메뉴 건너뛰기




Volumn 42, Issue 18, 2003, Pages 5378-5386

Kinetic mechanism and enantioselectivity of halohydrin dehalogenase from agrobacterium radiobacter

Author keywords

[No Author keywords available]

Indexed keywords

ENANTIOSELECTIVITY;

EID: 0038219597     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0273361     Document Type: Article
Times cited : (57)

References (31)
  • 1
    • 0022646837 scopus 로고
    • Assessment of the impact of the emission of certain organochlorin compounds on the aquatic environment. Part 3: Epichlorohydrin
    • Krijgsheld, K. R., and van de Gen, A. (1986) Assessment of the impact of the emission of certain organochlorin compounds on the aquatic environment. Part 3: epichlorohydrin, Chemosphere 15, 881-893.
    • (1986) Chemosphere , vol.15 , pp. 881-893
    • Krijgsheld, K.R.1    Van de Gen, A.2
  • 3
    • 0037062592 scopus 로고    scopus 로고
    • Raman evidence for Meisenheimer complex formation in the hydrolysis reactions of 4-fluorobenzoyl-and 4-nitrobenzoyl-coenzyme A catalyzed by 4-chlorobenzoyl-coenzyme A dehalogenase
    • Dong, J., Carey, P. R., Wei, Y., Luo, L., Lu, X., Liu, R. Q., and Dunaway-Mariano, D. (2002) Raman evidence for Meisenheimer complex formation in the hydrolysis reactions of 4-fluorobenzoyl-and 4-nitrobenzoyl-coenzyme A catalyzed by 4-chlorobenzoyl-coenzyme A dehalogenase, Biochemistry 41, 7453-7463.
    • (2002) Biochemistry , vol.41 , pp. 7453-7463
    • Dong, J.1    Carey, P.R.2    Wei, Y.3    Luo, L.4    Lu, X.5    Liu, R.Q.6    Dunaway-Mariano, D.7
  • 4
    • 0035951110 scopus 로고    scopus 로고
    • Role of active site binding interactions in 4-chlorobenzoyl-coenzyme A dehalogenase catalysis
    • Luo, L., Taylor, K. L., Xiang, H., Wei, Y., Zhang, W., and Dunaway-Mariano, D. (2001) Role of active site binding interactions in 4-chlorobenzoyl-coenzyme A dehalogenase catalysis, Biochemistry, 40, 15684-15692.
    • (2001) Biochemistry , vol.40 , pp. 15684-15692
    • Luo, L.1    Taylor, K.L.2    Xiang, H.3    Wei, Y.4    Zhang, W.5    Dunaway-Mariano, D.6
  • 7
    • 0027280086 scopus 로고
    • Refined X-ray structures of haloalkane dehalogenase at pH 6.2 and pH 8.2 and implications for the reaction mechanism
    • Verschueren, K. H., Franken, S. M., Rozeboom, H. J., Kalk, K. H., and Dijkstra, B. W. (1993) Refined X-ray structures of haloalkane dehalogenase at pH 6.2 and pH 8.2 and implications for the reaction mechanism, J. Mol. Biol. 232, 856-872.
    • (1993) J. Mol. Biol. , vol.232 , pp. 856-872
    • Verschueren, K.H.1    Franken, S.M.2    Rozeboom, H.J.3    Kalk, K.H.4    Dijkstra, B.W.5
  • 8
    • 0027819259 scopus 로고
    • Crystallographic and fluorescence studies of the interaction of haloalkane dehalogenase with halide ions. Studies with halide compounds reveal a halide binding site in the active site
    • Verschueren, K. H., Kingma, J., Rozeboom, H. J., Kalk, K. H., Janssen, D. B., and Dijkstra, B. W. (1993) Crystallographic and fluorescence studies of the interaction of haloalkane dehalogenase with halide ions. Studies with halide compounds reveal a halide binding site in the active site, Biochemistry 32, 9031-9037.
    • (1993) Biochemistry , vol.32 , pp. 9031-9037
    • Verschueren, K.H.1    Kingma, J.2    Rozeboom, H.J.3    Kalk, K.H.4    Janssen, D.B.5    Dijkstra, B.W.6
  • 9
    • 0027337615 scopus 로고
    • Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase
    • Verschueren, K. H., Seljee, F., Rozeboom, H. J., Kalk, K. H., and Dijkstra, B. W. (1993) Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase, Nature 363, 693-698.
