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Volumn 288, Issue 44, 2013, Pages 31602-31615

Complexes of trypanosoma cruzi Sterol 14α-Demethylase (CYP51) with Two Pyridine-based Drug Candidates for Chagas Disease: Structural basis for pathogen selectivity

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOLS; CODES (SYMBOLS); ENZYME ACTIVITY; IRON;

EID: 84887102957     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.497990     Document Type: Article
Times cited : (81)

References (61)
  • 1
    • 0024430490 scopus 로고
    • Mechanistic studies of lanosterol 14α-methyl demethylase: Substrate requirements for the component reactions catalyzed by a single cytochrome P-450 isozyme
    • Fischer, R. T., and Stam., S. H., Johnson, P. R., Ko, S. S., and Magolda., R. L., Gaylor, J. L., and Trzaskos, J. M. (1989) Mechanistic studies of lanosterol 14α-methyl demethylase: substrate requirements for the component reactions catalyzed by a single cytochrome P-450 isozyme. J. Lipid Res. 30, 1621-1632 (Pubitemid 19271057)
    • (1989) Journal of Lipid Research , vol.30 , Issue.10 , pp. 1621-1632
    • Fischer, R.T.1    Stam, S.H.2    Johnson, P.R.3    Ko, S.S.4    Magolda, R.L.5    Gaylor, J.L.6    Trzaskos, J.M.7
  • 2
    • 0021717363 scopus 로고
    • Cytochrome P-450-dependent oxidation of lanosterol in cholesterol biosynthesis. Microsomal electron transport and C-32 demethylation
    • Trzaskos, J. M., and Bowen., W. D., Shafiee, A., Fischer, R. T., and Gaylor, J. L. (1984) Cytochrome P-450-dependent oxidation of lanosterol in cholesterol biosynthesis. Microsomal electron transport and C-32 demethylation. J. Biol. Chem. 259, 13402-13412 (Pubitemid 15223873)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.21 , pp. 13402-13412
    • Trzaskos, J.M.1    Bowen, W.D.2    Shafiee, A.3
  • 4
    • 33846387040 scopus 로고    scopus 로고
    • Sterol 14α-demethylase cytochrome P450 (CYP51), a P450 in all biological kingdoms
    • DOI 10.1016/j.bbagen.2006.07.018, PII S0304416506002145
    • Lepesheva, G. I., and Waterman, M. R. (2007) Sterol 14a-demethylase cytochrome P450 (CYP51), a P450 in all biological kingdoms. Biochim. Biophys. Acta 1770, 467-477 (Pubitemid 46136743)
    • (2007) Biochimica et Biophysica Acta - General Subjects , vol.1770 , Issue.3 , pp. 467-477
    • Lepesheva, G.I.1    Waterman, M.R.2
  • 6
    • 0016386380 scopus 로고
    • Chemotherapy of systemic mycoses
    • Bennett, J. E. (1974) Chemotherapy of systemic mycoses. N. Engl. J. Med. 290, 320-323
    • (1974) N. Engl. J. Med. , vol.290 , pp. 320-323
    • Bennett, J.E.1
  • 8
    • 1642335814 scopus 로고    scopus 로고
    • History of the development of azole derivatives
    • Maertens, J. A. (2004) History of the development of azole derivatives. Clin. Microbiol. Infect. 10, Suppl. 1, 1-10 (Pubitemid 38379948)
    • (2004) Clinical Microbiology and Infection , vol.10 , Issue.SUPPL. 1 , pp. 1-10
    • Maertens, J.A.1
  • 9
    • 79960975304 scopus 로고    scopus 로고
    • Targeting trypanosoma cruzi sterol 14a-demethylase (CYP51)
    • Lepesheva, G.I., Villalta, F., and Waterman, M. R. (2011) Targeting Trypanosoma cruzi sterol 14a-demethylase (CYP51). Adv. Parasitol. 75, 65-87
