메뉴 건너뛰기




Volumn 43, Issue 19, 2004, Pages 5707-5715

Mechanism for the Hydrolysis of Organophosphates by the Bacterial Phosphotriesterase

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CATALYSIS; CHEMICAL ACTIVATION; ENZYMES; HYDROLYSIS; OXYGEN; PH EFFECTS; PHOSPHORUS COMPOUNDS; SULFUR; ZINC;

EID: 2442496666     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0497805     Document Type: Article
Times cited : (268)

References (27)
  • 1
    • 0024316913 scopus 로고
    • Purification and properties of the phosphotriesterase from Pseudomonas diminuta
    • Dumas, D. P., Caldwell, S. R., Wild, J. R., and Raushel, F. M. (1989) Purification and properties of the phosphotriesterase from Pseudomonas diminuta, J. Biol. Chem. 264, 19659-19665.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19659-19665
    • Dumas, D.P.1    Caldwell, S.R.2    Wild, J.R.3    Raushel, F.M.4
  • 2
    • 0024008341 scopus 로고
    • Cloning and sequencing of a plasmid-borne gene (opd) encoding a phosphotriesterase
    • McDaniel, C. S., Harper, L. L., and Wild, J. R. (1988) Cloning and sequencing of a plasmid-borne gene (opd) encoding a phosphotriesterase, J. Bacteriol. 170, 2306-2311.
    • (1988) J. Bacteriol. , vol.170 , pp. 2306-2311
    • McDaniel, C.S.1    Harper, L.L.2    Wild, J.R.3
  • 3
    • 0028288223 scopus 로고
    • Identification of the histidine ligands to the binuclear metal center of phosphotriesterase by site-directed mutagenesis
    • Kuo, J. M., and Raushel, F. M. (1994) Identification of the histidine ligands to the binuclear metal center of phosphotriesterase by site-directed mutagenesis, Biochemistry 33, 4265-4272.
    • (1994) Biochemistry , vol.33 , pp. 4265-4272
    • Kuo, J.M.1    Raushel, F.M.2
  • 4
    • 0026748791 scopus 로고
    • Characterization of the zinc binding site of bacterial phosphotriesterase
    • Omburo, G. A., Kuo, J. M., Mullins, L. S., and Raushel, F. M. (1992) Characterization of the zinc binding site of bacterial phosphotriesterase, J. Biol. Chem. 267, 13278-13283.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13278-13283
    • Omburo, G.A.1    Kuo, J.M.2    Mullins, L.S.3    Raushel, F.M.4
  • 6
    • 0025117439 scopus 로고
    • Inactivation of organophosphorus nerve agents by the phosphotriesterase from Pseudomonas diminuta
    • Dumas, D. P., Durst, H. D., Landis, W. G., Raushel, F. M., and Wild, J. R. (1990) Inactivation of organophosphorus nerve agents by the phosphotriesterase from Pseudomonas diminuta, Arch. Biochem. Biophys. 277, 155-159.
    • (1990) Arch. Biochem. Biophys. , vol.277 , pp. 155-159
    • Dumas, D.P.1    Durst, H.D.2    Landis, W.G.3    Raushel, F.M.4    Wild, J.R.5
  • 8
    • 0024281297 scopus 로고
    • Mechanism and stereochemical course at phosphorus of the reaction catalyzed by a bacterial phosphotriesterase
    • Lewis, V. E., Donarski, W. J., Wild, J. R., and Raushel, F. M. (1988) Mechanism and stereochemical course at phosphorus of the reaction catalyzed by a bacterial phosphotriesterase, Biochemistry 27, 1591-1597.
    • (1988) Biochemistry , vol.27 , pp. 1591-1597
    • Lewis, V.E.1    Donarski, W.J.2    Wild, J.R.3    Raushel, F.M.4
  • 9
    • 0028609492 scopus 로고
    • Three-dimensional structure of phosphotriesterase: An enzyme capable of detoxifying organophosphate nerve agents
    • Benning, M. M., Kuo, J. M., Raushel, F. M., and Holden, H. M. (1994) Three-dimensional structure of phosphotriesterase: an enzyme capable of detoxifying organophosphate nerve agents, Biochemistry 33, 15001-15007.
    • (1994) Biochemistry , vol.33 , pp. 15001-15007
