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Volumn 382, Issue 2, 2004, Pages 659-666

Active-site-mediated elimination of hydrogen fluoride from a fluorinated substrate analogue by isopenicillin N synthase

Author keywords

lactam antibiotic; Fluoride elimination; Lewis acid; Non haem iron oxidase; Penicillin biosynthesis

Indexed keywords

AMINO ACIDS; CATALYSIS; CRYSTALS; ENZYMES; IRON OXIDES;

EID: 4544226585     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20040529     Document Type: Article
Times cited : (24)

References (42)
  • 2
    • 0000502480 scopus 로고
    • Isopenicillin N synthase: Mechanistic studies
    • Baldwin, J. E. and Bradley, M. (1990) Isopenicillin N synthase: mechanistic studies Chem. Rev. 90, 1079-1088
    • (1990) Chem. Rev. , vol.90 , pp. 1079-1088
    • Baldwin, J.E.1    Bradley, M.2
  • 3
    • 0028168015 scopus 로고
    • Substrate specificity of L-δ-(α-aminoadipoyl)-L-cysteinyl-D- valine synthetase from Cephalosporium acremonium: Demonstration of the structure of several unnatural tripeptide products
    • Baldwin, J. E., Shiau, C.-Y., Byford, M. F. and Schofield, C. J. (1994) Substrate specificity of L-δ-(α-aminoadipoyl)-L-cysteinyl-D-valine synthetase from Cephalosporium acremonium: demonstration of the structure of several unnatural tripeptide products. Biochem. J. 301, 367-372
    • (1994) Biochem. J. , vol.301 , pp. 367-372
    • Baldwin, J.E.1    Shiau, C.-Y.2    Byford, M.F.3    Schofield, C.J.4
  • 9
    • 0022218689 scopus 로고
    • N-terminal amino acid sequence and some properties of isopenicillin-N synthetase from Cephalosporium acremonium
    • Baldwin, J. E., Gagnon, J. and Ting, H.-H. (1985) N-terminal amino acid sequence and some properties of isopenicillin-N synthetase from Cephalosporium acremonium. FEBS Letters 188, 253-256
    • (1985) FEBS Letters , vol.188 , pp. 253-256
    • Baldwin, J.E.1    Gagnon, J.2    Ting, H.-H.3
  • 10
    • 0025914883 scopus 로고
    • High-level soluble expression of isopenicillin N synthase isozymes in E coli
    • Baldwin, J. E., Blackburn, J. M., Sutherland, J. D. and Wright, M. C. (1991) High-level soluble expression of isopenicillin N synthase isozymes in E coli. Tetrahedron 47, 5991-6002
    • (1991) Tetrahedron , vol.47 , pp. 5991-6002
    • Baldwin, J.E.1    Blackburn, J.M.2    Sutherland, J.D.3    Wright, M.C.4
  • 11
    • 0028906347 scopus 로고
    • Crystallization and preliminary X-ray diffraction studies on recombinant isopenicillin N synthase from Aspergillus nidulans
    • Roach, P. L., Schofield, C. J., Baldwin, J. E., Clifton, I. J. and Hajdu, J. (1995) Crystallization and preliminary X-ray diffraction studies on recombinant isopenicillin N synthase from Aspergillus nidulans. Prot. Sci. 4, 1007-1009
    • (1995) Prot. Sci. , vol.4 , pp. 1007-1009
    • Roach, P.L.1    Schofield, C.J.2    Baldwin, J.E.3    Clifton, I.J.4    Hajdu, J.5
  • 14
    • 0038266917 scopus 로고    scopus 로고
    • Structural studies on the reaction of isopenicillin N synthase with the substrate analogue δ-(L-α-aminoadipoyl)-L-cysteinyl-D-α- aminobutyrate
    • Long, A. J., Clifton, I. J., Roach, P. L., Baldwin, J. E., Schofield, C. J. and Rutledge, P. J. (2003) Structural studies on the reaction of isopenicillin N synthase with the substrate analogue δ-(L-α- aminoadipoyl)-L-cysteinyl-D-α-aminobutyrate. Biochem. J. 372, 687-693