    • (2011) Adv. Parasitol. , vol.75 , pp. 65-87
    • Lepesheva, G.I.1    Villalta, F.2    Waterman, M.R.3
  • 10
    • 80051901437 scopus 로고    scopus 로고
    • Drug developers finally take aim at a neglected disease
    • Leslie, M. (2011) Drug developers finally take aim at a neglected disease. Science 333, 933-935
    • (2011) Science , vol.333 , pp. 933-935
    • Leslie, M.1
  • 13
    • 0023681312 scopus 로고
    • Antiproliferative synergism of the allylamine SF 86-327 and ketoconazole on epimastigotes and amastigotes of trypanosoma (Schizotrypanum) cruzi
    • Urbina, J. A., Lazardi, K., Aguirre, T., Piras, M. M., and Piras, R. (1988) Antiproliferative synergism of the allylamine SF 86-327 and ketoconazole on epimastigotes and amastigotes of Trypanosoma (Schizotrypanum) cruzi. Antimicrob. Agents Chemother. 32, 1237-1242
    • (1988) Antimicrob. Agents Chemother. , vol.32 , pp. 1237-1242
    • Urbina, J.A.1    Lazardi, K.2    Aguirre, T.3    Piras, M.M.4    Piras, R.5
  • 15
    • 0343527887 scopus 로고    scopus 로고
    • A combination of benznidazole and ketoconazole enhances efficacy of chemotherapy of experimental Chagas' disease
    • Araújo, M. S., Martins-Filho, O. A., Pereira, M. E., and Brener, Z. (2000) A combination of benznidazole and ketoconazole enhances efficacy of chemotherapy of experimental Chagas' disease. J. Antimicrob. Chemother. 45, 819-824 (Pubitemid 30348953)
    • (2000) Journal of Antimicrobial Chemotherapy , vol.45 , Issue.6 , pp. 819-824
    • Araujo, M.S.S.1    Martins-Filho, O.A.2    Pereira, M.E.S.3    Brener, Z.4
  • 16
    • 0033987127 scopus 로고    scopus 로고
    • Activities of the triazole derivative SCH 56592 (Posaconazole) against drug-resistant strains of the protozoan parasite Trypanosoma (Schizotrypanum) cruzi in immunocompetent and immunosuppressed murine hosts
    • Molina, J., Martins-Filho, O., Brener, Z., and Romanha., A. J., Loebenberg, D., and Urbina, J. A. (2000) Activities of the triazole derivative SCH 56592 (posaconazole) against drug-resistant strains of the protozoan parasite Trypanosoma (Schizotrypanum) cruzi in immunocompetent and immunosuppressed murine hosts. Antimicrob. Agents Chemother. 44, 150-155 (Pubitemid 30010686)
    • (2000) Antimicrobial Agents and Chemotherapy , vol.44 , Issue.1 , pp. 150-155
    • Molina, J.1    Martins-Filho, O.2    Brener, Z.3    Romanha, A.J.4    Loebenberg, D.5    Urbina, J.A.6
  • 17
    • 69049116505 scopus 로고    scopus 로고
    • Ergosterol biosynthesis and drug development for chagas disease
    • Urbina, J. A. (2009) Ergosterol biosynthesis and drug development for Chagas disease. Mem. Inst. Oswaldo Cruz 104, Suppl. 1, 311-318
    • (2009) Mem. Inst. Oswaldo Cruz , vol.104 , Issue.SUPPL. 1 , pp. 311-318
    • Urbina, J.A.1
  • 18
    • 77954207000 scopus 로고    scopus 로고
    • Chagas disease: Pushing through the pipeline
    • Clayton, J. (2010) Chagas disease: pushing through the pipeline. Nature 465, S12-S15
    • (2010) Nature , vol.465
    • Clayton, J.1
  • 19
    • 23944466866 scopus 로고    scopus 로고
    • The protein farnesyltransferase inhibitor tipifarnib as a new lead for the development of drugs against Chagas disease
