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Volumn 361, Issue 4, 2007, Pages 876-882

Crystal structure of cytochrome P450 MoxA from Nonomuraea recticatena (CYP105)

Author keywords

Crystal structure; CYP105; Cytochrome P450; MoxA; Nonomuraea recticatena

Indexed keywords

CYTOCHROME P450; CYTOCHROME P450 MOXA; LUCIFERIN; NITRIC OXIDE; UNCLASSIFIED DRUG; WATER;

EID: 34547889572     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.07.062     Document Type: Article
Times cited : (33)

References (33)
  • 2
    • 0035984571 scopus 로고    scopus 로고
    • Oxidizing species in the mechanism of cytochrome P450
    • Ortiz de Montellano P.R., and De Voss J.J. 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
  • 3
    • 34547899465 scopus 로고    scopus 로고
    • A. Arisawa, A. Kumeda, World Patent WO2003/087381 (Oct. 23. 2003).
  • 5
    • 0024442346 scopus 로고
    • Purification and characterization of cytochrome P-450sca from Streptomyces carbophilus, ML-236B (compactin) induces a cytochrome P-450sca in Streptomyces carbophilus that hydroxylates ML-236B to pravastatin sodium (CS-514), a tissue-selective inhibitor of 3-hydroxy-3-methylglutaryl-coenzyme-A reductase
    • Matsuoka T., Miyakoshi S., Tanzawa K., Nakahara K., Hosobuchi M., and Serizawa N. Purification and characterization of cytochrome P-450sca from Streptomyces carbophilus, ML-236B (compactin) induces a cytochrome P-450sca in Streptomyces carbophilus that hydroxylates ML-236B to pravastatin sodium (CS-514), a tissue-selective inhibitor of 3-hydroxy-3-methylglutaryl-coenzyme-A reductase. Eur. J. Biochem. 184 (1989) 707-713
    • (1989) Eur. J. Biochem. , vol.184 , pp. 707-713
    • Matsuoka, T.1    Miyakoshi, S.2    Tanzawa, K.3    Nakahara, K.4    Hosobuchi, M.5    Serizawa, N.6
  • 8
    • 0022909196 scopus 로고
    • Induction of cytochrome P-450 in Streptomyces griseus by soybean flour
    • Sariaslani F.S., and Kunz D.A. Induction of cytochrome P-450 in Streptomyces griseus by soybean flour. Biochem. Biophys. Res. Commun. 141 (1986) 405-410
    • (1986) Biochem. Biophys. Res. Commun. , vol.141 , pp. 405-410
    • Sariaslani, F.S.1    Kunz, D.A.2
  • 9
    • 0033527407 scopus 로고    scopus 로고
    • Cytochrome P450105D1 (CYP105D1) from Streptomyces griseus: heterologous expression, activity, and activation effects of multiple xenobiotics
    • Taylor M., Lamb D.C., Cannell R., Dawson M., and Kelly S.L. Cytochrome P450105D1 (CYP105D1) from Streptomyces griseus: heterologous expression, activity, and activation effects of multiple xenobiotics. Biochem. Biophys. Res. Commun. 263 (1999) 838-842
    • (1999) Biochem. Biophys. Res. Commun. , vol.263 , pp. 838-842
    • Taylor, M.1    Lamb, D.C.2    Cannell, R.3    Dawson, M.4    Kelly, S.L.5
  • 10
    • 33749018513 scopus 로고    scopus 로고
    • Hydroxylation of oleanolic acid to queretaronic acid by cytochrome P450 from Nonomuraea recticatena
    • Fujii Y., Hirosue S., Fujii T., Matsumoto N., Agematsu H., and Arisawa A. Hydroxylation of oleanolic acid to queretaronic acid by cytochrome P450 from Nonomuraea recticatena. Biosci. Biotechnol. Biochem. 70 (2006) 2299-2302
    • (2006) Biosci. Biotechnol. Biochem. , vol.70 , pp. 2299-2302
    • Fujii, Y.1    Hirosue, S.2    Fujii, T.3    Matsumoto, N.4    Agematsu, H.5    Arisawa, A.6
  • 11
    • 0034256965 scopus 로고    scopus 로고
    • On the recognition of mammalian microsomal cytochrome P450 substrates and their characteristics: towards the prediction of human P450 substrate specificity and metabolism
    • Lewis D.F. On the recognition of mammalian microsomal cytochrome P450 substrates and their characteristics: towards the prediction of human P450 substrate specificity and metabolism. Biochem. Pharmacol. 60 (2000) 293-306