    • (2003) Biochem. J. , vol.372 , pp. 687-693
    • Long, A.J.1    Clifton, I.J.2    Roach, P.L.3    Baldwin, J.E.4    Schofield, C.J.5    Rutledge, P.J.6
  • 16
    • 0034602030 scopus 로고    scopus 로고
    • The high-valent compound of cytochrome P450: The nature of the Fe-S bond and the role of the thiolate ligand as an internal electron donor
    • Ogliaro, F., Cohen, S., Filatov, M., Harris, N. and Shaik, S. (2000) The high-valent compound of cytochrome P450: the nature of the Fe-S bond and the role of the thiolate ligand as an internal electron donor. Angew. Chem. Int. Ed. 39, 3851-3855
    • (2000) Angew. Chem. Int. Ed. , vol.39 , pp. 3851-3855
    • Ogliaro, F.1    Cohen, S.2    Filatov, M.3    Harris, N.4    Shaik, S.5
  • 17
    • 33751158901 scopus 로고
    • Preparation and reactivity of oxoiron(IV) porphyrins
    • Groves, J. T., Gross, Z. and Stern, M. K. (1994) Preparation and reactivity of oxoiron(IV) porphyrins. Inorg. Chem. 33, 5065-5072
    • (1994) Inorg. Chem. , vol.33 , pp. 5065-5072
    • Groves, J.T.1    Gross, Z.2    Stern, M.K.3
  • 18
    • 33845376272 scopus 로고
    • Structural characterization of horseradish peroxidase using EXAFS spectroscopy Evidence for Fe=O ligation in compounds I and II
    • Penner-Hahn, J. E., Eble, K. S., McMurry, T. J., Renner, M., Balch, A. L., Groves, J. T., Dawson, J. H. and Hodgson, K. O. (1986) Structural characterization of horseradish peroxidase using EXAFS spectroscopy Evidence for Fe=O ligation in compounds I and II. J. Am. Chem. Soc. 108, 7819-7825
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 7819-7825
    • Penner-Hahn, J.E.1    Eble, K.S.2    McMurry, T.J.3    Renner, M.4    Balch, A.L.5    Groves, J.T.6    Dawson, J.H.7    Hodgson, K.O.8
  • 21
    • 0035898074 scopus 로고    scopus 로고
    • Geometric and electronic structure contributions to function in bioinorganic chemistry: Active sites in non-heme iron enzymes
    • Solomon, E. I. (2000) Geometric and electronic structure contributions to function in bioinorganic chemistry: active sites in non-heme iron enzymes. Inorg. Chem. 40, 3656-3669
    • (2000) Inorg. Chem. , vol.40 , pp. 3656-3669
    • Solomon, E.I.1
  • 22
    • 0032039677 scopus 로고    scopus 로고
    • Oxygen activating nonheme iron enzymes
    • Lange, S. J. and Que, L. J. (1998) Oxygen activating nonheme iron enzymes. Curr. Opin. Chem. Biol. 2, 159-172
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 159-172
    • Lange, S.J.1    Que, L.J.2
  • 23
    • 0031574232 scopus 로고    scopus 로고
    • The 2-His-1-carboxylate facial triad. An emerging structural motif in mononuclear non-heme iron(II) enzymes
    • Hegg, E. L. and Que, L. J. (1997) The 2-His-1-carboxylate facial triad. An emerging structural motif in mononuclear non-heme iron(II) enzymes. Eur. J. Biochem. 250, 625-629
    • (1997) Eur. J. Biochem. , vol.250 , pp. 625-629
    • Hegg, E.L.1    Que, L.J.2
  • 24
    • 0142183453 scopus 로고    scopus 로고
    • Evidence for hydrogen abstraction from C1 of taurine by the high-spin Fe(IV) intermediate detected during oxygen activation by taurine:α- ketoglutarate dioxygenase (TauD)
