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Volumn 287, Issue 5, 1999, Pages 943-960

Studies on the active site of deacetoxycephalosporin C synthase

Author keywords

2 Oxoglutarate; Antibiotic biosynthesis; Dioxygenase; EXAFS; Iron

Indexed keywords

DEACETOXYCEPHALOSPORIN C; PENICILLIN DERIVATIVE; SYNTHETASE;

EID: 0033574483     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2594     Document Type: Article
Times cited : (106)

References (51)
  • 1
    • 0023996141 scopus 로고
    • The biosynthesis of penicillins and cephalosporins
    • Baldwin J. E., Abraham E. P. The biosynthesis of penicillins and cephalosporins. Nature Prod. Rep. 5:1988;129-145.
    • (1988) Nature Prod. Rep. , vol.5 , pp. 129-145
    • Baldwin, J.E.1    Abraham, E.P.2
  • 2
    • 0000502480 scopus 로고
    • Isopenicillin N synthase: Mechanistic studies
    • Baldwin J. E., Bradley M. Isopenicillin N synthase: mechanistic studies. Chem. Rev. 90:1990;1079-1088.
    • (1990) Chem. Rev. , vol.90 , pp. 1079-1088
    • Baldwin, J.E.1    Bradley, M.2
  • 3
    • 0001769353 scopus 로고
    • The biosynthesis of β-lactams
    • M. I. Page. London: Blackie Academic and Professional
    • Baldwin J. E., Schofield C. J. The biosynthesis of β-lactams. Page M. I. The Chemistry of β-lactams. 1992;1-78 Blackie Academic and Professional, London.
    • (1992) The Chemistry of β-Lactams , pp. 1-78
    • Baldwin, J.E.1    Schofield, C.J.2
  • 5
    • 37049075408 scopus 로고
    • Stepwise hydrogen removal in the enzymic ring expansion of penicillin N to deacetoxycephalosporin C
    • Baldwin J. E., Adlington R. M., Crouch, Schofield C. J., Ting H-H. Stepwise hydrogen removal in the enzymic ring expansion of penicillin N to deacetoxycephalosporin C. J. Chem. Soc. Chem. Commun. 1987a;1654-1656.
    • (1987) J. Chem. Soc. Chem. Commun. , pp. 1654-1656
    • Baldwin, J.E.1    Adlington, R.M.2    Crouch3    Schofield, C.J.4    Ting, H.-H.5
  • 7
    • 0023677432 scopus 로고
    • The ring expansion of penicillins to cephams: A possible biomimetic process
    • Baldwin J. E., Adlington R. M., Kang T. W., Lee E., Schofield C. J. The ring expansion of penicillins to cephams: a possible biomimetic process. Tetrahedron. 44:1988;5953-5957.
    • (1988) Tetrahedron , vol.44 , pp. 5953-5957
    • Baldwin, J.E.1    Adlington, R.M.2    Kang, T.W.3    Lee, E.4    Schofield, C.J.5
  • 8
    • 0025232672 scopus 로고
    • Side-chain specificity in the enzymatic synthesis of penicillins
    • Baldwin J. E., Schofield C. J., Smith B. D. Side-chain specificity in the enzymatic synthesis of penicillins. Tetrahedron. 46:1990;3019-3028.
    • (1990) Tetrahedron , vol.46 , pp. 3019-3028
    • Baldwin, J.E.1    Schofield, C.J.2    Smith, B.D.3
  • 12
    • 0026620970 scopus 로고
    • Constrained and restrained refinement in EXAFS data analysis with curved wave theory
    • Binsted N., Strange R. W., Hasnain S. S. Constrained and restrained refinement in EXAFS data analysis with curved wave theory. Biochemistry. 1992;12117-12125.
    • (1992) Biochemistry , pp. 12117-12125
    • Binsted, N.1    Strange, R.W.2    Hasnain, S.S.3
  • 13
    • 0030032150 scopus 로고    scopus 로고
    • Ferrous active site of isopenicillin N synthase: Genetic and sequence analysis of the endogenous ligands
    • Borovok I., Landman O., Kreisberg-Zakarin R., Aharonowitz Y., Cohen G. Ferrous active site of isopenicillin N synthase: genetic and sequence analysis of the endogenous ligands. Biochemistry. 35:1996;1981-1987.
    • (1996) Biochemistry , vol.35 , pp. 1981-1987
    • Borovok, I.1    Landman, O.2    Kreisberg-Zakarin, R.3    Aharonowitz, Y.4    Cohen, G.5
  • 14
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 17
    • 0027631543 scopus 로고
    • The enzymes involved in the biosynthesis of penicillins and cephalosporins. Their structure and function
