scopus 로고
    • The synthetase domains of cobalamin biosynthesis amidotransferases cobB and cobQ belong to a new family of ATP-dependent amidoligases, related to dethiobiotin synthetase
    • Galperin, M. Y., and Grishin, N. V. (2000) The synthetase domains of cobalamin biosynthesis amidotransferases cobB and cobQ belong to a new family of ATP-dependent amidoligases, related to dethiobiotin synthetase, Proteins 41, 238-247.
    • (2000) Proteins , vol.41 , pp. 238-247
    • Galperin, M.Y.1    Grishin, N.V.2
  • 10
    • 0030957783 scopus 로고    scopus 로고
    • Structure of carbamoyl phosphate synthetase: A journey of 96 Å from substrate to product
    • Thoden, J. B., Holden, H. M., Wesenberg, G., Raushel, F. M., and Rayment, I. (1997) Structure of carbamoyl phosphate synthetase: A journey of 96 Å from substrate to product, Biochemistry 36, 6305-6316.
    • (1997) Biochemistry , vol.36 , pp. 6305-6316
    • Thoden, J.B.1    Holden, H.M.2    Wesenberg, G.3    Raushel, F.M.4    Rayment, I.5
  • 11
    • 0025925330 scopus 로고
    • 12: Stepwise amidation of carboxyl groups b, d, e, and g of cobyrinic acid a,c-diamide is catalyzed by one enzyme in Pseudomonas denitrificans
    • 12: Stepwise amidation of carboxyl groups b, d, e, and g of cobyrinic acid a,c-diamide is catalyzed by one enzyme in Pseudomonas denitrificans, J. Bacteriol. 173, 6046-6051.
    • (1991) J. Bacteriol. , vol.173 , pp. 6046-6051
    • Blanche, F.1    Couder, M.2    Debussche, L.3    Thibaut, D.4    Cameron, B.5    Crouzet, J.6
  • 12
    • 0029118765 scopus 로고
    • Mechanism of an ATP-dependent carboxylase, dethiobiotin synthetase, based on crystal-lographic studies of complexes with substrates and a reaction intermediate
    • Huang, W., Jia, J., Gibson, K. J., Taylor, W. S., Rendina, A. R., Schneider, G., and Lindqvist, Y. (1995) Mechanism of an ATP-dependent carboxylase, dethiobiotin synthetase, based on crystal-lographic studies of complexes with substrates and a reaction intermediate, Biochemistry 34, 10985-10995.
    • (1995) Biochemistry , vol.34 , pp. 10985-10995
    • Huang, W.1    Jia, J.2    Gibson, K.J.3    Taylor, W.S.4    Rendina, A.R.5    Schneider, G.6    Lindqvist, Y.7
  • 14
    • 0026039677 scopus 로고
    • The MinD protein is a membrane ATPase required for the correct placement of the Escherichia coli division site
    • De Boer, P. A., Crossley, R. E., Hand, A. R., and Rothfield, L. I. (1991) The MinD protein is a membrane ATPase required for the correct placement of the Escherichia coli division site, EMBO J. 10, 4371-4380.
    • (1991) EMBO J. , vol.10 , pp. 4371-4380
    • De Boer, P.A.1    Crossley, R.E.2    Hand, A.R.3    Rothfield, L.I.4
  • 15
    • 0033554863 scopus 로고    scopus 로고
    • Characterization of a novel dUTP-dependent activity of CTP synthetase from Saccharomyces cerevisiae
    • Pappas, A., Park, T. S., and Carman, G. M. (1999) Characterization of a novel dUTP-dependent activity of CTP synthetase from Saccharomyces cerevisiae, Biochemistry 38, 16671-16677.
    • (1999) Biochemistry , vol.38 , pp. 16671-16677
    • Pappas, A.1    Park, T.S.2    Carman, G.M.3
  • 16
    • 0028912102 scopus 로고
    • Novel protein families in archaean genomes
    • Ouzonis, C., Kyrpides, N., and Sander, C. (1995) Novel protein families in archaean genomes, Nucleic Acids Res. 23, 565-570.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 565-570
    • Ouzonis, C.1    Kyrpides, N.2    Sander, C.3
  • 17
    • 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. (2002) Classification and evolution of P-loop GTPases and related ATPases, J. Mol. Biol. 317, 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
  • 22
    • 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
  • 23
    • 0037040295 scopus 로고    scopus 로고
    • Inactivation of the amidotransferase activity of carbamoyl phosphate synthetase by the antibiotic acivicin
    • Miles, B. W., Thoden, J. B., Holden, H. M., and Raushel, F. M. (2002) Inactivation of the amidotransferase activity of carbamoyl phosphate synthetase by the antibiotic acivicin, J. Biol. Chem. 277, 4368-4373.