    • DOI 10.1021/jm050441z
    • Hucke, O., and Gelb., M. H., Verlinde, C L., and Buckner, F. S. (2005) The protein farnesyltransferase inhibitor tipifarnib as a new lead for the development of drugs against Chagas disease. J. Med. Chem. 48, 5415-5418 (Pubitemid 41209239)
    • (2005) Journal of Medicinal Chemistry , vol.48 , Issue.17 , pp. 5415-5418
    • Hucke, O.1    Gelb, M.H.2    Verlinde, C.L.M.J.3    Buckner, F.S.4
  • 23
    • 0037327813 scopus 로고    scopus 로고
    • Fatty acid and sterol metabolism: Potential antimicrobial targets in apicomplexan and trypanosomatid parasitic protozoa
    • DOI 10.1016/S0166-6851(02)00280-3, PII S0166685102002803
    • Roberts, C W., McLeod, R., Rice, D. W., Ginger, M., Chance, M. L., and Goad, L. J. (2003) Fatty acid and sterol metabolism: potential antimicrobial targets in apicomplexan and trypanosomatid parasitic protozoa. Mol. Biochem. Parasitol. 126, 129-142 (Pubitemid 36255612)
    • (2003) Molecular and Biochemical Parasitology , vol.126 , Issue.2 , pp. 129-142
    • Roberts, C.W.1    McLeod, R.2    Rice, D.W.3    Ginger, M.4    Chance, M.L.5    Goad, L.J.6
  • 24
    • 0025114817 scopus 로고
    • Ultrastructural alterations induced by two ergosterol biosynthesis inhibitors, ketoconazole and terbinafine, on epimastigotes and amastigotes of Trypanosoma (Schizotrypanum) cruzi
    • Lazardi, K., and Urbina., J. A., and de Souza, W. (1990) Ultrastructural alterations induced by two ergosterol biosynthesis inhibitors, ketoconazole and terbinafine, on epimastigotes and amastigotes of Trypanosoma (Schizotrypanum) cruzi. Antimicrob. Agents Chemother. 34, 2097-2105 (Pubitemid 20373840)
    • (1990) Antimicrobial Agents and Chemotherapy , vol.34 , Issue.11 , pp. 2097-2105
    • Lazardi, K.1    Urbina, J.A.2    De Souza, W.3
  • 26
    • 36049032778 scopus 로고    scopus 로고
    • Sterol 14α-Demethylase as a Potential Target for Antitrypanosomal Therapy: Enzyme Inhibition and Parasite Cell Growth
    • DOI 10.1016/j.chembiol.2007.10.011, PII S1074552107003626
    • Lepesheva, G. I., and Ott., R. D., Hargrove, T. Y., Kleshchenko, Y. Y., Schuster, I., and Nes., W. D., Hill, G. C, Villalta, F., and Waterman, M. R. (2007) Sterol 14a-demethylase as a potential target for antitrypanosomal therapy: enzyme inhibition and parasite cell growth. Chem. Biol. 14, 1283-1293 (Pubitemid 350102245)
    • (2007) Chemistry and Biology , vol.14 , Issue.11 , pp. 1283-1293
    • Lepesheva, G.I.1    Ott, R.D.2    Hargrove, T.Y.3    Kleshchenko, Y.Y.4    Schuster, I.5    Nes, W.D.6    Hill, G.C.7    Villalta, F.8    Waterman, M.R.9
  • 29
    • 33645639221 scopus 로고    scopus 로고
    • CYP51 from Trypanosoma cruzi: A phyla-specific residue in the B′ helix defines substrate preferences of sterol 14α-demethylase
    • DOI 10.1074/jbc.M510317200
    • Lepesheva, G. I., Zaitseva, N G., Nes, W. D., Zhou, W., Arase, M., Liu, J., Hill, G. C, and Waterman, M. R. (2006) CYP51 from Trypanosoma cruzi: a phyla-specific residue in the B' helix defines substrate preferences of sterol 14alpha-demethylase. J. Biol. Chem. 281, 3577-3585 (Pubitemid 43845975)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.6 , pp. 3577-3585
