Novel Properties of P450s in Streptomyces coelicolor

REFERENCES

• Aojula H. S., Wilson M. T., Drake A. Characterization of haem disorder by circular dichroism. Biochem. J. 1986; 237: 613–616
   PubMed Web of Science ®Google Scholar
• Austin M. A., Izumikawa M., Bowman M. E., Udwary D. W., Ferrer J.-L., Moore B. S., Noel J.P. Crystal structure of a bacterial type III polyketide synthase and enzymatic control of reactive polyketide intermediates. J. Biol. Chem. 2004; 279: 45162–45174
   PubMed Web of Science ®Google Scholar
• Banci L., Bertini I., Rosato A., Sacchieri S. Solution structure of oxidized microsomal rabbit cytochrome b5. Factors determining the heterogenous binding of the heme. Eur. J. Biochem. 2000; 267: 755–766
   PubMedGoogle Scholar
• Barnes H. J. Heterologous expression of bovine cytochrome P450 17α-hydroxylase. Ph.D. dissertation. Graduate School of Biomedical Sciences, The University of Texas Southwestern Medical School. 150–157
   Google Scholar
• Bellamine A., Mangla A. T., Nes W. D., Waterman M. R. Characterization and catalytic properties of the sterol 14α-demethylase from Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. USA 1999; 96: 8937–8942
   PubMed Web of Science ®Google Scholar
• Chen S., Zhou D. Functional domains of aromatase cytochrome P450 inferred from comparative analysis of amino acid sequences and substantiated by site-directed mutagenesis experinment. J. Biol. Chem. 1992; 267: 22587–22594
   PubMed Web of Science ®Google Scholar
• Chun Y.-J., Shimada T., Sanchez-Ponce R., Martin M. V., Lei L., Zhao B., Kelly S. L., Waterman M. R., Lamb D. C., Guengerich F. P. Electron transport pathway for a streptomyces cytochrome P450: Cytochrome P450105D5-catalyzed fatty acid hydroxylation in Streptomyces coelicolor A3(2). J. Biol. Chem. 2007; 282: 17486–17500
   PubMed Web of Science ®Google Scholar
• Funa N., Funabashi, Yoshimura E., Horinouchi S. A novel quinine-forming monooxygenase family involved in modification of aromatic polyketides. J. Biol. Chem. 2005; 280: 14514–14523
   PubMed Web of Science ®Google Scholar
• Hasemann C. A., Jurumbail R. G., Boddupalli S. S., Peterson J. A., Deisenhofer J. Structure and function of cytochromes P450: A comparative analysis of three crystal structures. Structure 1995; 3: 41–62
   PubMed Web of Science ®Google Scholar
• Hatae T., Hara S., Yokoyama C., Yabuki T., Iuoue H., Ullrich V., Tanabe T. Site-directed mutagenesis of human prostacyclin synthase: Alteration of Cys 441 of the Cys-pocket, and Ghi 347 and Arg 350 of the EXXR motif. FEBS Lett. 1996; 389: 268–272
   PubMed Web of Science ®Google Scholar
• Hopwood D. A. Forty years of genetics in Streptomyces: From In Vitro through In Vitro to In Silico. Microbiology 1999; 145: 2183–2202
   PubMed Web of Science ®Google Scholar
• Izumikawa M., Shipley P. R., Hopke J. N., O'Hare T., Xiang L., Noel J. P., Moore B. S. Expression and characterization of the type III polypeptide synthase 1,3,6,8-tetrahydroxynaphthalene synthase from Streptomyces coelicolor A3(2). J. Ind. Microbiol. Tiotechmol. 2003; 30: 510–515
   PubMed Web of Science ®Google Scholar
• Keller R. M., Wuthrich K. Structural study of the heme crevice in cytochrome b5on individual assignments of the IH-NMR lines of the heme group and selected amino acid residues. Biochim. Biophys. Acta. 1980; 621: 204–217
   PubMed Web of Science ®Google Scholar
• Kieser T., Bibb M. J., Buttner M. J., Chater F., Hopwood D. A. Practical Streptomyces Genetic. The John Innes Foundation, NorwichU.K. 2000
   Google Scholar
• LaMar G. N., David N. L., Parish D. W., Smith K. M. Heme orientational disorder in reconstituted and native sperm whale myoglobin. Proton nuclear magnetic resonance characterizations of heme methyl deuterium labeling in the Met-cyano protein. J. Mol. Biol. 1983; 168: 887–896