    • Benning, M.M.1    Kuo, J.M.2    Raushel, F.M.3    Holden, H.M.4
  • 10
    • 0031000649 scopus 로고    scopus 로고
    • An evolutionary treasure: Unification of a broad set of amidohydrolases related to urease
    • Holm, L., and Sander, C. (1997) An evolutionary treasure: unification of a broad set of amidohydrolases related to urease, Proteins 28, 72-82.
    • (1997) Proteins , vol.28 , pp. 72-82
    • Holm, L.1    Sander, C.2
  • 11
    • 0034720769 scopus 로고    scopus 로고
    • Self-assembly of the binuclear metal center of phosphotriesterase
    • Shim, H., and Raushel, F. M. (2000) Self-assembly of the binuclear metal center of phosphotriesterase, Biochemistry 39, 7357-7364.
    • (2000) Biochemistry , vol.39 , pp. 7357-7364
    • Shim, H.1    Raushel, F.M.2
  • 12
    • 0035819590 scopus 로고    scopus 로고
    • Mobility of the active site bound paraoxon and sarin in zinc-phosphotriesterase by molecular dynamics simulation and quantum chemical calculation
    • Koca, J., Zhan, C. G., Rittenhouse, R. C., and Ornstein, R. L. (2001) Mobility of the active site bound paraoxon and sarin in zinc-phosphotriesterase by molecular dynamics simulation and quantum chemical calculation, J. Am. Chem. Soc. 123, 817-826.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 817-826
    • Koca, J.1    Zhan, C.G.2    Rittenhouse, R.C.3    Ornstein, R.L.4
  • 13
    • 0024340489 scopus 로고
    • Structure-activity relationships in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta
    • Donarski, W. J., Dumas, D. P., Heitmeyer, D. P., Lewis, V. E., and Raushel, F. M. (1989) Structure-activity relationships in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta, Biochemistry 28, 4650-4655.
    • (1989) Biochemistry , vol.28 , pp. 4650-4655
    • Donarski, W.J.1    Dumas, D.P.2    Heitmeyer, D.P.3    Lewis, V.E.4    Raushel, F.M.5
  • 14
    • 0025836538 scopus 로고
    • Limits of diffusion in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta
    • Caldwell, S. R., Newcomb, J. R., Schlecht, K. A., and Raushel, F. M. (1991) Limits of diffusion in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta, Biochemistry 30, 7438-7444.
    • (1991) Biochemistry , vol.30 , pp. 7438-7444
    • Caldwell, S.R.1    Newcomb, J.R.2    Schlecht, K.A.3    Raushel, F.M.4
  • 15
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction, Gene 77, 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 16
    • 0343580454 scopus 로고    scopus 로고
    • Perturbations to the active site of phosphotriesterase
    • Kuo, J. M., Chae, M. Y., and Raushel, F. M. (1997) Perturbations to the active site of phosphotriesterase, Biochemistry 36, 1982-1988.
    • (1997) Biochemistry , vol.36 , pp. 1982-1988
    • Kuo, J.M.1    Chae, M.Y.2    Raushel, F.M.3
  • 17
    • 0020346954 scopus 로고
    • Solvent isotope effects of enzyme systems
    • Schowen, K. B., and Schowen, R. L. (1982) Solvent isotope effects of enzyme systems, Methods Enzymol. 87, 551-606.
    • (1982) Methods Enzymol. , vol.87 , pp. 551-606
    • Schowen, K.B.1    Schowen, R.L.2
  • 18
    • 0029759529 scopus 로고    scopus 로고
    • Metal-substrate interactions facilitate the catalytic activity of the bacterial phosphotriesterase
    • Hong, S. B., and Raushel, F. M. (1996) Metal-substrate interactions facilitate the catalytic activity of the bacterial phosphotriesterase, Biochemistry 35, 10904-10912.
    • (1996) Biochemistry , vol.35 , pp. 10904-10912
    • Hong, S.B.1    Raushel, F.M.2
  • 19
    • 0000715625 scopus 로고
    • Hydrolysis of cations. Formation constants and standard free energies of formation of hydroxy complexes
