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Volumn 53, Issue 3, 2009, Pages 1157-1164

Identification, characterization, and azole-binding properties of Mycobacterium smegmatis CYP164A2, a homolog of ML2088, the Sole cytochrome P450 gene of Mycobacterium leprae

Author keywords

[No Author keywords available]

Indexed keywords

CLOTRIMAZOLE; CYTOCHROME P450; ECONAZOLE; FLUCONAZOLE; ITRACONAZOLE; KETOCONAZOLE; MICONAZOLE; PYRROLE; SODIUM CHLORIDE; VORICONAZOLE;

EID: 62949204603     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.01237-08     Document Type: Article
Times cited : (19)

References (38)
  • 1
    • 37549026425 scopus 로고    scopus 로고
    • Novel chemotherapy for tuberculosis: Chemotherapeutic potential of econazole- and moxifloxacin-loaded PLG nanoparticles
    • Ahmad, Z., R. Pandey, S. Sharma, and G. K Khuller. 2008. Novel chemotherapy for tuberculosis: chemotherapeutic potential of econazole- and moxifloxacin-loaded PLG nanoparticles. Int. J. Antimicrob. Agents 31:142-146.
    • (2008) Int. J. Antimicrob. Agents , vol.31 , pp. 142-146
    • Ahmad, Z.1    Pandey, R.2    Sharma, S.3    Khuller, G.K.4
  • 2
    • 33646030623 scopus 로고    scopus 로고
    • Purification and characterization of bovine steroid 21-hydroxylase (P450c21) efficiently expressed in Escherichia coli
    • Arase, M., M. R. Waterman, and N. Kagawa. 2006. Purification and characterization of bovine steroid 21-hydroxylase (P450c21) efficiently expressed in Escherichia coli. Biochem. Biophys. Res. Commun. 344:400-405.
    • (2006) Biochem. Biophys. Res. Commun , vol.344 , pp. 400-405
    • Arase, M.1    Waterman, M.R.2    Kagawa, N.3
  • 3
    • 0033529797 scopus 로고    scopus 로고
    • Characterisation and catalytic properties of the sterol 14α-demethylase from Mycobacterium tuberculosis
    • Bellamine, A., A. T. Mangla, W. D. Nes, and M. R. Waterman. 1999. Characterisation and catalytic properties of the sterol 14α-demethylase from Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. USA 96:8937-8942.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8937-8942
    • Bellamine, A.1    Mangla, A.T.2    Nes, W.D.3    Waterman, M.R.4
  • 4
    • 15744377346 scopus 로고    scopus 로고
    • Fluconazole binding and sterol demethylation in three CYP51 isoforms indicate differences in active site topology
    • Bellamine, A., G. I. Lepesheva, and M. R. Waterman. 2004. Fluconazole binding and sterol demethylation in three CYP51 isoforms indicate differences in active site topology. J. Lipid Res. 45:2000-2007.
    • (2004) J. Lipid Res , vol.45 , pp. 2000-2007
    • Bellamine, A.1    Lepesheva, G.I.2    Waterman, M.R.3
  • 5
    • 34547912161 scopus 로고    scopus 로고
    • Activity of ketoconazole against Mycobacterium tuberculosis in vitro and in the mouse model
    • Byrne, S. T., S. M. Denkin, P. Gu, E. Nuermberger, and Y. Zhang. 2007. Activity of ketoconazole against Mycobacterium tuberculosis in vitro and in the mouse model. J. Med. Microbiol. 56:1047-1051.
    • (2007) J. Med. Microbiol , vol.56 , pp. 1047-1051
    • Byrne, S.T.1    Denkin, S.M.2    Gu, P.3    Nuermberger, E.4    Zhang, Y.5
  • 6
    • 0032508046 scopus 로고    scopus 로고
    • Cole, S. T., R. Brosch, J. Parkhill, T. Garnier, C. Churcher, D. Harris, S. V. Gordon, K. Eiglmeier, S. Gas, C. E. Barry III, F. Tekaia, K. Badcock, D. Basham, D. Brown, T. Chillingworth, R. Connor, R. Davies, K. Devlin, T. Feltwell, S. Gentles, N. Hamlin, S. Holroyd, T. Hornsby, K. Jagels, A. Krogh, J. McLean, S. Moule, L. Murphy, K. Oliver, J. Osborne, M. A. Quail, M.-A. Rajandream, J. Rodgers, S. Rutter, K. Seeger, J. Skelton, R. Squares, S. Squares, J. E. Sulston, K. Taylor, S. Whitehead, B. G. Barrell, et al. 1998. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393:537-544.
