메뉴 건너뛰기




Volumn 4, Issue 2, 2000, Pages 207-213

Dimetallic hydrolases and their models

Author keywords

[No Author keywords available]

Indexed keywords

ACID PHOSPHATASE; COPPER COMPLEX; HYDROLASE; IRON COMPLEX; METAL; ZINC COMPLEX;

EID: 0034035617     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(99)00076-9     Document Type: Review
Times cited : (141)

References (30)
  • 1
    • 0029837557 scopus 로고    scopus 로고
    • Two-metal ion catalysis in enzymatic acyl- And phosphoryl- transfer reactions
    • Sträter N., Lipscomb W.N., Klabunde T., Krebs B. Two-metal ion catalysis in enzymatic acyl- and phosphoryl- transfer reactions. Angew Chem Int Ed Engl. 35:1996;2024-2055.
    • (1996) Angew Chem Int Ed Engl , vol.35 , pp. 2024-2055
    • Sträter, N.1    Lipscomb, W.N.2    Klabunde, T.3    Krebs, B.4
  • 2
    • 0001431264 scopus 로고    scopus 로고
    • Binuclear metallohydrolases
    • Wilcox D.E. Binuclear metallohydrolases. Chem Rev. 96:1996;2435-2458.
    • (1996) Chem Rev , vol.96 , pp. 2435-2458
    • Wilcox, D.E.1
  • 3
    • 0032477286 scopus 로고    scopus 로고
    • Sulfate activity of E. coli alkaline phosphatase demonstrates a functional link to arylsulfatases, an evolutionarily related enzyme family
    • O'Brien P.J., Herschlag D. Sulfate activity of E. coli alkaline phosphatase demonstrates a functional link to arylsulfatases, an evolutionarily related enzyme family. J Am Chem Soc. 120:1998;12369-12370.
    • (1998) J Am Chem Soc , vol.120 , pp. 12369-12370
    • O'Brien, P.J.1    Herschlag, D.2
  • 4
    • 0033514981 scopus 로고    scopus 로고
    • Rate-determining step of E. coli alkaline phosphatase altered by the removal of a positive charge at the active center
    • Sun L., Martin D.C., Kantrowitz E.R. Rate-determining step of E. coli alkaline phosphatase altered by the removal of a positive charge at the active center. Biochemistry. 38:1999;2842-2848.
    • (1999) Biochemistry , vol.38 , pp. 2842-2848
    • Sun, L.1    Martin, D.C.2    Kantrowitz, E.R.3
  • 5
    • 0030596529 scopus 로고    scopus 로고
    • Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures
    • Klabunde T., Sträter N., Fröhlich R., Witzel H., Krebs B. Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures. J Mol Biol. 259:1996;737-745.
    • (1996) J Mol Biol , vol.259 , pp. 737-745
    • Klabunde, T.1    Sträter, N.2    Fröhlich, R.3    Witzel, H.4    Krebs, B.5
  • 6
    • 0029583122 scopus 로고
    • Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate
    • Egloff M.P., Cohen P.T.W., Reinemar P., Barford D. Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate. J Mol Biol. 254:1995;942-959.
    • (1995) J Mol Biol , vol.254 , pp. 942-959
    • Egloff, M.P.1    Cohen, P.T.W.2    Reinemar, P.3    Barford, D.4
  • 7
    • 0025093863 scopus 로고
    • Crystallisation and preliminary crystallographic analysis of P1 nuclease from Penicillium citrinum
    • Lahm A., Volbeda A., Suck D. Crystallisation and preliminary crystallographic analysis of P1 nuclease from Penicillium citrinum. J Mol Biol. 215:1990;207-210.
    • (1990) J Mol Biol , vol.215 , pp. 207-210
    • Lahm, A.1    Volbeda, A.2    Suck, D.3
  • 8
    • 0029032588 scopus 로고
    • Three-dimensional structure of the binuclear metal center of phosphotriesterase
    • Benning M.M., Kuo J.M., Raushel F.M., Holden H.M. Three-dimensional structure of the binuclear metal center of phosphotriesterase. Biochemistry. 34:1995;7973-7978.
    • (1995) Biochemistry , vol.34 , pp. 7973-7978
    • Benning, M.M.1    Kuo, J.M.2    Raushel, F.M.3    Holden, H.M.4
  • 9
    • 0028889561 scopus 로고
    • Two-metal ion mechanism of bovine lens leucine aminopeptidase: Active site solvent structure and binding mode of L-leucinal, a gem-diolate transition state analogue, by X-ray crystallography
    • Sträter N., Lipscomb W.N. Two-metal ion mechanism of bovine lens leucine aminopeptidase: active site solvent structure and binding mode of L-leucinal, a gem-diolate transition state analogue, by X-ray crystallography. Biochemistry. 34:1995;14792-14800.
    • (1995) Biochemistry , vol.34 , pp. 14792-14800
    • Sträter, N.1    Lipscomb, W.N.2
  • 10
    • 0032556222 scopus 로고    scopus 로고