    • Cooper R. D. G. The enzymes involved in the biosynthesis of penicillins and cephalosporins. Their structure and function. Bioorg. Med. Chem. 1:1993;1-17.
    • (1993) Bioorg. Med. Chem. , vol.1 , pp. 1-17
    • Cooper, R.D.G.1
  • 18
    • 0028835709 scopus 로고
    • Production of cephalosporin intermediates by feeding adipic acid to recombinant Penicillium chrysogenum strains expressing ring expansion activity
    • Crawford L., Stepan A. M., McAda P. C., Rambosek J. A., Condor M. J., Vinci V. A., Reeves C. J. Production of cephalosporin intermediates by feeding adipic acid to recombinant Penicillium chrysogenum strains expressing ring expansion activity. Bio/Technol. 13:1995;58-62.
    • (1995) Bio/Technol. , vol.13 , pp. 58-62
    • Crawford, L.1    Stepan, A.M.2    McAda, P.C.3    Rambosek, J.A.4    Condor, M.J.5    Vinci, V.A.6    Reeves, C.J.7
  • 19
    • 0024380165 scopus 로고
    • Purification and properties of deacetoxycephalosporin C synthase from recombinant Escherichia coli and its comparison with the native enzyme purified from Streptomyces clavuligerus
    • Dotzlaf J. E., Yeh W.-K. Purification and properties of deacetoxycephalosporin C synthase from recombinant Escherichia coli and its comparison with the native enzyme purified from Streptomyces clavuligerus. J. Biol. Chem. 264:1989;10219-10227.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10219-10227
    • Dotzlaf, J.E.1    Yeh, W.-K.2
  • 20
    • 35548993600 scopus 로고
    • A rapid, exact, curved wave theory for EXAFS calculations
    • Gurman S. L., Binsted N., Ross I. A rapid, exact, curved wave theory for EXAFS calculations. J. Phys. C: Sol. St. Phys. 17:1984;143-151.
    • (1984) J. Phys. C: Sol. St. Phys. , vol.17 , pp. 143-151
    • Gurman, S.L.1    Binsted, N.2    Ross, I.3
  • 21
    • 33744602646 scopus 로고
    • A rapid, exact, curved wave theory for EXAFS calculations II. The multiple scattering contributions
    • Gurman S. J., Binsted N., Ross I. A rapid, exact, curved wave theory for EXAFS calculations II. The multiple scattering contributions. J. Phys. C: Sol. St. Phys. 19:1986;1845-1861.
    • (1986) J. Phys. C: Sol. St. Phys. , vol.19 , pp. 1845-1861
    • Gurman, S.J.1    Binsted, N.2    Ross, I.3
  • 22
    • 77957001732 scopus 로고
    • Reaction of protein sulfhydryl groups with Ellman's reagent
    • C. H. W. Hirs, & S. N. Timersheff. London: Academic Press
    • Habeeb A. F. S. A. Reaction of protein sulfhydryl groups with Ellman's reagent. Hirs C. H. W., Timersheff S. N. Methods in Enzymol. 1974;457-464 Academic Press, London.
    • (1974) Methods in Enzymol , pp. 457-464
    • Habeeb, A.F.S.A.1
  • 23
    • 22144469121 scopus 로고
    • Effects of electron-electron and electron-phonon interactions on the one-electron states of solids
    • Hedin L., Lundqvist S. Effects of electron-electron and electron-phonon interactions on the one-electron states of solids. Solid State Phys. 23:1969;1-181.
    • (1969) Solid State Phys. , vol.23 , pp. 1-181
    • Hedin, L.1    Lundqvist, S.2
  • 24
    • 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., Que L. The 2-His-1-carboxylate facial triad. An emerging structural motif in mononuclear non-heme iron(II) enzymes. Eur. J. Biochem. 250:1997;625-629.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 625-629
    • Hegg, E.L.1    Que, L.2
  • 25
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiple anomalous diffraction (MAD): A vehicle for direct determination of three dimensional structure
    • Hendrickson W. A., Horton J. R., LeMaster D. M. Selenomethionyl proteins produced for analysis by multiple anomalous diffraction (MAD): a vehicle for direct determination of three dimensional structure. EMBO J. 9:1990;1665-1672.