    • Lepesheva, G.I.1    Zaitseva, N.G.2    Nes, W.D.3    Zhou, W.4    Arase, M.5    Liu, J.6    Hill, G.C.7    Waterman, M.R.8
  • 30
    • 4143104606 scopus 로고    scopus 로고
    • CYP51 from Trypanosoma brucei is obtusifoliol-specific
    • DOI 10.1021/bi048967t
    • Lepesheva, G. I., and Nes., W. D., Zhou, W., Hill, G. C, and Waterman, M. R. (2004) CYP51 from Trypanosoma brucei is obtusifoliol-specific. Biochemistry 43, 10789-10799 (Pubitemid 39096721)
    • (2004) Biochemistry , vol.43 , Issue.33 , pp. 10789-10799
    • Lepesheva, G.I.1    Nes, W.D.2    Zhou, W.3    Hill, G.C.4    Waterman, M.R.5
  • 31
    • 79960662249 scopus 로고    scopus 로고
    • Substrate preferences and catalytic parameters determined by structural characteristics of sterol 14a-demethylase (CYP51) from leishmania infantum
    • Hargrove, T. Y., Wawrzak, Z., Liu, J., Nes, W. D., and Waterman., M. R., and Lepesheva, G. I. (2011) Substrate preferences and catalytic parameters determined by structural characteristics of sterol 14a-demethylase (CYP51) from Leishmania infantum. J. Biol. Chem. 286, 26838-26848
    • (2011) J. Biol. Chem. , vol.286 , pp. 26838-26848
    • Hargrove, T.Y.1    Wawrzak, Z.2    Liu, J.3    Nes, W.D.4    Waterman, M.R.5    Lepesheva, G.I.6
  • 32
    • 84862909219 scopus 로고    scopus 로고
    • Structural complex of sterol 14a-demethylase (CYP51) with 14a-methylenecyclopropyl-A7-24, 25-dihydrolanosterol
    • Hargrove, T. Y., Wawrzak, Z., Liu, J., Waterman, M. R., and Nes., W. D., and Lepesheva, G. I. (2012) Structural complex of sterol 14a-demethylase (CYP51) with 14a-methylenecyclopropyl-A7-24, 25-dihydrolanosterol. J. Lipid Res. 53, 311-320
    • (2012) J. Lipid Res. , vol.53 , pp. 311-320
    • Hargrove, T.Y.1    Wawrzak, Z.2    Liu, J.3    Waterman, M.R.4    Nes, W.D.5    Lepesheva, G.I.6
  • 36
    • 78649446542 scopus 로고    scopus 로고
    • Structural basis for conservation in the CYP51 family
    • Lepesheva, G. I., and Waterman, M. R. (2011) Structural basis for conservation in the CYP51 family. Biochim. Biophys. Acta 1814, 88-93
    • (2011) Biochim. Biophys. Acta , vol.1814 , pp. 88-93
    • Lepesheva, G.I.1    Waterman, M.R.2
  • 37
    • 80051697828 scopus 로고    scopus 로고
    • Sterol 14a-demethylase (CYP51) as a therapeutic target for human trypanosomiasis and leishmaniasis
    • Lepesheva, G. I., and Waterman, M. R. (2011) Sterol 14a-demethylase (CYP51) as a therapeutic target for human trypanosomiasis and leishmaniasis. Curr. Top. Med. Chem. 11, 2060-2071
    • (2011) Curr. Top. Med. Chem. , vol.11 , pp. 2060-2071
    • Lepesheva, G.I.1    Waterman, M.R.2
  • 40
    • 0029861640 scopus 로고    scopus 로고
    • Efficient technique for screening drugs for activity against Trypanosoma cruzi using parasites expressing β-galactosidase
    • Buckner, F. S., and Verlinde., C. L., La Flamme, A. C, and Van Voorhis, W. C. (1996) Efficient technique for screening drugs for activity against Trypanosoma cruzi using parasites expressing β-galactosidase. Antimicrob. Agents Chemother. 40, 2592-2597 (Pubitemid 26367650)