    • (1993) Nature , vol.363 , pp. 693-698
    • Verschueren, K.H.1    Seljee, F.2    Rozeboom, H.J.3    Kalk, K.H.4    Dijkstra, B.W.5
  • 10
    • 0029786674 scopus 로고    scopus 로고
    • Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL: An α/β hydrolase structure that is different from the α/β hydrolase fold
    • Hisano, T., Hata, Y., Fujii, T., Liu, J. Q., Kurihara, T., Esaki, N., and Soda, K. (1996) Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL: an α/β hydrolase structure that is different from the α/β hydrolase fold, J. Biol. Chem. 271, 20322-20330.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20322-20330
    • Hisano, T.1    Hata, Y.2    Fujii, T.3    Liu, J.Q.4    Kurihara, T.5    Esaki, N.6    Soda, K.7
  • 11
    • 0032524179 scopus 로고    scopus 로고
    • Synthesis of chiral epihalohydrins using haloalcohol dehalogenase A from Arthrobacter erithii H10a
    • Assis, H. M., Bull, A. T., and Hardman, D. J. (1998) Synthesis of chiral epihalohydrins using haloalcohol dehalogenase A from Arthrobacter erithii H10a, Enzyme Microbiol. Technol. 22, 545- 551.
    • (1998) Enzyme Microbiol. Technol. , vol.22 , pp. 545-551
    • Assis, H.M.1    Bull, A.T.2    Hardman, D.J.3
  • 14
    • 0032479816 scopus 로고    scopus 로고
    • Chiral C3 epoxides and halohydrins: Their preparation and synthetic application
    • Kasai, N., Suzuki, T., and Furukawa, Y. (1998) Chiral C3 epoxides and halohydrins: their preparation and synthetic application, J. Mol. Catal. 4, 237-252.
    • (1998) J. Mol. Catal. , vol.4 , pp. 237-252
    • Kasai, N.1    Suzuki, T.2    Furukawa, Y.3
  • 16
    • 0019880773 scopus 로고
    • Mechanistic studies of epoxide hydrolase utilizing a continuous spectrophotometric assay
    • Westkaemper, R. B., and Hanzlik, R. P. (1981) Mechanistic studies of epoxide hydrolase utilizing a continuous spectrophotometric assay, Arch. Biochem. Biophys. 208, 195-204.
    • (1981) Arch. Biochem. Biophys. , vol.208 , pp. 195-204
    • Westkaemper, R.B.1    Hanzlik, R.P.2
  • 18
    • 0030969017 scopus 로고    scopus 로고
    • Primary structure and catalytic mechanism of epoxide hydrolase from Agrobacterium radiobacter AD1
    • Rink, R., Fennema, M., Smids, M., Dehmel, U., and Janssen, D. B. (1997) Primary structure and catalytic mechanism of epoxide hydrolase from Agrobacterium radiobacter AD1, J. Biol. Chem. 272, 14650-14657.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14650-14657
    • Rink, R.1    Fennema, M.2    Smids, M.3    Dehmel, U.4    Janssen, D.B.5
  • 19
    • 0037074924 scopus 로고    scopus 로고
    • Improved stability of halohydrin dehalogenase from Agrobacterium radiobacter AD1 by replacement of cysteine residues
    • Tang, L., van Hylckama Vlieg, J. E. T., Lutje Spelberg, J. H., Fraaije, M. W., and Janssen, D. B. (2002) Improved stability of halohydrin dehalogenase from Agrobacterium radiobacter AD1 by replacement of cysteine residues, Enzyme Microbiol. Technol. 30, 251-258.
    • (2002) Enzyme Microbiol. Technol. , vol.30 , pp. 251-258
    • Tang, L.1    Van Hylckama Vlieg, J.E.T.2    Lutje Spelberg, J.H.3    Fraaije, M.W.4    Janssen, D.B.5
  • 20
    • 0001520086 scopus 로고
    • Determination of trace amounts of chlorine in naphtha
    • Bergmann, J. G., and Sanik, J. (1957) Determination of trace amounts of chlorine in naphtha, Anal. Chem. 29, 241-243.
    • (1957) Anal. Chem. , vol.29 , pp. 241-243
    • Bergmann, J.G.1    Sanik, J.2
  • 22
    • 0037054398 scopus 로고    scopus 로고
    • Exploration of the biocatalytic potential of a halohydrin dehalogenase using chromogenic substrates