    • Price, J. C., Barr, E. W., Glass, T. E., Krebs, C. and Bollinger, Jr, J. M. (2003) Evidence for hydrogen abstraction from C1 of taurine by the high-spin Fe(IV) intermediate detected during oxygen activation by taurine:α- ketoglutarate dioxygenase (TauD). J. Am. Chem. Soc. 125, 13008-13009
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13008-13009
    • Price, J.C.1    Barr, E.W.2    Glass, T.E.3    Krebs, C.4    Bollinger Jr., J.M.5
  • 25
    • 0038747011 scopus 로고    scopus 로고
    • The first direct characterization of a high-valent iron intermediate in the reaction of an α-ketoglutarate-dependent dioxygenase: A high-spin Fe(IV) complex in taurine/α-ketoglutarate dioxygenase (TauD) from Escherichia coli
    • Price, J. C., Barr, E. W., Tirupati, B., Bollinger, Jr, J. M. and Krebs, C. (2003) The first direct characterization of a high-valent iron intermediate in the reaction of an α-ketoglutarate-dependent dioxygenase: a high-spin Fe(IV) complex in taurine/α-ketoglutarate dioxygenase (TauD) from Escherichia coli. Biochemistry 42, 7497-7508
    • (2003) Biochemistry , vol.42 , pp. 7497-7508
    • Price, J.C.1    Barr, E.W.2    Tirupati, B.3    Bollinger Jr., J.M.A.4    Krebs, C.5
  • 26
    • 0003661703 scopus 로고
    • Modern methods for the introduction of fluorine into organic molecules: An approach to compounds with altered chemical and biological activities
    • Mann, J. (1987) Modern methods for the introduction of fluorine into organic molecules: an approach to compounds with altered chemical and biological activities. Chem. Soc. Rev. 16, 381-436
    • (1987) Chem. Soc. Rev. , vol.16 , pp. 381-436
    • Mann, J.1
  • 27
    • 0037862197 scopus 로고
    • Bond dissociation energies by kinetic methods
    • Kerr, J. A. (1966) Bond dissociation energies by kinetic methods. Chem. Rev. 66, 465-500
    • (1966) Chem. Rev. , vol.66 , pp. 465-500
    • Kerr, J.A.1
  • 28
    • 33947092377 scopus 로고
    • Very low pressure reactor. A new technique for measuring rates and equilibria of radical-molecule reactions at low temperature. Heat of formation of the methyl radical
    • Baghal-Vayjooee, M. H., Colussi, A. J. and Benson, S. W. (1978) Very low pressure reactor. A new technique for measuring rates and equilibria of radical-molecule reactions at low temperature. Heat of formation of the methyl radical. J. Am. Chem. Soc. 100, 3214-3215
    • (1978) J. Am. Chem. Soc. , vol.100 , pp. 3214-3215
    • Baghal-Vayjooee, M.H.1    Colussi, A.J.2    Benson, S.W.3
  • 29
    • 4544258575 scopus 로고
    • DPhil thesis, Dyson Perrins Laboratory, University of Oxford, Oxford, U.K.
    • Moroney, S. E. (1985) DPhil thesis, Dyson Perrins Laboratory, University of Oxford, Oxford, U.K.
    • (1985)
    • Moroney, S.E.1
  • 30
    • 0033212815 scopus 로고    scopus 로고
    • Integration of macromolecular diffraction data
    • Leslie, A. G. W. (1999) Integration of macromolecular diffraction data. Acta Cryst. D 55, 1696-1702
    • (1999) Acta Cryst. D , vol.55 , pp. 1696-1702
    • Leslie, A.G.W.1
  • 31
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Cryst. D 50, 760-763
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 32
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W. and Kjelgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A 47, 110-119
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjelgaard, M.4
  • 33
    • 85077759504 scopus 로고