    • Cole, S. T., R. Brosch, J. Parkhill, T. Garnier, C. Churcher, D. Harris, S. V. Gordon, K. Eiglmeier, S. Gas, C. E. Barry III, F. Tekaia, K. Badcock, D. Basham, D. Brown, T. Chillingworth, R. Connor, R. Davies, K. Devlin, T. Feltwell, S. Gentles, N. Hamlin, S. Holroyd, T. Hornsby, K. Jagels, A. Krogh, J. McLean, S. Moule, L. Murphy, K. Oliver, J. Osborne, M. A. Quail, M.-A. Rajandream, J. Rodgers, S. Rutter, K. Seeger, J. Skelton, R. Squares, S. Squares, J. E. Sulston, K. Taylor, S. Whitehead, B. G. Barrell, et al. 1998. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393:537-544.
  • 7
    • 0035931926 scopus 로고    scopus 로고
    • Cole, S. T., K. Eiglmeier, J. Parkhill, K. D. James, N. R. Thomson, P. R. Wheeler, N. Honore, T. Garnier, C. Churcher, D. Harris, K. Mungall, D. Basham, D. Brown, T. Chillingworth, R. Connor, R. M. Davies, K. Devlin, S. Duthoy, T. Feltwell, A. Fraser, N. Hamlin, S. Holroyd, T. Hornsby, K. Jagels, C. Lacroix, J. Maclean, S. Moule, L. Murphy, K. Oliver, M. A. Quail, M.-A. Rajandream, K. M. Rutherford, S. Rutter, K. Seeger, S. Simon, M. Simmonds, J. Skelton, R. Squares, S. Squares, K. Stevens, K. Taylor, S. Whitehead, J. R. Woodward, and B. G. Barrell. 2001. Massive gene decay in the leprosy bacillus. Nature 409:1007-1011.
    • Cole, S. T., K. Eiglmeier, J. Parkhill, K. D. James, N. R. Thomson, P. R. Wheeler, N. Honore, T. Garnier, C. Churcher, D. Harris, K. Mungall, D. Basham, D. Brown, T. Chillingworth, R. Connor, R. M. Davies, K. Devlin, S. Duthoy, T. Feltwell, A. Fraser, N. Hamlin, S. Holroyd, T. Hornsby, K. Jagels, C. Lacroix, J. Maclean, S. Moule, L. Murphy, K. Oliver, M. A. Quail, M.-A. Rajandream, K. M. Rutherford, S. Rutter, K. Seeger, S. Simon, M. Simmonds, J. Skelton, R. Squares, S. Squares, K. Stevens, K. Taylor, S. Whitehead, J. R. Woodward, and B. G. Barrell. 2001. Massive gene decay in the leprosy bacillus. Nature 409:1007-1011.
  • 8
    • 2542623028 scopus 로고    scopus 로고
    • An electrostatically driven conformational transition is involved in the mechanisms of substrate binding and cooperativity in cytochrome P450eryF
    • Davydov, D. R., A. E. Botchkareva, S. Kumar, Y. Q. He, and J. R. Halpert. 2004. An electrostatically driven conformational transition is involved in the mechanisms of substrate binding and cooperativity in cytochrome P450eryF. Biochemistry 43:6475-6485.
    • (2004) Biochemistry , vol.43 , pp. 6475-6485
    • Davydov, D.R.1    Botchkareva, A.E.2    Kumar, S.3    He, Y.Q.4    Halpert, J.R.5
  • 9
    • 0028606520 scopus 로고    scopus 로고
    • Deprez, E., N. C. Gerber, C. Di Primo, P. Douzou, S. G. Sligar, and G. Hui Bon Hoa. 1994. Electrostatic control of the substrate access channel in cytochrome P-450cam. Biochemistry 33:14464-14468.