    • Lutje Spelberg, J. H., Tang, L., van Gelder, M., Kellogg, R. M., and Janssen, D. B. (2002) Exploration of the biocatalytic potential of a halohydrin dehalogenase using chromogenic Substrates, Tetrahedron: Asymmetry 13, 1083-1089.
    • (2002) Tetrahedron: Asymmetry , vol.13 , pp. 1083-1089
    • Lutje Spelberg, J.H.1    Tang, L.2    Van Gelder, M.3    Kellogg, R.M.4    Janssen, D.B.5
  • 23
    • 0003013146 scopus 로고
    • (Boyer, P. D., Ed.), 4th Ed. Academic Press, New York
    • Jonson, K. A. (1992) The enzymes (Boyer, P. D., Ed.), 4th ed., Vol. 20, pp 1-60, Academic Press, New York.
    • (1992) The Enzymes , vol.20 , pp. 1-60
    • Jonson, K.A.1
  • 24
    • 0018681639 scopus 로고
    • Derivation of initial velocity and isotope exchange rate equations
    • Huang, C. Y. (1979) Derivation of initial velocity and isotope exchange rate equations, Methods Enzymol. 63, 54-84.
    • (1979) Methods Enzymol. , vol.63 , pp. 54-84
    • Huang, C.Y.1
  • 25
    • 0033524351 scopus 로고    scopus 로고
    • Kinetic studies on the enzyme (S)-hydroxynitrile lyase from Hevea brasiliensis using initial rate methods and progress curve analysis
    • Bauer, M., Griengl, H., and Steiner, W. (1999) Kinetic studies on the enzyme (S)-hydroxynitrile lyase from Hevea brasiliensis using initial rate methods and progress curve analysis, Biotechnol. Bioeng. 62, 20-29.
    • (1999) Biotechnol. Bioeng. , vol.62 , pp. 20-29
    • Bauer, M.1    Griengl, H.2    Steiner, W.3
  • 27
    • 50549155520 scopus 로고
    • The kinetics of enzyme-catalyzed reactions with two or more substrates or products: III. Prediction of initial velocity and inhibition patterns by inspection
    • Cleland, W. W. (1963) The kinetics of enzyme-catalyzed reactions with two or more substrates or products: III. Prediction of initial velocity and inhibition patterns by inspection, Biochim. Biophys. Acta 67, 188-196.
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 188-196
    • Cleland, W.W.1
  • 28
    • 0028300363 scopus 로고
    • Replacement of catalytic histidine-195 of chloramphenicol acetyltransferase: Evidence for a general base role for glutamate
    • Lewendon, A., Murray, I. A., Shaw, W. V., Gibbs, M. R., and Leslie, A. G. (1994) Replacement of catalytic histidine-195 of chloramphenicol acetyltransferase: evidence for a general base role for glutamate, Biochemistry 33, 1944-1950,
    • (1994) Biochemistry , vol.33 , pp. 1944-1950
    • Lewendon, A.1    Murray, I.A.2    Shaw, W.V.3    Gibbs, M.R.4    Leslie, A.G.5
  • 29
    • 0028915619 scopus 로고
    • Histidine 289 is essential for hydrolysis of the alkyl-enzyme intermediate of haloalkane dehalogenase
    • Pries, F., Kingma, J., Krooshof, G. H., Jeronimus-Stratingh, C. M., Bruins, A. P., and Janssen, D. B. (1995) Histidine 289 is essential for hydrolysis of the alkyl-enzyme intermediate of haloalkane dehalogenase, J. Biol. Chem. 270, 10405-10411.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10405-10411
    • Pries, F.1    Kingma, J.2    Krooshof, G.H.3    Jeronimus-Stratingh, C.M.4    Bruins, A.P.5    Janssen, D.B.6
  • 30
    • 15844362298 scopus 로고    scopus 로고
    • Specificity and kinetics of haloalkane dehalogenase
    • Schanstra, J. P., Kingma, J., and Janssen, D. B. (1996) Specificity and kinetics of haloalkane dehalogenase, J. Biol. Chem. 271, 14747-14753.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14747-14753
    • Schanstra, J.P.1    Kingma, J.2    Janssen, D.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.