참고문헌
- Burg, R.W., Miller, B.M., Baker, E.E., Birnbaum, J., Currie, S.A., Hartman, R., Kong, Y.L., Monaghan, R.L., Olson, G., Putter, I., et al. (1979). Avermectins, new family of potent anthelmintic agents: producing organism and fermentation. Antimicrob. Agents Chemother. 15, 361-367. https://doi.org/10.1128/AAC.15.3.361
- Choi, S., Han, S., Lee, H., Chun, Y.J., and Kim, D. (2013). Evaluation of Luminescent P450 analysis for directed evolution of human CYP4A11. Biomol. Ther. 21, 487-492. https://doi.org/10.4062/biomolther.2013.086
- Durairaj, P., Malla, S., Nadarajan, S.P., Lee, P.G., Jung, E., Park, H.H., Kim, B.G., and Yun, H. (2015). Fungal cytochrome P450 monooxygenases of Fusarium oxysporum for the synthesis of omega-hydroxy fatty acids in engineered Saccharomyces cerevisiae. Microb Cell Fact 14, 45. https://doi.org/10.1186/s12934-015-0228-2
- Dyson, P. (2011). Streptomyces: Molecular Biology and Biotechnology (Norfolk, UK, Caister Academic Press).
- Emsley, P., and Cowtan, K. (2004). Coot: model-building tools for molecular graphics. Acta Crystallogr. D. Biol. Crystallogr. 60, 2126-2132. https://doi.org/10.1107/S0907444904019158
- Han, S., Pham, T.V., Kim, J.H., Lim, Y.R., Park, H.G., Cha, G.S., Yun, C.H., Chun, Y.J., Kang, L.W., and Kim, D. (2015). Functional characterization of CYP107W1 from Streptomyces avermitilis and biosynthesis of macrolide oligomycin A. Arch. Biochem. Biophys. 575, 1-7. https://doi.org/10.1016/j.abb.2015.03.025
- Ikeda, H., Nonomiya, T., Usami, M., Ohta, T., and Omura, S. (1999). Organization of the biosynthetic gene cluster for the polyketide anthelmintic macrolide avermectin in Streptomyces avermitilis. Proc. Natl. Acad. Sci. USA 96, 9509-9514. https://doi.org/10.1073/pnas.96.17.9509
- Kelly, S.L., Kelly, D.E., Jackson, C.J., Warrilow, A.G.S., and Lamb, D.C. (2005). The diversity and importance of microbial cytochrome P450. In cytochrome P450: structure, mechanism, and biochemistry, P.R. Ortiz de Montellano, ed. (New York, Plenum Press), pp. 585-617.
- Kim, D., Cha, G.S., Nagy, L.D., Yun, C.H., and Guengerich, F.P. (2014). Kinetic analysis of lauric acid hydroxylation by human cytochrome P450 4A11. Biochemistry 53, 6161-6172. https://doi.org/10.1021/bi500710e
- Lamb, D.C., Zhao, B., Guengerich, F.P., Kelly, S.L., and Waterman, M.R. (2011). Genomics of Streptomyces cytochrome P450. In streptomyces molecular biology and biotechnology, P. Dyson, ed. (Norfolk, UK, Caister Academic Press), pp. 233-253.
- Lee, H., Kim, J.H., Han, S., Lim, Y.R., Park, H.G., Chun, Y.J., Park, S.W., and Kim, D. (2014). Directed-evolution analysis of human cytochrome P450 2A6 for enhanced enzymatic catalysis. J. Toxicol. Environ. Health A 77, 1409-1418. https://doi.org/10.1080/15287394.2014.951757
- Li, S., Tietz, D.R., Rutaganira, F.U., Kells, P.M., Anzai, Y., Kato, F., Pochapsky, T.C., Sherman, D.H., and Podust, L.M. (2012). Substrate recognition by the multifunctional cytochrome P450 MycG in mycinamicin hydroxylation and epoxidation reactions. J. Biol. Chem. 287, 37880-37890. https://doi.org/10.1074/jbc.M112.410340
- Lim, Y.R., Hong, M.K., Kim, J.K., Doan, T.T., Kim, D.H., Yun, C.H., Chun, Y.J., Kang, L.W., and Kim, D. (2012). Crystal structure of cytochrome P450 CYP105N1 from Streptomyces coelicolor, an oxidase in the coelibactin siderophore biosynthetic pathway. Arch. Biochem. Biophys. 528, 111-117. https://doi.org/10.1016/j.abb.2012.09.001
- Min, H., Kawasaki, I., Gong, J., and Shim, Y.H. (2015). Caffeine induces high expression of cyp-35A family genes and inhibits the early larval development in Caenorhabditis elegans. Mol. Cells 38, 236-242. https://doi.org/10.14348/molcells.2015.2282
- Otwinowski, Z., and Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326. https://doi.org/10.1016/S0076-6879(97)76066-X
- Schenkman, J.B., Remmer, H., and Estabrook, R.W. (1967). Spectral studies of drug interaction with hepatic microsomal cytochrome P-450. Mol. Pharmacol. 3, 113-123.
- Schrodinger, L. (2010). The PyMOL Molecular Graphics System, Version 1.3r1.
- Schuttelkopf, A.W., and van Aalten, D.M. (2004). PRODRG: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr. D. Biol. Crystallogr. 60, 1355-1363. https://doi.org/10.1107/S0907444904011679
- Symersky, J., Osowski, D., Walters, D.E., and Mueller, D.M. (2012). Oligomycin frames a common drug-binding site in the ATP synthase. Proc. Natl. Acad. Sci. USA 109, 13961-13965. https://doi.org/10.1073/pnas.1207912109
- Vagin, A., and Teplyakov, A. (1997). MOLREP: an Automated Program for Molecular Replacement. J. Appl. Cryst. 30, 1022-1025. https://doi.org/10.1107/S0021889897006766
- Xu, L.H., Fushinobu, S., Ikeda, H., Wakagi, T., and Shoun, H. (2009). Crystal structures of cytochrome P450 105P1 from Streptomyces avermitilis: conformational flexibility and histidine ligation state. J. Bacteriol. 191, 1211-1219. https://doi.org/10.1128/JB.01276-08
- Xu, L.H., Fushinobu, S., Takamatsu, S., Wakagi, T., Ikeda, H., and Shoun, H. (2010). Regio- and stereospecificity of filipin hydroxylation sites revealed by crystal structures of cytochrome P450 105P1 and 105D6 from Streptomyces avermitilis. J. Biol. Chem. 285, 16844-16853. https://doi.org/10.1074/jbc.M109.092460
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