    • Direct observation of an enzyme-bound intermediate in the catalytic cycle of the metallo-β-lactamase from Bacteroides fragilis
    • Wang Z., Fast W., Benkovic S.J. Direct observation of an enzyme-bound intermediate in the catalytic cycle of the metallo-β-lactamase from Bacteroides fragilis. J Am Chem Soc. 120:1998;10788-10789.
    • (1998) J Am Chem Soc , vol.120 , pp. 10788-10789
    • Wang, Z.1    Fast, W.2    Benkovic, S.J.3
  • 11
    • 0033520073 scopus 로고    scopus 로고
    • On the mechanism of the metallo-beta-lactamase from Bacteroides fragilis
    • Wang Z., Fast W., Benkovic S.J. On the mechanism of the metallo-beta-lactamase from Bacteroides fragilis. Biochemistry. 38:1999;10013-10023.
    • (1999) Biochemistry , vol.38 , pp. 10013-10023
    • Wang, Z.1    Fast, W.2    Benkovic, S.J.3
  • 12
    • 0033523218 scopus 로고    scopus 로고
    • Structure and spectroscopy of metallo-lactamase active sites
    • Gilson H.S.R., Krauss M. Structure and spectroscopy of metallo-lactamase active sites. J Am Chem Soc. 121:1999;6984-6989.
    • (1999) J Am Chem Soc , vol.121 , pp. 6984-6989
    • Gilson, H.S.R.1    Krauss, M.2
  • 13
    • 84943968069 scopus 로고
    • Macrocyclic polyamines as a probe for equilibrium study of the acid function of Zn(II) in hydrolysis enzymes
    • Kimura E., Koike T. Macrocyclic polyamines as a probe for equilibrium study of the acid function of Zn(II) in hydrolysis enzymes. Commun Inorg Chem. 11:1991;285-301.
    • (1991) Commun Inorg Chem , vol.11 , pp. 285-301
    • Kimura, E.1    Koike, T.2
  • 14
    • 77956774360 scopus 로고    scopus 로고
    • Intrinstic properties of Zn(II) pertinent to zinc enzymes
    • A.G. Sykes. San Diego: Academic Press
    • Kimura E., Koike T. Intrinstic properties of Zn(II) pertinent to zinc enzymes. Sykes A.G. Advances in Inorganic Chemistry (Vol. 44). 1996;229-261 Academic Press, San Diego.
    • (1996) Advances in Inorganic Chemistry (Vol. 44) , pp. 229-261
    • Kimura, E.1    Koike, T.2
  • 15
    • 0033520085 scopus 로고    scopus 로고
    • Evidence for nonbridged coordination of p-nitrophenyl phosphate to the dinuclear Fe(III)-M(II) center in bovine spleen purple acid phosphatase during enzymatic turnover
    • For the first time, the pH-dependent phosphate biding mode has been carefully studied by kinetic approach.
    • Merkx M., Pinkse M.W.H., Averill B.A. Evidence for nonbridged coordination of p-nitrophenyl phosphate to the dinuclear Fe(III)-M(II) center in bovine spleen purple acid phosphatase during enzymatic turnover. Biochemistry. 38:1999;9914-9925. For the first time, the pH-dependent phosphate biding mode has been carefully studied by kinetic approach.
    • (1999) Biochemistry , vol.38 , pp. 9914-9925
    • Merkx, M.1    Pinkse, M.W.H.2    Averill, B.A.3
  • 16
    • 0033520112 scopus 로고    scopus 로고
    • Fluoride inhibition of bovine spleen purple acid phosphatase: Characterization of a ternary enzyme-phosphate-fluoride complex as a model for the active enzyme-substrate-hydroxide complex
    • •].
    • •].
    • (1999) Biochemistry , vol.38 , pp. 9926-9936
    • Pinkse, M.W.H.1    Merkx, M.2    Averill, B.A.3
  • 18
    • 0029989358 scopus 로고    scopus 로고
    • X-ray absorption spectroscopic studies of the FeZn derivative of uteroferrin
    • Wang X., Randall C.R., True A.E., Que L. X-ray absorption spectroscopic studies of the FeZn derivative of uteroferrin. Biochemistry. 35:1996;13946-13954.
    • (1996) Biochemistry , vol.35 , pp. 13946-13954
    • Wang, X.1    Randall, C.R.2    True, A.E.3    Que, L.4
  • 20
    • 0033553145 scopus 로고    scopus 로고
    • A structural and functional model of dinuclear metallophosphatases
    • -)) bridging the two metal centers might be a nucleophile in phosphatase enzymes.
    • -)) bridging the two metal centers might be a nucleophile in phosphatase enzymes.
    • (1999) J Am Chem Soc , vol.121 , pp. 3341-3348
    • Williams, N.H.1    Lebuis, A.M.2    Chin, J.3
  • 21
    • 0032547320 scopus 로고    scopus 로고
    • Reactivity of phosphate diesters doubly coordinated to a dinuclear Cobalt(III) complex: Dependence of the reactivity on the basicity of the leaving group
    • +) model complex, the authors presented enormous cooperativity of the bridging oxide nucleophile and the activation of phosphate esters.