    • (2000) Biochem. Pharmacol. , vol.60 , pp. 293-306
    • Lewis, D.F.1
  • 12
    • 0025831899 scopus 로고
    • Occurrence and biological function of cytochrome P450 monooxygenases in the actinomycetes
    • O'Keefe D.P., and Harder P.A. Occurrence and biological function of cytochrome P450 monooxygenases in the actinomycetes. Mol. Microbiol. 5 (1991) 2099-2105
    • (1991) Mol. Microbiol. , vol.5 , pp. 2099-2105
    • O'Keefe, D.P.1    Harder, P.A.2
  • 13
    • 1842578348 scopus 로고    scopus 로고
    • A novel system for expressing recombinant proteins over a wide temperature range from 4 to 35 °C
    • Nakashima T., and Tamura T. A novel system for expressing recombinant proteins over a wide temperature range from 4 to 35 °C. Biotechnol. Bioeng. 86 (2004) 136-148
    • (2004) Biotechnol. Bioeng. , vol.86 , pp. 136-148
    • Nakashima, T.1    Tamura, T.2
  • 14
    • 4644233997 scopus 로고    scopus 로고
    • Isolation and characterization of a rolling-circle-type plasmid from Rhodococcus erythropolis and application of the plasmid to multiple-recombinant-protein expression
    • Nakashima T., and Tamura T. Isolation and characterization of a rolling-circle-type plasmid from Rhodococcus erythropolis and application of the plasmid to multiple-recombinant-protein expression. Appl. Environ. Microbiol. 780 (2004) 5557-5568
    • (2004) Appl. Environ. Microbiol. , vol.780 , pp. 5557-5568
    • Nakashima, T.1    Tamura, T.2
  • 15
    • 0028950304 scopus 로고
    • Degradation of the thiocarbamate herbicide EPTC (S-ethyl dipropylcarbamothioate) and biosafening by Rhodococcus sp. strain NI86/21 involve an inducible cytochrome P-450 system and aldehyde dehydrogenase
    • Nagy I., Schoofs G., Compernolle F., Proost P., Vanderleyden J., and De Mot R. Degradation of the thiocarbamate herbicide EPTC (S-ethyl dipropylcarbamothioate) and biosafening by Rhodococcus sp. strain NI86/21 involve an inducible cytochrome P-450 system and aldehyde dehydrogenase. J. Bacteriol. 177 (1995) 676-687
    • (1995) J. Bacteriol. , vol.177 , pp. 676-687
    • Nagy, I.1    Schoofs, G.2    Compernolle, F.3    Proost, P.4    Vanderleyden, J.5    De Mot, R.6
  • 16
    • 0003076963 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data
    • Leslie A.G.W. Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4/ESF-EACBM Newsl. Protein Crystallogr. 26 (1992)
    • (1992) Joint CCP4/ESF-EACBM Newsl. Protein Crystallogr. , vol.26
    • Leslie, A.G.W.1
  • 17
    • 0028103275 scopus 로고    scopus 로고
    • Collaborative Computational Project, The CCP4 suite: programs for protein crystallography, Acta Crystallogr. Sect. D Biol. Crystallogr. 50 (1994) 760-763.
  • 18
    • 84920325457 scopus 로고
    • AMoRe: an automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. J. Appl. Crystallogr. A 50 (1994) 157-163
    • (1994) J. Appl. Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 19
    • 0035800617 scopus 로고    scopus 로고
    • Ketoconazole-induced conformational changes in the active site of cytochrome P450eryF
    • Cupp-Vickery J.R., Garcia C., Hofacre A., and McGee-Estrada K. Ketoconazole-induced conformational changes in the active site of cytochrome P450eryF. J. Mol. Biol. 311 (2001) 101-110
    • (2001) J. Mol. Biol. , vol.311 , pp. 101-110
    • Cupp-Vickery, J.R.1    Garcia, C.2    Hofacre, A.3    McGee-Estrada, K.4
  • 20
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit-a versatile program for manipulating atomic coordinates and electron density
    • McRee D.E. XtalView/Xfit-a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125 (1999) 156-165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 23
    • 0034973773 scopus 로고    scopus 로고
