메뉴 건너뛰기




Volumn 17, Issue 8, 2010, Pages 841-851

Structure of cytochrome P450 PimD suggests epoxidation of the polyene macrolide pimaricin occurs via a hydroperoxoferric intermediate

Author keywords

CHEMBIO; PROTEINS

Indexed keywords

ANTIINFECTIVE AGENT; BENZENE; CYTOCHROME P450; EPOXIDE; NATAMYCIN; PEROXYNITROUS ACID; PROTON;

EID: 77956013893     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2010.05.026     Document Type: Article
Times cited : (47)

References (55)
  • 3
    • 1842450538 scopus 로고    scopus 로고
    • Strain energy of small ring hydrocarbons. Influence of C-H bond dissociation energies
    • R.D. Bach, and O. Dmitrenko Strain energy of small ring hydrocarbons. Influence of C-H bond dissociation energies J. Am. Chem. Soc. 126 2004 4444 4452
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 4444-4452
    • Bach, R.D.1    Dmitrenko, O.2
  • 4
    • 27644547262 scopus 로고    scopus 로고
    • Molecular modelling of membrane activity of amphotericin B, a polyene macrolide antifungal antibiotic
    • M. Baginski, K. Sternal, J. Czub, and E. Borowski Molecular modelling of membrane activity of amphotericin B, a polyene macrolide antifungal antibiotic Acta Biochim. Pol. 52 2005 655 658
    • (2005) Acta Biochim. Pol. , vol.52 , pp. 655-658
    • Baginski, M.1    Sternal, K.2    Czub, J.3    Borowski, E.4
  • 5
    • 34247464340 scopus 로고    scopus 로고
    • Interaction of amphotericin B and its selected derivatives with membranes: Molecular modeling studies
    • M. Baginski, J. Czub, and K. Sternal Interaction of amphotericin B and its selected derivatives with membranes: molecular modeling studies Chem. Rec. 6 2006 320 332
    • (2006) Chem. Rec. , vol.6 , pp. 320-332
    • Baginski, M.1    Czub, J.2    Sternal, K.3
  • 8
    • 0346968196 scopus 로고    scopus 로고
    • Biosynthesis of deoxyamphotericins and deoxyamphoteronolides by engineered strains of Streptomyces nodosus
    • B. Byrne, M. Carmody, E. Gibson, B. Rawlings, and P. Caffrey Biosynthesis of deoxyamphotericins and deoxyamphoteronolides by engineered strains of Streptomyces nodosus Chem. Biol. 10 2003 1215 1224
    • (2003) Chem. Biol. , vol.10 , pp. 1215-1224
    • Byrne, B.1    Carmody, M.2    Gibson, E.3    Rawlings, B.4    Caffrey, P.5
  • 9
    • 47249110302 scopus 로고    scopus 로고
    • Biosynthetic engineering of polyene macrolides towards generation of improved antifungal and antiparasitic agents
    • P. Caffrey, J.F. Aparicio, F. Malpartida, and S.B. Zotchev Biosynthetic engineering of polyene macrolides towards generation of improved antifungal and antiparasitic agents Curr. Top. Med. Chem. 8 2008 639 653
    • (2008) Curr. Top. Med. Chem. , vol.8 , pp. 639-653
    • Caffrey, P.1    Aparicio, J.F.2    Malpartida, F.3    Zotchev, S.B.4
  • 13
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4) The CCP4 suite: programs for protein crystallography Acta Crysallogr D 50 1994 760 763
    • (1994) Acta Crysallogr D , vol.50 , pp. 760-763
  • 14
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building. 1. Tracing protein chains
    • K. Cowtan The Buccaneer software for automated model building. 1. Tracing protein chains Acta Crystallogr. D Biol. Crystallogr. 62 2006 1002 1011
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 1002-1011
    • Cowtan, K.1
  • 18
    • 0015215440 scopus 로고
    • Polyene macrolide antibiotic amphotericin B. Crystal structure of the N-iodoacetyl derivative
    • P. Ganis, G. Avitabile, W. Mechlinski, and C.P. Schaffner Polyene macrolide antibiotic amphotericin B. Crystal structure of the N-iodoacetyl derivative J. Am. Chem. Soc. 93 1971 4560 4564
    • (1971) J. Am. Chem. Soc. , vol.93 , pp. 4560-4564