    • +) model complex, the authors presented enormous cooperativity of the bridging oxide nucleophile and the activation of phosphate esters.
    • (1998) J Am Chem Soc , vol.120 , pp. 8079-8087
    • Williams, N.H.1    Cheung, W.2    Chin, J.3
  • 22
    • 14844285583 scopus 로고    scopus 로고
    • Structure of a (μ-oxo)(dihydroxo)diiron(III) complex and its reactivity toward phosphodiesters
    • Duboc-Toia C., Ménage S., Vincent J.M., Averbuch-Pouchot M.T., Fontecave M. Structure of a (μ-oxo)(dihydroxo)diiron(III) complex and its reactivity toward phosphodiesters. Inorg Chem. 36:1997;6148-6149.
    • (1997) Inorg Chem , vol.36 , pp. 6148-6149
    • Duboc-Toia, C.1    Ménage, S.2    Vincent, J.M.3    Averbuch-Pouchot, M.T.4    Fontecave, M.5
  • 23
    • 0001689887 scopus 로고    scopus 로고
    • Functional model complexes for dinuclear phosphoesterase enzymes
    • London: JAI Press Inc.; This review covers recent models for dinuclear phosphatases that are not described in this paper
    • Krämer, R., Gajda, T.: Functional model complexes for dinuclear phosphoesterase enzymes. In Perspectives on Bioinorganic Chemistries. London: JAI Press Inc.; 1999, 4:209-240. This review covers recent models for dinuclear phosphatases that are not described in this paper.
    • (1999) In Perspectives on Bioinorganic Chemistries , vol.4 , pp. 209-240
    • Krämer, R.1    Gajda, T.2
  • 24
    • 33749084503 scopus 로고    scopus 로고
    • Dinuclear copper(II) complexes that promote hydrolysis of GpppG, a model for the 5′-cap of mRNA
    • McCue K.P., Voss D.A., Marks C., Morrow J.R. Dinuclear copper(II) complexes that promote hydrolysis of GpppG, a model for the 5′-cap of mRNA. J Chem Soc Dalton Trans. 1998;2961-2963.
    • (1998) J Chem Soc Dalton Trans , pp. 2961-2963
    • McCue, K.P.1    Voss, D.A.2    Marks, C.3    Morrow, J.R.4
  • 25
    • 0032542328 scopus 로고    scopus 로고
    • Conjugates of a dinuclear zinc(II) complex and DNA oligomers as novel sequence-selective artificial ribonuclease
    • Matsuda S., Ishikubo A., Kuzuya A., Yashiro M., Komiyama M. Conjugates of a dinuclear zinc(II) complex and DNA oligomers as novel sequence-selective artificial ribonuclease. Angew Chem Int Ed Eng. 37:1998;3284-3286.
    • (1998) Angew Chem Int Ed Eng , vol.37 , pp. 3284-3286
    • Matsuda, S.1    Ishikubo, A.2    Kuzuya, A.3    Yashiro, M.4    Komiyama, M.5
  • 27
    • 0033531617 scopus 로고    scopus 로고
    • Rapid and highly base selective RNA cleavage by a dinuclear Cu(II) complex
    • Liu S., Hamilton A.D. Rapid and highly base selective RNA cleavage by a dinuclear Cu(II) complex. J Chem Soc Chem Commun. 1999;587-588.
    • (1999) J Chem Soc Chem Commun , pp. 587-588
    • Liu, S.1    Hamilton, A.D.2
  • 28
    • 0030567366 scopus 로고    scopus 로고
    • Novel properties of cooperative dinuclear zinc(II) ions: The selective recognition of phosphomonoesters and their p-o ester bond cleavage by a new dinuclear zinc(II) cryptate
    • Koike T., Inoue M., Kimura E., Shiro M. Novel properties of cooperative dinuclear zinc(II) ions: the selective recognition of phosphomonoesters and their p-o ester bond cleavage by a new dinuclear zinc(II) cryptate. J Am Chem Soc. 118:1996;3091-3099.
    • (1996) J Am Chem Soc , vol.118 , pp. 3091-3099
    • Koike, T.1    Inoue, M.2    Kimura, E.3    Shiro, M.4
  • 29
    • 0000474926 scopus 로고    scopus 로고
    • A new bis(zinc(II)-cyclen) complex as a novel chelator for barbiturates and phosphates
    • Fujioka H., Koike T., Yamada N., Kimura E. A new bis(zinc(II)-cyclen) complex as a novel chelator for barbiturates and phosphates. Heterocycles. 42:1996;775-787.
    • (1996) Heterocycles , vol.42 , pp. 775-787
    • Fujioka, H.1    Koike, T.2    Yamada, N.3    Kimura, E.4
  • 30
    • 0030954582 scopus 로고    scopus 로고
    • II-1,4,7,10-tetraazacyclododecane) complex as a new receptor for phosphate dianions in aqueous solution
    • II-1,4,7,10-tetraazacyclododecane) complex as a new receptor for phosphate dianions in aqueous solution. J Am Chem Soc. 119:1997;3068-3076.
    • (1997) J Am Chem Soc , vol.119 , pp. 3068-3076
    • Kimura, E.1    Aoki, S.2    Koike, T.3    Shiro, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.