Sequence modifications and heterologous expression of eukaryotic cytochromes P450 in Escherichia coli

Journal of Bioscience and Bioengineering

Volumn 120, Issue 3, 2015, Pages 268-274

  Ichinose, Hirofumi ^a   Hatakeyama, Mayumi ^a   Yamauchi, Yukiyo ^a  

^a KYUSHU UNIVERSITY   (Japan)

Author keywords

Chimerization; Escherichia coli; Eukaryotic cytochrome P450; Heterologous expression; N terminal domain; Sequence modification

Indexed keywords

AMINO ACIDS;

CHIMERIZATION; CYTOCHROME P450; HETEROLOGOUS EXPRESSION; N-TERMINAL DOMAINS; SEQUENCE MODIFICATION;

ESCHERICHIA COLI;

CYTOCHROME P450; CYTOCHROME P450 5037 EV2; CYTOCHROME P450 5139 D7V1; CYTOCHROME P450 5144 C1; CYTOCHROME P450 5147 A3; CYTOCHROME P450 5147 A4; CYTOCHROME P450 5152 A2; NUCLEOTIDE; PROLINE; UNCLASSIFIED DRUG; CHIMERIC PROTEIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CHEMICAL MODIFICATION; COMPARATIVE STUDY; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE AMPLIFICATION; GENETIC IDENTIFICATION; HETEROLOGOUS EXPRESSION; NONHUMAN; PROTEIN EXPRESSION; PROTEIN PROCESSING; SCREENING TEST; SEQUENCE ANALYSIS; BIOSYNTHESIS; CHEMISTRY; ENZYMOLOGY; FUNGUS; GENETICS; METABOLISM; PROTEIN TERTIARY STRUCTURE;

ESCHERICHIA COLI; EUKARYOTA;

CYTOCHROME P-450 ENZYME SYSTEM; ESCHERICHIA COLI; FUNGI; MUTANT CHIMERIC PROTEINS; PROTEIN STRUCTURE, TERTIARY;

EID: 84938293809     PISSN: 13891723     EISSN: 13474421     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2015.01.019     Document Type: Article

References (32)

