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Volumn 11, Issue 1, 2004, Pages 95-101

The structural basis of cephalosporin formation in a mononuclear ferrous enzyme

Author keywords

[No Author keywords available]

Indexed keywords

2 OXOGLUTARIC ACID; AMPICILLIN; CARBON; CARBON DIOXIDE; CEPHALOSPORIN; DEACETOXYCEPHALOSPORIN C; DEACETOXYCEPHALOSPORIN C SYNTHASE; FERROUS ION; IRON; OXYGEN; PENICILLIN G; SUCCINIC ACID; SYNTHETASE; UNCLASSIFIED DRUG;

EID: 0842313011     PISSN: 15459993     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsmb712     Document Type: Article
Times cited : (79)

References (45)
  • 1
    • 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, 849-861 (1993).
    • (1993) J. Exp. Bot. , vol.44 , pp. 849-861
    • Prescott, A.G.1
  • 2
    • 0032552110 scopus 로고    scopus 로고
    • Structure of a cephalosporin synthase
    • Valegård, K. et al. Structure of a cephalosporin synthase. Nature 394, 805-809 (1998).
    • (1998) Nature , vol.394 , pp. 805-809
    • Valegård, K.1
  • 3
    • 0023996141 scopus 로고
    • The biosynthesis of penicillins and cephalosporins
    • Baldwin, J.E. & Abraham, E. The biosynthesis of penicillins and cephalosporins. Nat. Prod. Rep. 5, 129-145 (1988).
    • (1988) Nat. Prod. Rep. , vol.5 , pp. 129-145
    • Baldwin, J.E.1    Abraham, E.2
  • 4
    • 0033981009 scopus 로고    scopus 로고
    • Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase
    • Zhang, Z. et al. Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase. Nat. Struct. Biol. 7, 127-133 (2000).
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 127-133
    • Zhang, Z.1
  • 5
    • 0036151286 scopus 로고    scopus 로고
    • Structure and mechanism of anthocyanidin synthase from Arabidopsis thaliana
    • Wilmouth, R. et al. Structure and mechanism of anthocyanidin synthase from Arabidopsis thaliana. Structure 10, 93-103 (2002).
    • (2002) Structure , vol.10 , pp. 93-103
    • Wilmouth, R.1
  • 6
    • 0037161271 scopus 로고    scopus 로고
    • X-ray crystal structure of Escherichia coli taurine/α -ketoglutarate dioxygenase complexed to ferrous iron and substrates
    • Elkins, J.M. et al. X-ray crystal structure of Escherichia coli taurine/α-ketoglutarate dioxygenase complexed to ferrous iron and substrates. Biochemistry 41, 5185-5192 (2002).
    • (2002) Biochemistry , vol.41 , pp. 5185-5192
    • Elkins, J.M.1
  • 7
    • 0035663669 scopus 로고    scopus 로고
    • Structure of proline 3-hydrolase. Evolution of the family of 2-oxoglutarate dependent oxygenases
    • Clifton, I.J., Hsueh, L.C., Baldwin, J.E., Harlos, K. & Schofield, C.J. Structure of proline 3-hydrolase. Evolution of the family of 2-oxoglutarate dependent oxygenases. Eur. J. Biochem. 268, 6625-6636 (2001).
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6625-6636
    • Clifton, I.J.1    Hsueh, L.C.2    Baldwin, J.E.3    Harlos, K.4    Schofield, C.J.5
  • 8
    • 0037180452 scopus 로고    scopus 로고
    • Structure of a factor-inhibiting hypoxia-inducible factor 1: An asparaginyl hydroxylase involved in the hypoxic response pathway
    • Dann, C.E., III, Bruick, R.K. & Deisenhofer, J. Structure of a factor-inhibiting hypoxia-inducible factor 1: an asparaginyl hydroxylase involved in the hypoxic response pathway. Proc. Natl. Acad. Sci. USA 99, 15351-15356 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 15351-15356
    • Dann III, C.E.1    Bruick, R.K.2    Deisenhofer, J.3
  • 9
    • 0037449811 scopus 로고    scopus 로고
    • Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1α
    • Elkins et al. Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1α. J. Biol. Chem. 278, 1802-1806 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 1802-1806
    • Elkins1
  • 10
    • 0037470162 scopus 로고    scopus 로고
    • Structure of human FIH-1 reveals a unique active site pocket and interaction sites for HIF-1 and von Hippel-Lindau
    • Lee, C., Kim, S.J., Jeong, D.G., Lee, S.M. & Ryu, S.E. Structure of human FIH-1 reveals a unique active site pocket and interaction sites for HIF-1 and von Hippel-Lindau. J. Biol. Chem. 278, 7558-7563.