    • Ganis, P.1    Avitabile, G.2    Mechlinski, W.3    Schaffner, C.P.4
  • 19
  • 20
    • 0037223878 scopus 로고    scopus 로고
    • Cytochrome P450 oxidations in the generation of reactive electrophiles: Epoxidation and related reactions
    • F.P. Guengerich Cytochrome P450 oxidations in the generation of reactive electrophiles: epoxidation and related reactions Arch. Biochem. Biophys. 409 2003 59 71
    • (2003) Arch. Biochem. Biophys. , vol.409 , pp. 59-71
    • Guengerich, F.P.1
  • 21
    • 0032500330 scopus 로고    scopus 로고
    • Theoretical investigation of the proton assisted pathway to formation of cytochrome P450 Compound i
    • D.L. Harris, and G.H. Loew Theoretical investigation of the proton assisted pathway to formation of cytochrome P450 Compound I J. Am. Chem. Soc. 120 1998 8941 8948
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 8941-8948
    • Harris, D.L.1    Loew, G.H.2
  • 22
    • 33750966099 scopus 로고    scopus 로고
    • On the identity and reactivity patterns of the "second oxidant" of the T252A mutant of cytochrome P450cam in the oxidation of 5-methylenenylcamphor
    • H. Hirao, D. Kumar, and S. Shaik On the identity and reactivity patterns of the "second oxidant" of the T252A mutant of cytochrome P450cam in the oxidation of 5-methylenenylcamphor J. Inorg. Biochem. 100 2006 2054 2068
    • (2006) J. Inorg. Biochem. , vol.100 , pp. 2054-2068
    • Hirao, H.1    Kumar, D.2    Shaik, S.3
  • 23
    • 1242274650 scopus 로고    scopus 로고
    • Automated protein crystal structure determination using ELVES
    • J. Holton, and T. Alber Automated protein crystal structure determination using ELVES Proc. Natl. Acad. Sci. USA 101 2004 1537 1542
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 1537-1542
    • Holton, J.1    Alber, T.2
  • 24
    • 0001541099 scopus 로고
    • Uncoupling of the cytochrome P-450cam monooxygenase reaction by a single mutation, threonine-252 to alanine or valine: Possible role of the hydroxy amino acid in oxygen activation
    • M. Imai, H. Shimada, Y. Watanabe, Y. Matsushima-Hibiya, R. Makino, H. Koga, T. Horiuchi, and Y. Ishimura Uncoupling of the cytochrome P-450cam monooxygenase reaction by a single mutation, threonine-252 to alanine or valine: possible role of the hydroxy amino acid in oxygen activation Proc. Natl. Acad. Sci. USA 86 1989 7823 7827
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 7823-7827
    • Imai, M.1    Shimada, H.2    Watanabe, Y.3    Matsushima-Hibiya, Y.4    Makino, R.5    Koga, H.6    Horiuchi, T.7    Ishimura, Y.8
  • 26
    • 4644317084 scopus 로고    scopus 로고
    • Hydroperoxoferric heme intermediate as a second electrophilic oxidant in cytochrome P450-catalyzed reactions
    • S. Jin, T.A. Bryson, and J.H. Dawson Hydroperoxoferric heme intermediate as a second electrophilic oxidant in cytochrome P450-catalyzed reactions J. Biol. Inorg. Chem. 9 2004 644 653
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 644-653
    • Jin, S.1    Bryson, T.A.2    Dawson, J.H.3
  • 27
    • 0037155911 scopus 로고    scopus 로고
    • Kinetic characterization of compound i formation in the thermostable cytochrome P450 CYP119
    • D.G. Kellner, S.C. Hung, K.E. Weiss, and S.G. Sligar Kinetic characterization of compound I formation in the thermostable cytochrome P450 CYP119 J. Biol. Chem. 277 2002 9641 9644
    • (2002) J. Biol. Chem. , vol.277 , pp. 9641-9644
    • Kellner, D.G.1    Hung, S.C.2    Weiss, K.E.3    Sligar, S.G.4
  • 28
    • 0003076963 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data
    • Leslie, A.G.W. (1992). Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4 ESF-EAMCB Newslett Protein Crystallogr 26.