   PubMed Web of Science ®Google Scholar
• Lamb D. C., Skang T., Song H.-H., Jackson C. J., Podust L. M., Waterman M. R., Kell D. B., Kelly D. E., Kelly S. L. The cytochrome P450 complement (CYPome) of Streptomyces coelicolor A3(2). J. Biol. Chem. 2002; 277: 24000–24005
   PubMed Web of Science ®Google Scholar
• Lamb D. C., Guengerich F. P., Kelly S. L., Waterman M. R. Exploiting Streptomyces coelicolor A3(2) P450s as a model for application in drug discovery. Expert Opin. Drug Metab. Toxicol. 2006; 2: 27–40
   PubMed Web of Science ®Google Scholar
• Leys D., Mowat C. G., McLean K. J., Richmond A., Chapman S. K., Wakin-Shaw M. D., Munro A. D. Aromatic structure of Mycobacterium tuberculosis CYP121 to 1.06Å reveals novel features of cytochrome P450. J. Biol. Chem. 2003; 278: 5141–5147
   PubMed Web of Science ®Google Scholar
• McLachlan S. J., LaMar G. N., Burns P. D., Smith K. M., Langry K. C. 1H-NMR assignments and the dynamics of interconversion of the isomeric forms of cytochrome b5in solution. Biochim. Biophys. Acta 1986; 874: 274–284
   PubMed Web of Science ®Google Scholar
• Martinis S. A., Atkins W. M., Slayton P. S., Poulos T. L. A conserved residue of cytochrome P450 is involved in heme-oxygen stability and activation. J. Am. Chem. Soc. 1989; 20: 9252–9253
   Web of Science ®Google Scholar
• Moczygemba C., Guidry J., Wittung-Stafshede P. Heme concentration affects holo-myoglobin folding and unfolding kinetics. FEBS Lett. 2000; 470: 203–206
   PubMed Web of Science ®Google Scholar
• Podust L. M., Kim Y., Arase M., Neely B. A., Beck B. J., Bach H., Sherman D. H., Lamb D. C., Kelly S. L., Waterman M. R. The 1.92-Å structure of Streptomyces coelicolor A3(2) CYP154C1. A new monooxygenase that functionalizes macrolide ring systems. J. Biol. Chem. 2003; 278: 12214–12221
   PubMed Web of Science ®Google Scholar
• Podust L. M., Bach H., Kim Y., Lamb D. C., Arase M., Sherman D. H., Kelly S. L., Waterman M. R. Comparison of the 1.85Å structure of CYP154A1 from Streptomyces coelicolor A3(2) with the closely related CYP154C1 and CYPs from antibiotic biosynthetic pathways. Prot. Sci. 2004; 13: 255–268
   PubMed Web of Science ®Google Scholar
• Rupasinghe S., Schuler M. A., Kagawa N., Yuan H., Lei L., Zhao B., Kelly S. L., Waterman M. R., Lamb D. C. The cytochrome P450 gene family CYP157 does not contain EXXR in the K-helix reducing the absolute conserved P450 residues to a single cysteine. FEBS Lett. 2006; 280: 6338–6342
   Google Scholar
• Shimizu T., Tateishi T., Hatano M., Fujii-Kuriyama Y. Probing the role of lysines and arginines in the catalytic function of cytochrome P450d by site-directed mutagenesis interaction with NADPH-cytochrome P450 reductase. J. Biol. Chem. 1991; 266: 3372–3375
   PubMed Web of Science ®Google Scholar
• Zhao B., Guengerich F. P., Bellamine A., Lamb D. C., Izumikawa M., Lei L., Podust L. M., Sundaramoorthy M., Kalaitzis J. A., Reddy L. M., Kelly S. L., Moore B. S., Stec D., Voehler M., Falck J. R., Shimada T., Waterman M. R. Binding of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450158A2. J. Biol. Chem. 2005a; 280: 11599–11607
   PubMed Web of Science ®Google Scholar
• Zhao B., Guengerich F. P., Voehler M., Waterman M. R. Role of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: A new mechanism of proton transfer. J. Biol. Chem. 2005b; 280: 42188–42197
   PubMed Web of Science ®Google Scholar
• Zhao B., Lamb D. C., Lei L., Kelly S. L., Yuan H., Hachey D. L., Waterman M. R. Different binding modes of two flaviolin substrate molecules in cytochrome P450 158A1 (CYP158A1) compared to CYP158A2. Biochemistry 2007, (In press).
   Web of Science ®Google Scholar