    • J. Biol. Chem. , vol.278 , pp. 7558-7563
    • Lee, C.1    Kim, S.J.2    Jeong, D.G.3    Lee, S.M.4    Ryu, S.E.5
  • 11
    • 0029038392 scopus 로고
    • Crystal structure of isopenicillin N synthase, first of a new structural family of enzymes
    • Roach, P.L. et al. Crystal structure of isopenicillin N synthase, first of a new structural family of enzymes. Nature 375, 700-704 (1995).
    • (1995) Nature , vol.375 , pp. 700-704
    • Roach, P.L.1
  • 12
    • 0031574232 scopus 로고    scopus 로고
    • The 2-His-carboxylate facial triad. An emerging structural motif in mononuclear non-heme iron(II) enzymes
    • Hegg, E.L. & Que, L. Jr. The 2-His-carboxylate facial triad. An emerging structural motif in mononuclear non-heme iron(II) enzymes. Eur. J. Biochem. 250, 625-629 (1997).
    • (1997) Eur. J. Biochem. , vol.250 , pp. 625-629
    • Hegg, E.L.1    Que Jr., L.2
  • 13
    • 0030903149 scopus 로고    scopus 로고
    • Inactivation of 1-aminocyclopropane-1-carboxylate oxidase involves oxidative modifications
    • Barlow, J.N., Zhang, Z.H., John, P., Baldwin, J.E. & Schofield, C.J. Inactivation of 1-aminocyclopropane-1-carboxylate oxidase involves oxidative modifications. Biochemistry 36, 3563-3569 (1997).
    • (1997) Biochemistry , vol.36 , pp. 3563-3569
    • Barlow, J.N.1    Zhang, Z.H.2    John, P.3    Baldwin, J.E.4    Schofield, C.J.5
  • 14
    • 0034802889 scopus 로고    scopus 로고
    • Alternative reactivity of an α-ketoglutarate-dependent iron(II) oxygenase: Enzyme self-hydroxylation
    • Liu, A., Ho, R.Y.N. & Que, L. Jr. Alternative reactivity of an α-ketoglutarate-dependent iron(II) oxygenase: enzyme self-hydroxylation. J. Am. Chem. Soc. 123, 5126-5127 (2001).
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5126-5127
    • Liu, A.1    Ho, R.Y.N.2    Que Jr., L.3
  • 15
    • 0037465344 scopus 로고    scopus 로고
    • 2- and α-ketoglutarate-dependent tyrosyl radical formation in TauD, an α-keto acid-dependent non-heme iron dioxygenase
    • 2- and α-ketoglutarate-dependent tyrosyl radical formation in TauD, an α-keto acid-dependent non-heme iron dioxygenase. Biochemistry 42, 1854-1862 (2003).
    • (2003) Biochemistry , vol.42 , pp. 1854-1862
    • Ryle, M.J.1
  • 17
    • 0023697439 scopus 로고
    • Substrate specificity of cloned deacetoxycephalosporin C/deacetylcephalosporin C synthetase
    • Baldwin, J.E. et al. Substrate specificity of cloned deacetoxycephalosporin C/deacetylcephalosporin C synthetase. J. Antibiot. 41, 1694-1695 (1988).
    • (1988) J. Antibiot. , vol.41 , pp. 1694-1695
    • Baldwin, J.E.1
  • 18
    • 0034968454 scopus 로고    scopus 로고
    • Probing the penicillin sidechain selectivity of recombinant deacetoxycephalosporin C synthase
    • Dubus, A. et al. Probing the penicillin sidechain selectivity of recombinant deacetoxycephalosporin C synthase. Cell. Mol. Life Sci. 58, 835-843 (2001).
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 835-843
    • Dubus, A.1
  • 19
    • 0037165643 scopus 로고    scopus 로고
    • Crystal structure of a clavaminate synthase-Fe(II)-2-oxoglutarate-substrate-NO complex: Evidence for metal centred rearrangements
    • Zhang, Z. et al. Crystal structure of a clavaminate synthase-Fe(II)-2-oxoglutarate-substrate-NO complex: evidence for metal centred rearrangements. FEBS Lett. 517, 7-12 (2002).
    • (2002) FEBS Lett. , vol.517 , pp. 7-12
    • Zhang, Z.1
  • 20
    • 0033554721 scopus 로고    scopus 로고
    • The reaction cycle of isopenicillin N synthase observed by X-ray diffraction
    • Burzlaff, N.I. et al. The reaction cycle of isopenicillin N synthase observed by X-ray diffraction. Nature 401, 721-724 (1999).
    • (1999) Nature , vol.401 , pp. 721-724
    • Burzlaff, N.I.1
  • 21
    • 0038290551 scopus 로고    scopus 로고
    • Substrate-induced conformational changes in Escherichia coli taurine/α-ketoglutarate dioxygenase and insight into the oligomeric structure
    • O'Brien, J.R., Schuller, D.J., Yang, V.S., Dillard, B.D. & Lanzilotta, W.N. Substrate-induced conformational changes in Escherichia coli taurine/α-ketoglutarate dioxygenase and insight into the oligomeric structure. Biochemistry 42, 5547-5554 (2003).