    • (1990) EMBO J. , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    Lemaster, D.M.3
  • 26
    • 0016751962 scopus 로고
    • A kinetic study of thymine hydroxylase from Neurospora crassa
    • Holme E. A kinetic study of thymine hydroxylase from Neurospora crassa. Biochemistry. 14:1975;4999-5003.
    • (1975) Biochemistry , vol.14 , pp. 4999-5003
    • Holme, E.1
  • 27
    • 0024535307 scopus 로고
    • Cloning, characterisation and expression in Escherichia coli of the Streptomyces clavuligerus gene encoding deacetoxycephalosporin C synthase
    • Kovacevic S., Weigal B. J., Tobin M. B., Ingolia T., Miller J. R. Cloning, characterisation and expression in Escherichia coli of the Streptomyces clavuligerus gene encoding deacetoxycephalosporin C synthase. J. Bacteriol. 171:1989;754-760.
    • (1989) J. Bacteriol. , vol.171 , pp. 754-760
    • Kovacevic, S.1    Weigal, B.J.2    Tobin, M.B.3    Ingolia, T.4    Miller, J.R.5
  • 28
    • 0000059497 scopus 로고
    • Theory of the extended X-ray absorption fine structure
    • Lee P. A., Pendry J. B. Theory of the extended X-ray absorption fine structure. Phys. Rev. B11:1975;2795-2811.
    • (1975) Phys. Rev. , vol.11 , pp. 2795-2811
    • Lee, P.A.1    Pendry, J.B.2
  • 30
    • 0030262724 scopus 로고    scopus 로고
    • Fast staining and destaining of sodium dodecyl sulphate polyacrylamide gels
    • and references therein
    • Lloyd M. D. Fast staining and destaining of sodium dodecyl sulphate polyacrylamide gels. Anal. Biochem. 241:1996;139-140 and references therein.
    • (1996) Anal. Biochem. , vol.241 , pp. 139-140
    • Lloyd, M.D.1
  • 31
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B. W. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 34
    • 0001265131 scopus 로고
    • Chemistry of cephalosporin antibiotics. III. Chemical correlation of penicillins & cephalosporin antibiotics
    • Morin R. B., Jackson B. G., Mueller R. A., Lavagnino E. R., Scanlon W. B., Andrews S. L. Chemistry of cephalosporin antibiotics. III. Chemical correlation of penicillins & cephalosporin antibiotics. J. Am. Chem. Soc. 85:1963;1896-1897.
    • (1963) J. Am. Chem. Soc. , vol.85 , pp. 1896-1897
    • Morin, R.B.1    Jackson, B.G.2    Mueller, R.A.3    Lavagnino, E.R.4    Scanlon, W.B.5    Andrews, S.L.6
  • 35
    • 0030962028 scopus 로고    scopus 로고
    • Characterization of the iron- And 2-oxoglutarate-binding sites of prolyl 4-hydroxylase
    • Myllyharju J., Kivirikko K. I. Characterization of the iron- and 2-oxoglutarate-binding sites of prolyl 4-hydroxylase. EMBO J. 16:1997;1173-1180.
    • (1997) EMBO J. , vol.16 , pp. 1173-1180
    • Myllyharju, J.1    Kivirikko, K.I.2
  • 36
  • 37
    • 0030271746 scopus 로고    scopus 로고
    • Incorporating anomalous scattering centres into macromolecules
    • Pappa H. S., Steward A. E., McDonald N. Q. Incorporating anomalous scattering centres into macromolecules. Curr. Opin Struct. Biol. 6:1996;611-616.
    • (1996) Curr. Opin Struct. Biol. , vol.6 , pp. 611-616
    • Pappa, H.S.1    Steward, A.E.2    McDonald, N.Q.3
  • 38
    • 0032481388 scopus 로고    scopus 로고
    • Circular dichroism and magnetic circular dichroism spectroscopic studies of the non-heme ferrous active site in clavaminate synthase and its interaction with α-ketoglutarate cosubstrate
    • Pavel E. G., Zhou L., Busby R. W., Gunsior M., Townsend C. A., Solomon E. I. Circular dichroism and magnetic circular dichroism spectroscopic studies of the non-heme ferrous active site in clavaminate synthase and its interaction with α-ketoglutarate cosubstrate. J. Am. Chem. Soc. 120:1998;743-753.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 743-753
    • Pavel, E.G.1    Zhou, L.2    Busby, R.W.3    Gunsior, M.4    Townsend, C.A.5    Solomon, E.I.6
  • 39
    • 0000658037 scopus 로고