1. Nelson D.R. A world of cytochrome P450s. Philos. Trans. R. Soc. Lond. B Biol. Sci. 2013, 368:20120430.
2. Ortiz de Montellano P.R. Cytochrome P450: Structure, mechanism, and biochemistry 2005, Kluwer Academic/Plenum Publishers, New York. 3rd ed.
3. Nelson D.R. The cytochrome p450 homepage. Hum. Genomics 2009, 4:59-65.
4. Kelly S.L., Kelly D.E. Microbial cytochromes P450: biodiversity and biotechnology. Where do cytochromes P450 come from, what do they do and what can they do for us?. Philos. Trans. R. Soc. Lond. B Biol. Sci. 2013, 368:20120476.
5. Hirosue S., Tazaki M., Hiratsuka N., Yanai S., Kabumoto H., Shinkyo R., Arisawa A., Sakaki T., Tsunekawa H., Johdo O., Ichinose H., Wariishi H. Insight into functional diversity of cytochrome P450 in the white-rot basidiomycete Phanerochaete chrysosporium: involvement of versatile monooxygenase. Biochem. Biophys. Res. Commun. 2011, 407:118-123.
6. Ide M., Ichinose H., Wariishi H. Molecular identification and functional characterization of cytochrome P450 monooxygenases from the brown-rot basidiomycete Postia placenta. Arch. Microbiol. 2012, 194:243-253.
7. Nazir K.H.M.N.H., Ichinose H., Wariishi H. Molecular characterization and isolation of cytochrome P450 genes from the filamentous fungus Aspergillus oryzae. Arch. Microbiol. 2010, 192:395-408.
8. Demain A.L., Fang A. The natural functions of secondary metabolites. Adv. Biochem. Eng. Biotechnol. 2000, 69:1-39.
9. Dixon R.A., Ferreira D. Genistein. Phytochemistry 2002, 60:205-211.
10. Bernhardt R. Cytochromes P450 as versatile biocatalysts. J. Biotechnol. 2006, 124:128-145.
11. Urlacher V.B., Eiben S. Cytochrome P450 monooxygenases: perspectives for synthetic application. Trends Biotechnol. 2006, 24:324-330.
12. Guengerich F.P. Cytochrome p450 enzymes in the generation of commercial products. Nat. Rev. Drug. Discov. 2002, 1:359-366.
13. Ro D.K., Paradise E.M., Ouellet M., Fisher K.J., Newman K.L., Ndungu J.M., Ho K.A., Eachus R.A., Ham T.S., Kirby J., other five authors Production of the antimalarial drug precursor artemisinic acid in engineered yeast. Nature 2006, 440:940-943.
14. Chang M.C.Y., Eachus R.A., Trieu W., Ro D.K., Keasling J.D. Engineering Escherichia coli for production of functionalized terpenoids using plant P450s. Nat. Chem. Biol. 2007, 3:274-277.
15. Barnes H.J., Arlotto M.P., Waterman M.R. Expression and enzymatic activity of recombinant cytochrome P450 17 alpha-hydroxylase in Escherichia coli. Proc. Natl. Acad. Sci. USA 1991, 88:5597-5601.
16. Cheng D., Kelley R.W., Cawley G.F., Backes W.L. High-level expression of recombinant rabbit cytochrome P450 2E1 in Escherichia coli C41 and its purification. Protein Expr. Purif. 2004, 33:66-71.
17. Yun C.H., Yim S.K., Kim D.H., Ahn T. Functional expression of human cytochrome P450 enzymes in Escherichia coli. Curr. Drug Metab. 2006, 7:411-429.
18. Ichinose H., Wariishi H. Heterologous expression and mechanistic investigation of a fungal cytochrome P450 (CYP5150A2): involvement of alternative redox partners. Arch. Biochem. Biophys. 2012, 518:8-15.
19. 2-terminal region on localization in cytosol and membranes. Proc. Natl. Acad. Sci. USA 1993, 90:2651-2655.
20. Shukla A., Huang W., Depaz I.M., Gillam E.M. Membrane integration of recombinant human P450 forms. Xenobiotica 2009, 39:495-507.
21. Ichinose H., Wariishi H. High-level heterologous expression of fungal cytochrome P450s in Escherichia coli. Biochem. Biophys. Res. Commun. 2013, 438:289-294.
22. Sohl C.D., Guengerich F.P. Kinetic analysis of the three-step steroid aromatase reaction of human cytochrome P450 19A1. J. Biol. Chem. 2010, 285:17734-17743.
23. Zelasko S., Palaria A., Das A. Optimizations to achieve high-level expression of cytochrome P450 proteins using Escherichia coli expression systems. Protein Expr. Purif. 2013, 92:77-87.
24. Omura T., Sato R. The carbon monoxide-binding pigment of liver microsomes, II. Solubilization, purification, and properties. J. Biol. Chem. 1964, 239:2379-2385.
25. Yamasaki T., Izumi S., Ide H., Ohyama Y. Identification of a novel rat microsomal vitamin D3 25-hydroxylase. J. Biol. Chem. 2004, 279:22848-22856.
26. McDougle D.R., Palaria A., Magnetta E., Meling D.D., Das A. Functional studies of N-terminally modified CYP2J2 epoxygenase in model lipid bilayers. Protein Sci. 2013, 22:964-979.
27. Kusano K., Sakaguchi M., Kagawa N., Waterman M.R., Omura T. Microsomal p450s use specific proline-rich sequences for efficient folding, but not for maintenance of the folded structure. J. Biochem. 2001, 129:259-269.
28. Kusano K., Kagawa N., Sakaguchi M., Omura T., Waterman M.R. Importance of a proline-rich sequence in the amino-terminal region for correct folding of mitochondrial and soluble microbial p450s. J. Biochem. 2001, 129:271-277.
29. Kemper B. Structural basis for the role in protein folding of conserved proline-rich regions in cytochromes P450. Toxicol. Appl. Pharmacol. 2004, 199:305-315.
30. Szczesna-Skorupa E., Straub P., Kemper B. Deletion of a conserved tetrapeptide, PPGP, in P450 2C2 results in loss of enzymatic activity without a change in its cellular location. Arch. Biochem. Biophys. 1993, 304:170-175.
31. Chen C.D., Kemper B. Different structural requirements at specific proline residue positions in the conserved proline-rich region of cytochrome P450 2C2. J. Biol. Chem. 1996, 271:28607-28611.
32. Chen C.D., Doray B., Kemper B. A conserved proline-rich sequence between the N-terminal signal-anchor and catalytic domains is required for assembly of functional cytochrome P450 2C2. Arch. Biochem. Biophys. 1998, 350:233-238.