    • Asymmetric synthesis via heterocyclic intermediates; XIX. On the enantioselective synthesis of β-fluorovaline methyl ester and related α-amino-β-fluorocarboxylic esters
    • Groth, U. and Schöllkopf, U. (1983) Asymmetric synthesis via heterocyclic intermediates; XIX. On the enantioselective synthesis of β-fluorovaline methyl ester and related α-amino-β- fluorocarboxylic esters. Synthesis, 673-675
    • (1983) Synthesis , pp. 673-675
    • Groth, U.1    Schöllkopf, U.2
  • 34
    • 84985516415 scopus 로고
    • Enantioselective synthesis of (R)-amino acids using L-valine as chiral agent
    • Schöllkopf, U., Groth, U. and Deng, C. (1981) Enantioselective synthesis of (R)-amino acids using L-valine as chiral agent. Angew. Chem. Int. Ed. 20, 798-799
    • (1981) Angew. Chem. Int. Ed. , vol.20 , pp. 798-799
    • Schöllkopf, U.1    Groth, U.2    Deng, C.3
  • 35
    • 0012476236 scopus 로고
    • Asymmetric syntheses via heterocyclic intermediates; XV. Enantioselective synthesis of (R)-(-)-β-hydroxyvaline using L-valine or (S)-O,O-dimethyl-α-methyldopa as chiral auxiliary reagents
    • Schöllkopf, U., Nozulak, J. and Groth, U. (1982) Asymmetric syntheses via heterocyclic intermediates; XV. Enantioselective synthesis of (R)-(-)-β-hydroxyvaline using L-valine or (S)-O,O-dimethyl-α- methyldopa as chiral auxiliary reagents. Synthesis, 868-870
    • (1982) Synthesis , pp. 868-870
    • Schöllkopf, U.1    Nozulak, J.2    Groth, U.3
  • 36
    • 4244038183 scopus 로고
    • Asymmetrische synthesen über heterocyclische zwischenstufen, XVIII. Zur enantioselektiven synthese von (2R)-Serin-methylestern oder (2R)-serinen ausgehend vom bislactimether von cyclo-(L-Val-Gly-)
    • Schöllkopf, U., Groth, U., Gull, M.-R. and Nozulak, J. (1983) Asymmetrische synthesen über heterocyclische zwischenstufen, XVIII. Zur enantioselektiven synthese von (2R)-Serin-methylestern oder (2R)-serinen ausgehend vom bislactimether von cyclo-(L-Val-Gly-). Liebigs Ann, Chem., 1133-1151
    • (1983) Liebigs Ann, Chem. , pp. 1133-1151
    • Schöllkopf, U.1    Groth, U.2    Gull, M.-R.3    Nozulak, J.4
  • 37
    • 33847800447 scopus 로고
    • New fluoridating reagents. Dialkylamino sulphur fluorides
    • Middleton, W. J. (1975) New fluoridating reagents. Dialkylamino sulphur fluorides. J. Org. Chem. 40, 574-578
    • (1975) J. Org. Chem. , vol.40 , pp. 574-578
    • Middleton, W.J.1
  • 39
    • 0000841649 scopus 로고
    • A rapid synthesis of oligopeptide derivatives without isolation of intermediates
    • Sheehan, J. C., Preston, J. and Cruickshank, P. A. (1965) A rapid synthesis of oligopeptide derivatives without isolation of intermediates. J. Am. Chem. Soc. 87, 2492-2493
    • (1965) J. Am. Chem. Soc. , vol.87 , pp. 2492-2493
    • Sheehan, J.C.1    Preston, J.2    Cruickshank, P.A.3
  • 42
    • 0032575228 scopus 로고    scopus 로고
    • Synthesis of δ-(L-α-aminoadipoyl)-L-cysteinyl-D-(O-methyl)-o- allothreonine a substrate for isopenicillin-N synthase and its O-methyl-D-threonine epimer
    • Petursson, S. and Baldwin, J. E. (1998) Synthesis of δ-(L-α- aminoadipoyl)-L-cysteinyl-D-(O-methyl)-o-allothreonine a substrate for isopenicillin-N synthase and its O-methyl-D-threonine epimer. Tetrahedron 54, 6001-6010
    • (1998) Tetrahedron , vol.54 , pp. 6001-6010
    • Petursson, S.1    Baldwin, J.E.2


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