    • Barnum, D. W. (1983) Hydrolysis of cations. Formation constants and standard free energies of formation of hydroxy complexes, Inorg. Chem. 22, 2297-2305.
    • (1983) Inorg. Chem. , vol.22 , pp. 2297-2305
    • Barnum, D.W.1
  • 20
    • 0034639450 scopus 로고    scopus 로고
    • Modeling carboxylate-bridged dinuclear active site in metalloenzymes using a novel naphthyridine-based dinucleating ligand
    • He, C., and Lippard, S. J. (2000) Modeling carboxylate-bridged dinuclear active site in metalloenzymes using a novel naphthyridine-based dinucleating ligand, J. Am. Chem. Soc. 122, 184-185.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 184-185
    • He, C.1    Lippard, S.J.2
  • 21
    • 0034709838 scopus 로고    scopus 로고
    • Reactivity of μ-hydroxodizinc (II) center in enzymatic catalysis through model studies
    • Kaminshaia, N. V., He, C., and Lippard, S. J. (2000) Reactivity of μ-hydroxodizinc (II) center in enzymatic catalysis through model studies, Inorg. Chem. 39, 3365-3373.
    • (2000) Inorg. Chem. , vol.39 , pp. 3365-3373
    • Kaminshaia, N.V.1    He, C.2    Lippard, S.J.3
  • 22
    • 0035814923 scopus 로고    scopus 로고
    • High-resolution X-ray structures of different metal-substituted forms of phosphotriesterase from Pseudomonas diminuta
    • Benning, M. M., Shim, H., Raushel, F. M., and Holden, H. M. (2001) High-resolution X-ray structures of different metal-substituted forms of phosphotriesterase from Pseudomonas diminuta, Biochemistry 40, 2712-2722.
    • (2001) Biochemistry , vol.40 , pp. 2712-2722
    • Benning, M.M.1    Shim, H.2    Raushel, F.M.3    Holden, H.M.4
  • 23
    • 0034730534 scopus 로고    scopus 로고
    • The binding of substrate analogues to phosphotriesterase
    • Benning, M. M., Hong, S. B., Raushel, F. M., and Holden, H. M. (2000) The binding of substrate analogues to phosphotriesterase, J. Biol. Chem. 275, 30556-30560.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30556-30560
    • Benning, M.M.1    Hong, S.B.2    Raushel, F.M.3    Holden, H.M.4
  • 24
    • 0029993512 scopus 로고    scopus 로고
    • Three-dimensional structure of the zinc-containing phosphotriesterase with the bound substrate analogue diethyl 4-methylbenzylphosphonate
    • Vanhooke, J. L., Benning M. M., Raushel, F. M., and Holden, H. M. (1996) Three-dimensional structure of the zinc-containing phosphotriesterase with the bound substrate analogue diethyl 4-methylbenzylphosphonate, Biochemistry 35, 6020-6025.
    • (1996) Biochemistry , vol.35 , pp. 6020-6025
    • Vanhooke, J.L.1    Benning, M.M.2    Raushel, F.M.3    Holden, H.M.4
  • 26
    • 0035912842 scopus 로고    scopus 로고
    • Molecular structure of dihydroorotase: A paradigm for catalysis through the use of a binuclear metal center
    • Thoden, J. B., Phillips, G. N., Jr., Neal, T. M., Raushel, F. M., and Holden, H. M. (2001) Molecular structure of dihydroorotase: a paradigm for catalysis through the use of a binuclear metal center, Biochemistry 40, 6989-6997.
    • (2001) Biochemistry , vol.40 , pp. 6989-6997
    • Thoden, J.B.1    Phillips Jr., G.N.2    Neal, T.M.3    Raushel, F.M.4    Holden, H.M.5
  • 27
    • 0018653912 scopus 로고
    • Interconversion of carbamoyl-L-aspartate and L-dihydroorotate by dihydroorotase from mouse Ehrlich ascites carcinoma
    • Christopherson, R. I., and Jones, M. E. (1979) Interconversion of carbamoyl-L-aspartate and L-dihydroorotate by dihydroorotase from mouse Ehrlich ascites carcinoma, J. Biol. Chem. 254, 12506-12512.
    • (1979) J. Biol. Chem. , vol.254 , pp. 12506-12512
    • Christopherson, R.I.1    Jones, M.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.