    • (1992) Joint CCP4 ESF-EAMCB Newslett Protein Crystallogr , pp. 26
    • Leslie, A.G.W.1
  • 29
    • 0024832753 scopus 로고
    • A conserved residue of P450 involved in haem-oxygen stability and activation
    • S.A. Martinis, W.M. Atkins, P.S. Stayton, and S.G. Sligar A conserved residue of P450 involved in haem-oxygen stability and activation J. Am. Chem. Soc. 111 1989 9252 9253
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 9252-9253
    • Martinis, S.A.1    Atkins, W.M.2    Stayton, P.S.3    Sligar, S.G.4
  • 30
    • 0034945645 scopus 로고    scopus 로고
    • Engineered biosynthesis of novel polyenes: A pimaricin derivative produced by targeted gene disruption in Streptomyces natalensis
    • M.V. Mendes, E. Recio, R. Fouces, R. Luiten, J.F. Martin, and J.F. Aparicio Engineered biosynthesis of novel polyenes: a pimaricin derivative produced by targeted gene disruption in Streptomyces natalensis Chem. Biol. 8 2001 635 644
    • (2001) Chem. Biol. , vol.8 , pp. 635-644
    • Mendes, M.V.1    Recio, E.2    Fouces, R.3    Luiten, R.4    Martin, J.F.5    Aparicio, J.F.6
  • 31
    • 14244251991 scopus 로고    scopus 로고
    • Characterization of the polyene macrolide P450 epoxidase from Streptomyces natalensis that converts de-epoxypimaricin into pimaricin
    • M.V. Mendes, N. Anton, J.F. Martin, and J.F. Aparicio Characterization of the polyene macrolide P450 epoxidase from Streptomyces natalensis that converts de-epoxypimaricin into pimaricin Biochem. J. 386 2005 57 62
    • (2005) Biochem. J. , vol.386 , pp. 57-62
    • Mendes, M.V.1    Anton, N.2    Martin, J.F.3    Aparicio, J.F.4
  • 32
    • 4644275807 scopus 로고    scopus 로고
    • Mechanism of oxidation reactions catalyzed by cytochrome P450 enzymes
    • B. Meunier, S.P. deVisser, and S. Shaik Mechanism of oxidation reactions catalyzed by cytochrome P450 enzymes Chem. Rev. 104 2004 3947 3980
    • (2004) Chem. Rev. , vol.104 , pp. 3947-3980
    • Meunier, B.1    Devisser, S.P.2    Shaik, S.3
  • 34
    • 0242582120 scopus 로고    scopus 로고
    • Crystal structures of epothilone D-bound, epothilone B-bound, and substrate-free forms of cytochrome P450epoK
    • S. Nagano, H. Li, H. Shimizu, C. Nishida, H. Ogura, P.R. Ortiz de Montellano, and T.L. Poulos Crystal structures of epothilone D-bound, epothilone B-bound, and substrate-free forms of cytochrome P450epoK J. Biol. Chem. 278 2003 44886 44893
    • (2003) J. Biol. Chem. , vol.278 , pp. 44886-44893
    • Nagano, S.1    Li, H.2    Shimizu, H.3    Nishida, C.4    Ogura, H.5    Ortiz De Montellano, P.R.6    Poulos, T.L.7
  • 35
    • 20444491589 scopus 로고    scopus 로고
    • Crystal structures of the ferrous dioxygen complex of wild-type cytochrome P450eryF and its mutants, A245S and A245T: Investigation of the proton transfer system in P450eryF
    • S. Nagano, J.R. Cupp-Vickery, and T.L. Poulos Crystal structures of the ferrous dioxygen complex of wild-type cytochrome P450eryF and its mutants, A245S and A245T: investigation of the proton transfer system in P450eryF J. Biol. Chem. 280 2005 22102 22107
    • (2005) J. Biol. Chem. , vol.280 , pp. 22102-22107
    • Nagano, S.1    Cupp-Vickery, J.R.2    Poulos, T.L.3
  • 36
    • 0037228374 scopus 로고    scopus 로고