    • Deprez, E., N. C. Gerber, C. Di Primo, P. Douzou, S. G. Sligar, and G. Hui Bon Hoa. 1994. Electrostatic control of the substrate access channel in cytochrome P-450cam. Biochemistry 33:14464-14468.
  • 10
    • 0037145071 scopus 로고    scopus 로고
    • Deprez, E., E. Gill, V. Helms, R. C. Wade, and G. Hui Bon Hoa. 2002. Specific and non-specific effects of potassium cations on substrate-protein interactions in cytochromes P450cam and P450lin. J. Inorg. Biochem. 91:597-606.
    • Deprez, E., E. Gill, V. Helms, R. C. Wade, and G. Hui Bon Hoa. 2002. Specific and non-specific effects of potassium cations on substrate-protein interactions in cytochromes P450cam and P450lin. J. Inorg. Biochem. 91:597-606.
  • 11
    • 47249136624 scopus 로고    scopus 로고
    • X-ray structure of 4,4′- dihydroxybenzophenone mimicking sterol substrate in the active site of sterol 14α-demethylase (CYP51)
    • Eddine, A. N., J. P. von Kries, M. V. Podust, T. Warrier, S. H. E. Kaufmann, and L. M. Podust. 2008. X-ray structure of 4,4′- dihydroxybenzophenone mimicking sterol substrate in the active site of sterol 14α-demethylase (CYP51). J. Biol. Chem. 283:15152-15159.
    • (2008) J. Biol. Chem , vol.283 , pp. 15152-15159
    • Eddine, A.N.1    von Kries, J.P.2    Podust, M.V.3    Warrier, T.4    Kaufmann, S.H.E.5    Podust, L.M.6
  • 12
    • 0000921783 scopus 로고
    • The spectrophotometric measurement of turbid suspensions of cytochromes associated with drug metabolism
    • C. F. Chignell ed, Appleton-Century-Crofts, New York, NY
    • Estabrook, R. W., J. A. Peterson, J. Baron, and A. G. Hildebrandt. 1972. The spectrophotometric measurement of turbid suspensions of cytochromes associated with drug metabolism, p. 303-350. In C. F. Chignell (ed.), Methods in pharmacology, vol. 2. Appleton-Century-Crofts, New York, NY.
    • (1972) Methods in pharmacology , vol.2 , pp. 303-350
    • Estabrook, R.W.1    Peterson, J.A.2    Baron, J.3    Hildebrandt, A.G.4
  • 13
    • 33745907251 scopus 로고    scopus 로고
    • CYP153A6, a soluble P450 oxygenase catalyzing terminal-alkane hydroxylation
    • Funhoff, E. G., U. Bauer, I. Garcia-Rubio, B. Witholt, and J. B. van Beilen. 2006. CYP153A6, a soluble P450 oxygenase catalyzing terminal-alkane hydroxylation. J. Bacteriol. 188:5220-5227.
    • (2006) J. Bacteriol , vol.188 , pp. 5220-5227
    • Funhoff, E.G.1    Bauer, U.2    Garcia-Rubio, I.3    Witholt, B.4    van Beilen, J.B.5
  • 14
    • 0035876976 scopus 로고    scopus 로고
    • Azole-antifungal binding to a novel cytochrome P450 from Mycobacterium tuberculosis: Implications for treatment of tuberculosis
    • Guardiola-Diaz, H. B., L.-A. Foster, D. Mushrush, and A. D. N. Vaz. 2001. Azole-antifungal binding to a novel cytochrome P450 from Mycobacterium tuberculosis: implications for treatment of tuberculosis. Biochem. Pharmacol. 61:1463-1470.