    • (2003) Biochemistry , vol.42 , pp. 5547-5554
    • O'Brien, J.R.1    Schuller, D.J.2    Yang, V.S.3    Dillard, B.D.4    Lanzilotta, W.N.5
  • 22
    • 0000208617 scopus 로고    scopus 로고
    • Geometric and electronic structure/function correlations in non-heme iron enzymes
    • Solomon, E.I. et al. Geometric and electronic structure/function correlations in non-heme iron enzymes. Chem. Rev. 100, 235-349 (2000).
    • (2000) Chem. Rev. , vol.100 , pp. 235-349
    • Solomon, E.I.1
  • 23
    • 0034828607 scopus 로고    scopus 로고
    • Spectroscopic studies of substrate interactions with clavaminate synthase 2, a multifunctional α-KG-dependent non-heme iron enzyme: Correlation with mechanisms and reactivities
    • Zhou, J. et al. Spectroscopic studies of substrate interactions with clavaminate synthase 2, a multifunctional α-KG-dependent non-heme iron enzyme: correlation with mechanisms and reactivities. J. Am. Chem. Soc. 123, 7388-7398 (2001).
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 7388-7398
    • Zhou, J.1
  • 24
    • 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, J.M. Jr. & Krebs, C. 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).
    • (2003) Biochemistry , vol.42 , pp. 7497-7508
    • Price, J.C.1    Barr, E.W.2    Tirupati, B.3    Bollinger Jr., J.M.4    Krebs, C.5
  • 25
    • 0036294889 scopus 로고    scopus 로고
    • Active site mutations of recombinant deacetoxycephalosporin C synthase
    • Lee, H.J., Schofield, C.J. & Lloyd, M.D. Active site mutations of recombinant deacetoxycephalosporin C synthase. Biochem. Biophys. Res. Commun. 292, 66-70 (2002).
    • (2002) Biochem. Biophys. Res. Commun. , vol.292 , pp. 66-70
    • Lee, H.J.1    Schofield, C.J.2    Lloyd, M.D.3
  • 26
    • 0035906733 scopus 로고    scopus 로고
    • Kinetic and crystallographic studies on deacetoxycephalosporin C synthase (DAOCS)
    • Lee, H.-J. et al. Kinetic and crystallographic studies on deacetoxycephalosporin C synthase (DAOCS). J. Mol. Biol. 308, 937-948 (2001).
    • (2001) J. Mol. Biol. , vol.308 , pp. 937-948
    • Lee, H.-J.1
  • 27
    • 0033854668 scopus 로고    scopus 로고
    • The iron(II) and 2-oxoacid-dependent dioxygenases and their role in metabolism
    • Prescott, A.G. & Lloyd, M.D. The iron(II) and 2-oxoacid-dependent dioxygenases and their role in metabolism. Nat. Prod. Rep. 17, 367-383 (2000).
    • (2000) Nat. Prod. Rep. , vol.17 , pp. 367-383
    • Prescott, A.G.1    Lloyd, M.D.2
  • 28
    • 0021158796 scopus 로고
    • Stereochemistry of the incorporation of valine methyl groups into methylene groups in cephalosporin C
    • Pang, C.P. et al. Stereochemistry of the incorporation of valine methyl groups into methylene groups in cephalosporin C. Biochem. J. 222, 777-788 (1984).
    • (1984) Biochem. J. , vol.222 , pp. 777-788
    • Pang, C.P.1
  • 29
    • 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, 4760-4767 (1985).
    • (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
  • 30
    • 0023677432 scopus 로고
    • The ring expansion of penams to cephams: A possible biomimetic process
    • Baldwin, J.E., Adlington, R.M., Kang, T.W., Lee, E. & Schofield, C.J. The ring expansion of penams to cephams: a possible biomimetic process. Tetrahedron 44, 5953-5957 (1988).
    • (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
  • 31
    • 0033572748 scopus 로고    scopus 로고
    • β-secondary kinetic isotope effects in the clavaminate synthase-catalysed oxidative cyclization of proclavaminic acid and in related azetidinone model reactions
    • Iwata-Reuyl, D., Basak, A. & Townsend, C.A. β-Secondary kinetic isotope effects in the clavaminate synthase-catalysed oxidative cyclization of proclavaminic acid and in related azetidinone model reactions. J. Am. Chem. Soc. 121, 11356-11368 (1999).
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 11356-11368
    • Iwata-Reuyl, D.1    Basak, A.2    Townsend, C.A.3
  • 32
    • 0033608080 scopus 로고    scopus 로고
    • Mechanism-based inactivation of the human prolyl-4-hydroxylase by 5-oxaproline-containing peptides: Evidence for a prolyl radical intermediate