    • Common and uncommon P450 reactions related to metabolism and chemical toxicity
    • Guegerich F.P. Common and uncommon P450 reactions related to metabolism and chemical toxicity. Chem. Res. Toxicol. 14 (2001) 611-650
    • (2001) Chem. Res. Toxicol. , vol.14 , pp. 611-650
    • Guegerich, F.P.1
  • 24
    • 4644355809 scopus 로고    scopus 로고
    • The architecture of metal coordination groups in proteins
    • Harding M.M. The architecture of metal coordination groups in proteins. Acta Crystallogr. Sect. D Biol. Crystallogr. 60 (2004) 849-859
    • (2004) Acta Crystallogr. Sect. D Biol. Crystallogr. , vol.60 , pp. 849-859
    • Harding, M.M.1
  • 25
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L., and Sander C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233 (1993) 123-138
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 27
    • 0034681370 scopus 로고    scopus 로고
    • Proton delivery in NO reduction by fungal nitric-oxide reductase: cryogenic crystallography, spectroscopy, and kinetics of ferric-NO complexes of wild-type and mutant enzymes
    • Shimizu H., Obayashi E., Gomi Y., Arakawa H., Park S.-Y., Nakamura H., Adachi S., Shoun H., and Shiro Y. Proton delivery in NO reduction by fungal nitric-oxide reductase: cryogenic crystallography, spectroscopy, and kinetics of ferric-NO complexes of wild-type and mutant enzymes. J. Biol. Chem. 275 (2000) 4816-4826
    • (2000) J. Biol. Chem. , vol.275 , pp. 4816-4826
    • Shimizu, H.1    Obayashi, E.2    Gomi, Y.3    Arakawa, H.4    Park, S.-Y.5    Nakamura, H.6    Adachi, S.7    Shoun, H.8    Shiro, Y.9
  • 28
    • 4143049187 scopus 로고    scopus 로고
    • Structural evidence for direct hydride transfer from NADH to cytochrome P450nor
    • Oshima R., Fushinobu S., Su F., Zhang L., Takaya N., and Shoun H. Structural evidence for direct hydride transfer from NADH to cytochrome P450nor. J. Mol. Biol. 342 (2004) 207-217
    • (2004) J. Mol. Biol. , vol.342 , pp. 207-217
    • Oshima, R.1    Fushinobu, S.2    Su, F.3    Zhang, L.4    Takaya, N.5    Shoun, H.6
  • 29
    • 33748750539 scopus 로고    scopus 로고
    • The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae
    • Sherman D.H., Li S., Yarmalitskaya L.V., Kim Y., Smith J.A., Waterman M.R., and Podust M.L. The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae. J. Biol. Chem. 281 (2006) 26289-26297
    • (2006) J. Biol. Chem. , vol.281 , pp. 26289-26297
    • Sherman, D.H.1    Li, S.2    Yarmalitskaya, L.V.3    Kim, Y.4    Smith, J.A.5    Waterman, M.R.6    Podust, M.L.7
  • 30
    • 1542364450 scopus 로고    scopus 로고
    • Structure of human microsomal cytochrome P450 2C8: evidence for a peripheral fatty acid binding site
    • Schoch G.A., Yano J.K., Wester M.R., Griffin K.J., Stout C.D., and Johnson E.F. Structure of human microsomal cytochrome P450 2C8: evidence for a peripheral fatty acid binding site. J. Biol. Chem. 279 (2004) 9497-9503
    • (2004) J. Biol. Chem. , vol.279 , pp. 9497-9503
    • Schoch, G.A.1    Yano, J.K.2    Wester, M.R.3    Griffin, K.J.4    Stout, C.D.5    Johnson, E.F.6
  • 31
    • 4644301430 scopus 로고    scopus 로고
    • The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05-Å resolution
    • Yano J.K., Wester M.R., Schoch G.A., Griffin K.J., Stout C.D., and Johnson E.F. The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05-Å resolution. J. Biol. Chem. 279 (2004) 38090-38091
    • (2004) J. Biol. Chem. , vol.279 , pp. 38090-38091
    • Yano, J.K.1    Wester, M.R.2    Schoch, G.A.3    Griffin, K.J.4    Stout, C.D.5    Johnson, E.F.6
  • 33
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. 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


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