    • (2001) Biochem. Pharmacol , vol.61 , pp. 1463-1470
    • Guardiola-Diaz, H.B.1    Foster, L.-A.2    Mushrush, D.3    Vaz, A.D.N.4
  • 15
    • 0034669750 scopus 로고    scopus 로고
    • Bactericidal and inhibitory effects of azole antifungal compounds on Mycobacterium smegmatis
    • Jackson, C. J., D. C. Lamb, D. E. Kelly, and S. L. Kelly. 2000. Bactericidal and inhibitory effects of azole antifungal compounds on Mycobacterium smegmatis. FEMS Lett. 192:159-162.
    • (2000) FEMS Lett , vol.192 , pp. 159-162
    • Jackson, C.J.1    Lamb, D.C.2    Kelly, D.E.3    Kelly, S.L.4
  • 16
    • 0037423691 scopus 로고    scopus 로고
    • Conservation of CYP51 in mycobacteria; cloning and characterisation of sterol 14α-demethylase (CYP51) from Mycobacterium smegmatis
    • Jackson, C. J., D. C. Lamb, T. H. Marczylo, J. E. Parker, N. L. Manning, D. E. Kelly, and S. L. Kelly. 2003. Conservation of CYP51 in mycobacteria; cloning and characterisation of sterol 14α-demethylase (CYP51) from Mycobacterium smegmatis. Biochem. Biophys. Res. Commun. 301:558-563.
    • (2003) Biochem. Biophys. Res. Commun , vol.301 , pp. 558-563
    • Jackson, C.J.1    Lamb, D.C.2    Marczylo, T.H.3    Parker, J.E.4    Manning, N.L.5    Kelly, D.E.6    Kelly, S.L.7
  • 17
    • 0017794351 scopus 로고
    • Measurement of substrate and inhibitor binding to microsomal cytochrome P-450 by optical-difference spectroscopy
    • Jefcoate, C. R. 1978. Measurement of substrate and inhibitor binding to microsomal cytochrome P-450 by optical-difference spectroscopy. Methods Enzymol. 52:258-279.
    • (1978) Methods Enzymol , vol.52 , pp. 258-279
    • Jefcoate, C.R.1
  • 18
    • 0030572468 scopus 로고    scopus 로고
    • Randomised controlled trial of single BCG, repeated BCG, or combined BCG and killed Mycobacterium leprae vaccine for prevention of leprosy and tuberculosis in Malawi
    • Karonga Prevention Trial Group
    • Karonga Prevention Trial Group. 1996. Randomised controlled trial of single BCG, repeated BCG, or combined BCG and killed Mycobacterium leprae vaccine for prevention of leprosy and tuberculosis in Malawi. Lancet 348:17-24.
    • (1996) Lancet , vol.348 , pp. 17-24
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0031054924 scopus 로고    scopus 로고
    • The mutation T315A in Candida albicans sterol 14α-demethylase causes reduced enzyme activity and fluconazole resistance through reduced affinity
    • Lamb, D. C., D. E. Kelly, W. H. Schunck, A. Z. Shyadehi, M. Akhtar, D. J. Lowe, B. C. Baldwin, and S. L. Kelly. 1997. The mutation T315A in Candida albicans sterol 14α-demethylase causes reduced enzyme activity and fluconazole resistance through reduced affinity. J. Biol. Chem. 272:5682-5688.
    • (1997) J. Biol. Chem , vol.272 , pp. 5682-5688
    • Lamb, D.C.1    Kelly, D.E.2    Schunck, W.H.3    Shyadehi, A.Z.4    Akhtar, M.5    Lowe, D.J.6    Baldwin, B.C.7    Kelly, S.L.8
  • 22
    • 0033529315 scopus 로고    scopus 로고
    • Generationofacomplete,soluble, and catalytically active sterol 14 alpha-demethylase-reductase complex
    • Lamb, D. C., D. E. Kelly, K. Venkateswarlu, N. J. Manning, H. F. Bligh, W. H. Schunck, and S. L. Kelly. 1999. Generationofacomplete,soluble, and catalytically active sterol 14 alpha-demethylase-reductase complex. Biochemistry 38:8733-8738.