    • Wu, M., Moon, H.-S. & Begley, T.P. Mechanism-based inactivation of the human prolyl-4-hydroxylase by 5-oxaproline-containing peptides: evidence for a prolyl radical intermediate. J. Am. Chem. Soc. 121, 587-588 (1999).
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 587-588
    • Wu, M.1    Moon, H.-S.2    Begley, T.P.3
  • 33
    • 0001265131 scopus 로고
    • Chemistry of cephalosporin antibiotics. III. Chemical correlation of penicillin and cephalosporin antibiotics
    • Morin, R.B. et al. Chemistry of cephalosporin antibiotics. III. Chemical correlation of penicillin and cephalosporin antibiotics. J. Am. Chem. Soc. 85, 1896-1897 (1963).
    • (1963) J. Am. Chem. Soc. , vol.85 , pp. 1896-1897
    • Morin, R.B.1
  • 34
    • 0036305290 scopus 로고    scopus 로고
    • C-terminus modification of Streptomyces clavuligerus deacetoxycephalosporin C synthase improves catalysis with an expanded substrate specificity
    • Chin, H.S. & Sim, T.S. C-terminus modification of Streptomyces clavuligerus deacetoxycephalosporin C synthase improves catalysis with an expanded substrate specificity. Biochem. Biophys. Res. Commun. 295, 55-61 (2002).
    • (2002) Biochem. Biophys. Res. Commun. , vol.295 , pp. 55-61
    • Chin, H.S.1    Sim, T.S.2
  • 35
    • 7444269437 scopus 로고    scopus 로고
    • Catalysis, evolution and life
    • Szoke, A., Scott, W.G. & Hajdu, J. Catalysis, evolution and life. FEBS Lett. 553, 18-20 (2003).
    • (2003) FEBS Lett. , vol.553 , pp. 18-20
    • Szoke, A.1    Scott, W.G.2    Hajdu, J.3
  • 36
    • 0025230340 scopus 로고
    • Enzymatic-reaction selectivity by negative catalysis or how do enzymes deal with highly reactive intermediates
    • Retey, J. Enzymatic-reaction selectivity by negative catalysis or how do enzymes deal with highly reactive intermediates. Angew. Chem. Int. Ed. 29, 355-361 (1990).
    • (1990) Angew. Chem. Int. Ed. , vol.29 , pp. 355-361
    • Retey, J.1
  • 37
    • 0033574483 scopus 로고    scopus 로고
    • Studies on the active site of deacetoxycephalosporin C synthase
    • Lloyd, M.D. et al. Studies on the active site of deacetoxycephalosporin C synthase. J. Mol. Biol. 287, 943-960 (1999).
    • (1999) J. Mol. Biol. , vol.287 , pp. 943-960
    • Lloyd, M.D.1
  • 38
    • 0035207968 scopus 로고    scopus 로고
    • Multiple isomorphous replacement on merohedral twins: Structure determination of deacetoxycephalosporin C synthase
    • Terwisscha van Scheltinga, A.C., Valegård, K., Subramanian, R., Hajdu, J. & Andersson, I. Multiple isomorphous replacement on merohedral twins: structure determination of deacetoxycephalosporin C synthase. Acta Crystallogr. D 57, 1776-1785 (2001).
    • (2001) Acta Crystallogr. D , vol.57 , pp. 1776-1785
    • Terwisscha Van Scheltinga, A.C.1    Valegård, K.2    Subramanian, R.3    Hajdu, J.4    Andersson, I.5
  • 39
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 40
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G.N., Vagin, A.A. & Dodson, E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53, 240-255 (1997).
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 42
    • 0034903751 scopus 로고    scopus 로고
    • Molray - A web interface between 0 and the Pov-Ray ray tracer
    • Harris, M. & Jones, T.A. Molray - a web interface between 0 and the Pov-Ray ray tracer. Acta Crystallogr. D 57, 1201-1203 (2001).
    • (2001) Acta Crystallogr. D , vol.57 , pp. 1201-1203
    • Harris, M.1    Jones, T.A.2
  • 43
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 44
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf, R.M. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. Model. 15, 132-134 (1997).
    • (1997) J. Mol. Graph. Model. , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 45
    • 0030815133 scopus 로고    scopus 로고
    • Raster 3D: Photorealistic molecular graphics
    • Merrit, E.A. & Bacon D.J. Raster 3D: photorealistic molecular graphics. Methods Enzymol. 277, 505-524 (1997).
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merrit, E.A.1    Bacon, D.J.2


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