    • (1996) Antimicrobial Agents and Chemotherapy , vol.40 , Issue.11 , pp. 2592-2597
    • Buckner, F.S.1    Verlinde, C.L.M.J.2    La Flamme, A.C.3    Van Voorhis, W.C.4
  • 41
    • 0041664878 scopus 로고    scopus 로고
    • Conservation in the CYP51 family. Role of the B′ helix/BC loop and helices F and G in enzymatic function
    • DOI 10.1021/bi034663f
    • Lepesheva, G. I., Virus, C, and Waterman, M. R. (2003) Conservation in the CYP51 family. Role of the B' helix/BC loop and helices F and G in enzymatic function. Biochemistry 42, 9091-9101 (Pubitemid 36935417)
    • (2003) Biochemistry , vol.42 , Issue.30 , pp. 9091-9101
    • Lepesheva, G.I.1    Virus, C.2    Waterman, M.R.3
  • 42
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • Omura, T., and Sato, R. (1964) The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature. J. Biol. Chem. 239, 2370-2378
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 43
    • 84861723942 scopus 로고    scopus 로고
    • Unusual spectroscopic and ligand binding properties of the cytochrome P450-flavodoxin fusion enzyme XplA
    • Bui, S. H, McLean, K. J., and Cheesman., M. R., Bradley, J. M., Rigby, S. E., and Levy., C. W., Leys, D., and Munro, A. W. (2012) Unusual spectroscopic and ligand binding properties of the cytochrome P450-flavodoxin fusion enzyme XplA. J. Biol. Chem. 287, 19699-19714
    • (2012) J. Biol. Chem. , vol.287 , pp. 19699-19714
    • Bui, S.H.1    McLean, K.J.2    Cheesman, M.R.3    Bradley, J.M.4    Rigby, S.E.5    Levy, C.W.6    Leys, D.7    Munro, A.W.8
  • 44
    • 33644874235 scopus 로고    scopus 로고
    • The integration of macromolecular diffraction data
    • Leslie, A. (2006) The integration of macromolecular diffraction data. Acta Crystallogr. D Biol. Crystallogr. 62, 48-57
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 48-57
    • Leslie, A.1
  • 45
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 48
    • 33645050104 scopus 로고    scopus 로고
    • Cytochrome P450s and other enzymes in drug metabolism and toxicity
    • Guengerich, F. P. (2006) Cytochrome P450s and other enzymes in drug metabolism and toxicity. AAPS J. 8, E101-E111
    • (2006) AAPS J. , vol.8
    • Guengerich, F.P.1
  • 49
    • 0035958915 scopus 로고    scopus 로고
    • Folding requirements are different between sterol 14α-demethylase (CYP51) from mycobacterium tuberculosis and human or fungal orthologs
    • Lepesheva, G. I., and Podust., L. M., Bellamine, A., and Waterman, M. R. (2001) Folding requirements are different between sterol 14α-demethylase (CYP51) from Mycobacterium tuberculosis and human or fungal orthologs. J. Biol. Chem. 276, 28413-28420
    • (2001) J. Biol. Chem. , vol.276 , pp. 28413-28420
    • Lepesheva, G.I.1    Podust, L.M.2    Bellamine, A.3    Waterman, M.R.4
  • 54
    • 34548394436 scopus 로고    scopus 로고
    • Inhibition of cytochromes P450: Existing and new promising therapeutic targets
    • DOI 10.1080/03602530701498455, PII 781827648
    • Schuster, I., and Bernhardt, R. (2007) Inhibition of cytochromes P450: existing and new promising therapeutic targets. Drug. Metab. Rev. 39, 481-499 (Pubitemid 47355725)
    • (2007) Drug Metabolism Reviews , vol.39 , Issue.2-3 , pp. 481-499