    • (1999) Biochemistry , vol.38 , pp. 8733-8738
    • Lamb, D.C.1    Kelly, D.E.2    Venkateswarlu, K.3    Manning, N.J.4    Bligh, H.F.5    Schunck, W.H.6    Kelly, S.L.7
  • 24
    • 0017402363 scopus 로고
    • Ionization dependence of camphor binding and spin conversion of the complex between cytochrome P-450 and camphor: Kinetic and static studies at sub-zero temperatures
    • Lange, R., G. Hui Bon Hoa, P. Debey, and I. C. Gunsalus. 1977. Ionization dependence of camphor binding and spin conversion of the complex between cytochrome P-450 and camphor: kinetic and static studies at sub-zero temperatures. Eur. J. Biochem. 77:479-485.
    • (1977) Eur. J. Biochem , vol.77 , pp. 479-485
    • Lange, R.1    Hui Bon Hoa, G.2    Debey, P.3    Gunsalus, I.C.4
  • 25
    • 0017766053 scopus 로고
    • The low-spin ↔ high-spin transition of camphor-bound cytochrome P-450: Effects of medium and temperature on equilibrium data
    • Lange, R., C. Bonfils, and P. Debey. 1977. The low-spin ↔ high-spin transition of camphor-bound cytochrome P-450: effects of medium and temperature on equilibrium data. Eur. J. Biochem. 79:623-628.
    • (1977) Eur. J. Biochem , vol.79 , pp. 623-628
    • Lange, R.1    Bonfils, C.2    Debey, P.3
  • 26
    • 33745832316 scopus 로고    scopus 로고
    • Biophysical characterization of the sterol demethylase P450 from Mycobacterium tuberculosis, its cognate ferredoxin and their interactions
    • McLean, K. J., A. J. Warman, H. E. Seward, K. R. Marshall, H. M. Girvan, M. R. Cheesman, M. R. Waterman, and A. W. Munro. 2006. Biophysical characterization of the sterol demethylase P450 from Mycobacterium tuberculosis, its cognate ferredoxin and their interactions. Biochemistry 45:8427-8443.
    • (2006) Biochemistry , vol.45 , pp. 8427-8443
    • McLean, K.J.1    Warman, A.J.2    Seward, H.E.3    Marshall, K.R.4    Girvan, H.M.5    Cheesman, M.R.6    Waterman, M.R.7    Munro, A.W.8
  • 27
    • 50449100139 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes
    • Omura, T., and R. Sato. 1964. The carbon monoxide-binding pigment of liver microsomes. J. Biol. Chem. 239:2379-2385.
    • (1964) J. Biol. Chem , vol.239 , pp. 2379-2385
    • Omura, T.1    Sato, R.2
  • 28
    • 41949110521 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis CYP130: Crystal structure, biophysical characterization, and interactions with antifungal azole drugs
    • Ouellet, H., L. M. Podust, and P. R. Ortiz de Montellano. 2008. Mycobacterium tuberculosis CYP130: crystal structure, biophysical characterization, and interactions with antifungal azole drugs. J. Biol. Chem. 283:5069-5080.
    • (2008) J. Biol. Chem , vol.283 , pp. 5069-5080
    • Ouellet, H.1    Podust, L.M.2    Ortiz de Montellano, P.R.3
  • 29
    • 54049121819 scopus 로고    scopus 로고
    • Differential azole antifungal efficacy contrasted using a yeast strain humanized for sterol 14α-demthylase at the homologous locus
    • Parker, J. E., M. Merkamm, N. J. Manning, D. Pompon, S. L. Kelly, and D. E. Kelly. 2008. Differential azole antifungal efficacy contrasted using a yeast strain humanized for sterol 14α-demthylase at the homologous locus. Antimicrob. Agents Chemother. 52:3597-3603.
    • (2008) Antimicrob. Agents Chemother , vol.52 , pp. 3597-3603
    • Parker, J.E.1    Merkamm, M.2    Manning, N.J.3    Pompon, D.4    Kelly, S.L.5    Kelly, D.E.6
  • 31
    • 0029982945 scopus 로고    scopus 로고
    • Renaud, J. P., D. R. Davydov, K. P. M. Heirwegh, D. Mansuy, and G. Hui Bon Hoa. 1996. Thermodynamic studies of substrate binding and spin transitions in human cytochrome P-450 3A4 expressed in yeast microsomes. Biochem. J. 319:675-681.