    • A dilemma of dioxygenases (or where biochemistry and molecular biology fail to meet)
    • Prescott A. G. A dilemma of dioxygenases (or where biochemistry and molecular biology fail to meet). J. Exp. Bot. 44:1993;849-861.
    • (1993) J. Exp. Bot. , vol.44 , pp. 849-861
    • Prescott, A.G.1
  • 40
    • 0039302669 scopus 로고    scopus 로고
    • Dioxygen activation by enzymes with mononuclear non-heme iron active sites
    • Que L., Ho R. Y. N. Dioxygen activation by enzymes with mononuclear non-heme iron active sites. Chem. Rev. 96:1996;2607-2624.
    • (1996) Chem. Rev. , vol.96 , pp. 2607-2624
    • Que, L.1    Ho, R.Y.N.2
  • 43
    • 0030947388 scopus 로고    scopus 로고
    • Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation
    • Roach P. L., Clifton L., Hensgens C. M. H., Shibata N., Schofield C. J., Hajdu J., Baldwin J. E. Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation. Nature. 387:1997;827-830.
    • (1997) Nature , vol.387 , pp. 827-830
    • Roach, P.L.1    Clifton, L.2    Hensgens, C.M.H.3    Shibata, N.4    Schofield, C.J.5    Hajdu, J.6    Baldwin, J.E.7
  • 45
    • 0031004173 scopus 로고    scopus 로고
    • Glutamine-330 is not essential for activity in isopenicillin N synthase from Aspergillus nidulans
    • Sami M., Brown T. J. N., Roach P. L., Schofield C. J., Baldwin J. E. Glutamine-330 is not essential for activity in isopenicillin N synthase from Aspergillus nidulans. FEBS Letters. 405:1997;191-194.
    • (1997) FEBS Letters , vol.405 , pp. 191-194
    • Sami, M.1    Brown, T.J.N.2    Roach, P.L.3    Schofield, C.J.4    Baldwin, J.E.5
  • 47
    • 0030576318 scopus 로고    scopus 로고
    • Adipoyl-6-aminopenicillanic acid is a substrate for deacetoxycephalosporin C synthase (DAOCS)
    • and references therein
    • Shibata N., Lloyd M. D., Baldwin J. E., Schofield C. J. Adipoyl-6-aminopenicillanic acid is a substrate for deacetoxycephalosporin C synthase (DAOCS). Bioorg. Med. Chem. Letters. 6:1996;1579-1584 and references therein.
    • (1996) Bioorg. Med. Chem. Letters , vol.6 , pp. 1579-1584
    • Shibata, N.1    Lloyd, M.D.2    Baldwin, J.E.3    Schofield, C.J.4
  • 48
    • 0022382829 scopus 로고
    • Stereochemical fate of chiral-methyl valine in the ring expansion of penicillin N to deacetoxycephalosporin C
    • Townsend C. A., Theis A. B., Neese A. S., Barrabee E. B., Poland D. Stereochemical fate of chiral-methyl valine in the ring expansion of penicillin N to deacetoxycephalosporin C. J. Am. Chem. Soc. 107:1985;4760-4767.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 4760-4767
    • Townsend, C.A.1    Theis, A.B.2    Neese, A.S.3    Barrabee, E.B.4    Poland, D.5
  • 50
    • 0030983568 scopus 로고    scopus 로고
    • Metal co-ordination environment of a Cu(II)-substituted α-keto acid-dependent dioxygenase that degrades the herbicide 2,4-D
    • Whiting A. K., Que L., Saari R. E., Hausinger R. P., Fredrich M. A., McCracken J. Metal co-ordination environment of a Cu(II)-substituted α-keto acid-dependent dioxygenase that degrades the herbicide 2,4-D. J. Am. Chem. Soc. 119:1997;3413-3414.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 3413-3414
    • Whiting, A.K.1    Que, L.2    Saari, R.E.3    Hausinger, R.P.4    Fredrich, M.A.5    McCracken, J.6
  • 51
    • 0031455762 scopus 로고    scopus 로고
    • Metal-catalysed oxidation and mutagenesis studies on the iron(II) binding site of 1-aminocyclopropane-1-carboxylate oxidase
    • Zhang Z.-E., Barlow J. N., Baldwin J. E., Schofield C. J. Metal-catalysed oxidation and mutagenesis studies on the iron(II) binding site of 1-aminocyclopropane-1-carboxylate oxidase. Biochemistry. 36:1997;15999-16007.
    • (1997) Biochemistry , vol.36 , pp. 15999-16007
    • Zhang, Z.-E.1    Barlow, J.N.2    Baldwin, J.E.3    Schofield, C.J.4


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