    • (2002) J. Biol. Chem. , vol.277 , pp. 4368-4373
    • Miles, B.W.1    Thoden, J.B.2    Holden, H.M.3    Raushel, F.M.4
  • 24
    • 0025076610 scopus 로고
    • Identification and quantitation of corrinoid precursors of cobalamin from Pseudomonas denitrificans by high-performance liquid chromatography
    • Blanche, F., Thibaut, D., Couder, M., and Muller, J. C. (1990) Identification and quantitation of corrinoid precursors of cobalamin from Pseudomonas denitrificans by high-performance liquid chromatography, Anal. Biochem. 189, 24-29.
    • (1990) Anal. Biochem. , vol.189 , pp. 24-29
    • Blanche, F.1    Thibaut, D.2    Couder, M.3    Muller, J.C.4
  • 25
    • 0028269406 scopus 로고
    • Analysis of progress curves for enzyme-catalyzed reactions: Application to unstable enzymes, coupled reactions, and transient-state kinetics
    • Duggleby, R. G. (1994) Analysis of progress curves for enzyme-catalyzed reactions: Application to unstable enzymes, coupled reactions, and transient-state kinetics, Biochim. Biophys. Acta 1205, 268-274.
    • (1994) Biochim. Biophys. Acta , vol.1205 , pp. 268-274
    • Duggleby, R.G.1
  • 26
    • 0013612812 scopus 로고
    • Steady-state kinetics
    • Cleland, W. W. (1970) Steady-state kinetics, The Enzymes 3rd ed., Vol. 2, pp 1-65.
    • (1970) The Enzymes 3rd Ed. , vol.2 , pp. 1-65
    • Cleland, W.W.1
  • 27
    • 0017089363 scopus 로고
    • A stereochemical method for detection of ATP terminal phosphate transfer in enzymatic reactions
    • Midelfort, C., and Rose, I. A. (1976) A stereochemical method for detection of ATP terminal phosphate transfer in enzymatic reactions, J. Biol. Chem. 251, 5881-5888.
    • (1976) J. Biol. Chem. , vol.251 , pp. 5881-5888
    • Midelfort, C.1    Rose, I.A.2
  • 28
    • 0018788328 scopus 로고
    • Paramagnetic probes for carbamoyl-phosphate synthetase: Metal ion binding studies and preparation of nitroxide spin-labeled derivatives
    • Raushel, F. M., Rawding, C. J., Anderson, P. M., and Villafranca, J. J. (1979) Paramagnetic probes for carbamoyl-phosphate synthetase: Metal ion binding studies and preparation of nitroxide spin-labeled derivatives, Biochemistry 18, 5562-5566.
    • (1979) Biochemistry , vol.18 , pp. 5562-5566
    • Raushel, F.M.1    Rawding, C.J.2    Anderson, P.M.3    Villafranca, J.J.4
  • 29
    • 0029920154 scopus 로고    scopus 로고
    • Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site
    • Kim, H. K., Krahn, J. M., Tomchick, D. R., Smith, J. L., and Zalkin, H. (1996) Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site, J. Biol. Chem. 271, 15549-15557.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15549-15557
    • Kim, H.K.1    Krahn, J.M.2    Tomchick, D.R.3    Smith, J.L.4    Zalkin, H.5
  • 30
    • 0037404142 scopus 로고    scopus 로고
    • Revisiting the steady-state kinetic mechanism of glutamine-dependent asparagine synthetase from Escherichia coli
    • Tesson, A. R., Soper, T. S., Ciustea, M., and Richards, N. G. (2003) Revisiting the steady-state kinetic mechanism of glutamine-dependent asparagine synthetase from Escherichia coli Arch. Biochem. Biophys. 413, 23-31.
    • (2003) Arch. Biochem. Biophys. , vol.413 , pp. 23-31
    • Tesson, A.R.1    Soper, T.S.2    Ciustea, M.3    Richards, N.G.4
  • 31
    • 0030933184 scopus 로고    scopus 로고
    • Active site mutants of Escherichia coli dethiobiotin synthetase: Effects of mutations on enzyme catalytic and structural properties
    • Yang, G., Sandalova, T., Lohman, K., Lindqvist, Y., and Rendina, A. R. (1997) Active site mutants of Escherichia coli dethiobiotin synthetase: Effects of mutations on enzyme catalytic and structural properties, Biochemistry 36, 4751-4760.
    • (1997) Biochemistry , vol.36 , pp. 4751-4760
    • Yang, G.1    Sandalova, T.2    Lohman, K.3    Lindqvist, Y.4    Rendina, A.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.