    • Renaud, J. P., D. R. Davydov, K. P. M. Heirwegh, D. Mansuy, and G. Hui Bon Hoa. 1996. Thermodynamic studies of substrate binding and spin transitions in human cytochrome P-450 3A4 expressed in yeast microsomes. Biochem. J. 319:675-681.
  • 32
    • 0029806798 scopus 로고    scopus 로고
    • Structural changes in cytochrome P-450cam effected by the binding of the enantiomers (1R)-camphor and (1S)-camphor
    • Schulze, H., G. Hui Bon Hoa, V. Helms, R. C. Wade, and C. Jung. 1996. Structural changes in cytochrome P-450cam effected by the binding of the enantiomers (1R)-camphor and (1S)-camphor. Biochemistry 35:14127-14138.
    • (1996) Biochemistry , vol.35 , pp. 14127-14138
    • Schulze, H.1    Hui Bon Hoa, G.2    Helms, V.3    Wade, R.C.4    Jung, C.5
  • 33
    • 44149098003 scopus 로고    scopus 로고
    • Expression of microsomal lanosterol 14α-demethylase (CYP51) in an engineered soluble monomeric form
    • Seliskar, M., R. Kosir, and D. Rozman. 2008. Expression of microsomal lanosterol 14α-demethylase (CYP51) in an engineered soluble monomeric form. Biochem. Biophys. Res. Commun. 371:855-859.
    • (2008) Biochem. Biophys. Res. Commun , vol.371 , pp. 855-859
    • Seliskar, M.1    Kosir, R.2    Rozman, D.3
  • 34
    • 0017170343 scopus 로고
    • Coupling of spin, substrate and redox equilibria in cytochrome P450
    • Sligar, S. G. 1976. Coupling of spin, substrate and redox equilibria in cytochrome P450. Biochemistry 15:5399-5406.
    • (1976) Biochemistry , vol.15 , pp. 5399-5406
    • Sligar, S.G.1
  • 35
    • 0034307605 scopus 로고    scopus 로고
    • The genome sequence of Mycobacterium tuberculosis reveals cytochromes P450 as novel anti-TB drug targets
    • Souter, A., K. J. McLean, W. E. Smith, and A. W. Munro. 2000. The genome sequence of Mycobacterium tuberculosis reveals cytochromes P450 as novel anti-TB drug targets. J. Chem. Technol. Biotechnol. 75:933-941.
    • (2000) J. Chem. Technol. Biotechnol , vol.75 , pp. 933-941
    • Souter, A.1    McLean, K.J.2    Smith, W.E.3    Munro, A.W.4
  • 36
    • 0034647399 scopus 로고    scopus 로고
    • Leprosy - global situation. In
    • World Health Organization
    • World Health Organization. 2000. Leprosy - global situation. In WHO Wkly. Epidemiol. Rec. 75:226-231.
    • (2000) WHO Wkly. Epidemiol. Rec , vol.75 , pp. 226-231
  • 37
    • 0029856855 scopus 로고    scopus 로고
    • Conformational change of cytochrome P450 1A2 induced by sodium chloride
    • Yun, C. H., M. Song, T. Ahn, and H. Kim. 1996. Conformational change of cytochrome P450 1A2 induced by sodium chloride. J. Biol. Chem. 49:31312-31316.
    • (1996) J. Biol. Chem , vol.49 , pp. 31312-31316
    • Yun, C.H.1    Song, M.2    Ahn, T.3    Kim, H.4
  • 38
    • 0032529219 scopus 로고    scopus 로고
    • Conformational change and activation of cytochrome P450 2B1 induced by salt and phospholipid
    • Yun, C. H., T. Ahn, and F. P. Guengerich. 1998. Conformational change and activation of cytochrome P450 2B1 induced by salt and phospholipid. Arch. Biochem. Biophys. 356:229-238.
    • (1998) Arch. Biochem. Biophys , vol.356 , pp. 229-238
    • Yun, C.H.1    Ahn, T.2    Guengerich, F.P.3


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