    • Schuster, I.1    Bernhardt, R.2
  • 55
    • 77954627675 scopus 로고    scopus 로고
    • Azole antimycotics and drug interactions in the perioperative period
    • Saari, T. I., and Olkkola, K. T. (2010) Azole antimycotics and drug interactions in the perioperative period. Curr. Opin. Anaesthesiol. 23, 441-448
    • (2010) Curr. Opin. Anaesthesiol. , vol.23 , pp. 441-448
    • Saari, T.I.1    Olkkola, K.T.2
  • 56
    • 80054724621 scopus 로고    scopus 로고
    • Triazole antifungal agents drug-drug interactions involving hepatic cytochrome P450
    • Gubbins, P. O. (2011) Triazole antifungal agents drug-drug interactions involving hepatic cytochrome P450. Expert Opin. Drug. Metab. Toxicol. 7, 1411-1429
    • (2011) Expert Opin. Drug. Metab. Toxicol. , vol.7 , pp. 1411-1429
    • Gubbins, P.O.1
  • 57
    • 84879070955 scopus 로고    scopus 로고
    • Antifungal azoles: Structural insights into undesired tight binding to cholesterol-metabolizing CYP46A1
    • Mast, N., Zheng, W., Stout, C. D., and Pikuleva, I. A. (2013) Antifungal azoles: structural insights into undesired tight binding to cholesterol- metabolizing CYP46A1. Mol. Pharmacol. 84, 86-94
    • (2013) Mol. Pharmacol. , vol.84 , pp. 86-94
    • Mast, N.1    Zheng, W.2    Stout, C.D.3    Pikuleva, I.A.4
  • 58
    • 39349086422 scopus 로고    scopus 로고
    • Resistance to antifungal agents: Mechanisms and clinical impact
    • DOI 10.1086/524071
    • Kanafani, Z. A., and Perfect, J. R. (2008) Resistance to antifungal agents: mechanisms and clinical impact. Clin. Infect. Dis. 46, 120-128 (Pubitemid 351263573)
    • (2008) Clinical Infectious Diseases , vol.46 , Issue.1 , pp. 120-128
    • Kanafani, Z.A.1    Perfect, J.R.2
  • 59
    • 44849143048 scopus 로고    scopus 로고
    • Mechanisms of resistance to antifungal agents: Yeasts and filamentous fungi
    • Espinel-Ingroff, A. (2008) Mechanisms of resistance to antifungal agents: yeasts and filamentous fungi. Rev. Iberoam. Micol. 25, 101-106 (Pubitemid 351798337)
    • (2008) Revista Iberoamericana de Micologia , vol.25 , Issue.2 , pp. 101-106
    • Espinel-Ingroff, A.1
  • 60
    • 84871585821 scopus 로고    scopus 로고
    • Organocatalytic, enantioselective synthesis of VNI: A robust therapeutic development platform for chagas, a neglected tropical disease
    • Dobish, M. C., Villalta, F., Waterman, M. R., and Lepesheva., G. I., and Johnston, J. N. (2012) Organocatalytic, enantioselective synthesis of VNI: a robust therapeutic development platform for Chagas, a neglected tropical disease. Org. Lett. 14, 6322-6325
    • (2012) Org. Lett. , vol.14 , pp. 6322-6325
    • Dobish, M.C.1    Villalta, F.2    Waterman, M.R.3    Lepesheva, G.I.4    Johnston, J.N.5
  • 61
    • 77950023120 scopus 로고    scopus 로고
    • Structural basis of human CYP51 inhibition by antifungal azoles
    • Strushkevich, N., and Usanov., S. A., and Park, H. W. (2010) Structural basis of human CYP51 inhibition by antifungal azoles. J. Mol. Biol. 397, 1067-1078
    • (2010) J. Mol. Biol. , vol.397 , pp. 1067-1078
    • Strushkevich, N.1    Usanov, S.A.2    Park, H.W.3


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