    • Multiple mechanisms and multiple oxidants in P450-catalyzed hydroxylations
    • M. Newcomb, P.F. Hollenberg, and M.J. Coon Multiple mechanisms and multiple oxidants in P450-catalyzed hydroxylations Arch. Biochem. Biophys. 409 2003 72 79
    • (2003) Arch. Biochem. Biophys. , vol.409 , pp. 72-79
    • Newcomb, M.1    Hollenberg, P.F.2    Coon, M.J.3
  • 39
    • 0037139511 scopus 로고    scopus 로고
    • Searching for the second oxidant in the catalytic cycle of cytochrome P450: A theoretical investigation of the iron(III)-hydroperoxo species and its epoxidation pathways
    • F. Ogliaro, S.P. de Visser, S. Cohen, P.K. Sharma, and S. Shaik Searching for the second oxidant in the catalytic cycle of cytochrome P450: a theoretical investigation of the iron(III)-hydroperoxo species and its epoxidation pathways J. Am. Chem. Soc. 124 2002 2806 2817
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 2806-2817
    • Ogliaro, F.1    De Visser, S.P.2    Cohen, S.3    Sharma, P.K.4    Shaik, S.5
  • 40
  • 41
    • 0035984571 scopus 로고    scopus 로고
    • Oxidizing species in the mechanism of cytochrome P450
    • P.R. Ortiz de Montellano, and J.J. De Voss Oxidizing species in the mechanism of cytochrome P450 Nat. Prod. Rep. 19 2002 477 493
    • (2002) Nat. Prod. Rep. , vol.19 , pp. 477-493
    • Ortiz De Montellano, P.R.1    De Voss, J.J.2
  • 43
    • 0038679668 scopus 로고
    • Polyene macrolides in clinical practice: Pharmacology and adverse and other effects
    • C.P. Schaffner Polyene macrolides in clinical practice: pharmacology and adverse and other effects S. Omura, Macrolide Antibiotics, Chemistry, Biology and Practice 1984 Academic Press New York 457 507
    • (1984) Macrolide Antibiotics, Chemistry, Biology and Practice , pp. 457-507
    • Schaffner, C.P.1
  • 44
    • 34249787625 scopus 로고    scopus 로고
    • Reactivity patterns of cytochrome P450 enzymes: Multifunctionality of the active species, and the two states-two oxidants conundrum
    • S. Shaik, H. Hirao, and D. Kumar Reactivity patterns of cytochrome P450 enzymes: multifunctionality of the active species, and the two states-two oxidants conundrum Nat. Prod. Rep. 24 2007 533 552
    • (2007) Nat. Prod. Rep. , vol.24 , pp. 533-552
    • Shaik, S.1    Hirao, H.2    Kumar, D.3
  • 45
    • 53549099423 scopus 로고    scopus 로고
    • Spectra and kinetic studies of the compound i derivative of cytochrome P450 119
    • X. Sheng, J.H. Horner, and M. Newcomb Spectra and kinetic studies of the compound I derivative of cytochrome P450 119 J. Am. Chem. Soc. 130 2008 13310 13320
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 13310-13320
    • Sheng, X.1    Horner, J.H.2    Newcomb, M.3
  • 47
    • 20144385036 scopus 로고    scopus 로고
    • Reaction of ferric cytochrome P450cam with peracids: Kinetic characterization of intermediates on the reaction pathway
    • T. Spolitak, J.H. Dawson, and D.P. Ballou Reaction of ferric cytochrome P450cam with peracids: kinetic characterization of intermediates on the reaction pathway J. Biol. Chem. 280 2005 20300 20309
    • (2005) J. Biol. Chem. , vol.280 , pp. 20300-20309
    • Spolitak, T.1    Dawson, J.H.2    Ballou, D.P.3
  • 48
    • 33750953768 scopus 로고    scopus 로고
    • Rapid kinetics investigations of peracid oxidation of ferric cytochrome P450cam: Nature and possible function of compound ES
    • T. Spolitak, J.H. Dawson, and D.P. Ballou Rapid kinetics investigations of peracid oxidation of ferric cytochrome P450cam: nature and possible function of compound ES J. Inorg. Biochem. 100 2006 2034 2044
    • (2006) J. Inorg. Biochem. , vol.100 , pp. 2034-2044
    • Spolitak, T.1    Dawson, J.H.2    Ballou, D.P.3
  • 49
    • 43249095177 scopus 로고    scopus 로고
    • Replacement of tyrosine residues by phenylalanine in cytochrome P450cam alters the formation of Cpd II-like species in reactions with artificial oxidants
    • T. Spolitak, J.H. Dawson, and D.P. Ballou Replacement of tyrosine residues by phenylalanine in cytochrome P450cam alters the formation of Cpd II-like species in reactions with artificial oxidants J. Biol. Inorg. Chem. 13 2008 599 611
    • (2008) J. Biol. Inorg. Chem. , vol.13 , pp. 599-611
    • Spolitak, T.1    Dawson, J.H.2    Ballou, D.P.3
  • 51
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins, and T.J. Gibson CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22 1994 4673 4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 52
    • 0032584090 scopus 로고    scopus 로고
    • Epoxidation of olefins by cytochrome P450: Evidence from site-specific mutagenesis for hydroperoxo-iron as an electrophilic oxidant
    • A.D.N. Vaz, D.F. McGinnity, and M.J. Coon Epoxidation of olefins by cytochrome P450: Evidence from site-specific mutagenesis for hydroperoxo-iron as an electrophilic oxidant Proc. Natl. Acad. Sci. USA 95 1998 3555 3560
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3555-3560
    • Vaz, A.D.N.1    McGinnity, D.F.2    Coon, M.J.3
  • 53
    • 33646094958 scopus 로고    scopus 로고
    • Characterization of the P450 monooxygenase NysL, responsible for C-10 hydroxylation during biosynthesis of the polyene macrolide antibiotic nystatin in Streptomyces noursei
    • O. Volokhan, H. Sletta, T.E. Ellingsen, and S.B. Zotchev Characterization of the P450 monooxygenase NysL, responsible for C-10 hydroxylation during biosynthesis of the polyene macrolide antibiotic nystatin in Streptomyces noursei Appl. Environ. Microbiol. 72 2006 2514 2519
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 2514-2519
    • Volokhan, O.1    Sletta, H.2    Ellingsen, T.E.3    Zotchev, S.B.4
  • 54
    • 0036379348 scopus 로고    scopus 로고
    • Solution NMR structure of five representative glycosylated polyene macrolide antibiotics with a sterol-dependent antifungal activity
    • L. Volpon, and J.M. Lancelin Solution NMR structure of five representative glycosylated polyene macrolide antibiotics with a sterol-dependent antifungal activity Eur. J. Biochem. 269 2002 4533 4541
    • (2002) Eur. J. Biochem. , vol.269 , pp. 4533-4541
    • Volpon, L.1    Lancelin, J.M.2
  • 55
    • 0037239016 scopus 로고    scopus 로고
    • Polyene macrolide antibiotics and their applications in human therapy
    • S.B. Zotchev Polyene macrolide antibiotics and their applications in human therapy Curr. Med. Chem. 10 2003 211 223
    • (2003) Curr. Med. Chem. , vol.10 , pp. 211-223
    • Zotchev, S.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.