Expression of microsomal lanosterol 14α-demethylase (CYP51) in an engineered soluble monomeric form

Biochemical and Biophysical Research Communications

Volumn 371, Issue 4, 2008, Pages 855-859

  Seliškar, Matej ^a   Košir, Rok ^a   Rozman, Damjana ^a  

^a UNIVERSITY OF LJUBLJANA   (Slovenia)

Author keywords

CYP51; Lanosterol 14 demethylase; Microsomal cytochrome P450; Monomeric; N terminus; Soluble form

Indexed keywords

MONOMER; OLIGOMER; STEROL 14ALPHA DEMETHYLASE;

ARTICLE; CONTROLLED STUDY; COW; CRYSTALLIZATION; ENGINEERING; ENZYME STRUCTURE; ESCHERICHIA COLI; GEL PERMEATION CHROMATOGRAPHY; MAMMAL; MEMBRANE; MICROSOME; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN MODIFICATION; PROTEIN PURIFICATION; PROTEIN VARIANT; SOLUBILITY;

AMINO ACID SEQUENCE; ANIMALS; CATTLE; CHROMATOGRAPHY, GEL; CRYSTALLIZATION; CYTOCHROME P-450 ENZYME SYSTEM; ESCHERICHIA COLI; HUMANS; KETOCONAZOLE; MOLECULAR SEQUENCE DATA; OXIDOREDUCTASES; PROTEIN ENGINEERING; RECOMBINANT PROTEINS; SOLUBILITY;

BOVINAE; ESCHERICHIA COLI; MAMMALIA;

EID: 44149098003     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.04.157     Document Type: Article

References (22)

1. Lepesheva G.I., and Waterman M.R. Sterol 14alpha-demethylase cytochrome P450 (CYP51), a P450 in all biological kingdoms. Biochim. Biophys. Acta 1770 (2007) 467-477
2. Waterman M.R., and Lepesheva G.I. Sterol 14 alpha-demethylase, an abundant and essential mixed-function oxidase. Biochem. Biophys. Res. Commun. 338 (2005) 418-422
3. Rozman D., Seliskar M., Cotman M., and Fink M. Pre-cholesterol precursors in gametogenesis. Mol. Cell. Endocrinol. 234 (2005) 47-56
4. Trosken E.R., Adamska M., Arand M., Zarn J.A., Patten C., Volkel W., and Lutz W.K. Comparison of lanosterol-14 alpha-demethylase (CYP51) of human and Candida albicans for inhibition by different antifungal azoles. Toxicology 228 (2006) 24-32
5. Korosec T., Acimovic J., Seliskar M., Kocjan D., Tacer K.F., Rozman D., and Urleb U. Novel cholesterol biosynthesis inhibitors targeting human lanosterol 14alpha-demethylase (CYP51). Bioorg. Med. Chem. 16 (2008) 209-221
6. Lamb D.C., Kelly D.E., Waterman M.R., Stromstedt M., Rozman D., and Kelly S.L. Characteristics of the heterologously expressed human lanosterol 14alpha-demethylase (other names: P45014DM, CYP51, P45051) and inhibition of the purified human and Candida albicans CYP51 with azole antifungal agents. Yeast 15 (1999) 755-763
7. Podust L.M., Poulos T.L., and Waterman M.R. Crystal structure of cytochrome P450 14alpha-sterol demethylase (CYP51) from Mycobacterium tuberculosis in complex with azole inhibitors. Proc. Natl. Acad. Sci. USA 98 (2001) 3068-3073
8. Cosme J., and Johnson E.F. Engineering microsomal cytochrome P450 2C5 to be a soluble, monomeric enzyme. Mutations that alter aggregation, phospholipid dependence of catalysis, and membrane binding. J. Biol. Chem. 275 (2000) 2545-2553
9. Johnson E.F., Wester M.R., and Stout C.D. The structure of microsomal cytochrome P450 2C5: a steroid and drug metabolizing enzyme. Endocr. Res. 28 (2002) 435-441
10. Chiang C.W., Yeh H.C., Wang L.H., and Chan N.L. Crystal structure of the human prostacyclin synthase. J. Mol. Biol. 364 (2006) 266-274
11. Debeljak N., Fink M., and Rozman D. Many facets of mammalian lanosterol 14alpha-demethylase from the evolutionarily conserved cytochrome P450 family CYP51. Arch. Biochem. Biophys. 409 (2003) 159-171
12. Lepesheva G.I., Podust L.M., Bellamine A., and Waterman M.R. Folding requirements are different between sterol 14alpha-demethylase (CYP51) from Mycobacterium tuberculosis and human or fungal orthologs. J. Biol. Chem. 276 (2001) 28413-28420
13. Wester M.R., Yano J.K., Schoch G.A., Yang C., Griffin K.J., Stout C.D., and Johnson E.F. The structure of human cytochrome P450 2C9 complexed with flurbiprofen at 2.0-A resolution. J. Biol. Chem. 279 (2004) 35630-35637
14. Lepesheva G.I., Virus C., and Waterman M.R. Conservation in the CYP51 family. Role of the B′ helix/BC loop and helices F and G in enzymatic function. Biochemistry 42 (2003) 9091-9101
15. Scott E.E., White M.A., He Y.A., Johnson E.F., Stout C.D., and Halpert J.R. Structure of mammalian cytochrome P450 2B4 complexed with 4-(4-chlorophenyl)imidazole at 1.9-A resolution: insight into the range of P450 conformations and the coordination of redox partner binding. J. Biol. Chem. 279 (2004) 27294-27301
16. Williams P.A., Cosme J., Sridhar V., Johnson E.F., and McRee D.E. Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity. Mol. Cell 5 (2000) 121-131
17. Lepesheva G.I., Nes W.D., Zhou W., Hill G.C., and Waterman M.R. CYP51 from Trypanosoma brucei is obtusifoliol-specific. Biochemistry 43 (2004) 10789-10799
18. Ji H., Zhang W., Zhang M., Kudo M., Aoyama Y., Yoshida Y., Sheng C., Song Y., Yang S., Zhou Y., Lu J., and Zhu J. Structure-based de novo design, synthesis, and biological evaluation of non-azole inhibitors specific for lanosterol 14alpha-demethylase of fungi. J. Med. Chem. 46 (2003) 474-485
19. Zhu J., Lu J., Zhou Y., Li Y., Cheng J., and Zheng C. Design, synthesis, and antifungal activities in vitro of novel tetrahydroisoquinoline compounds based on the structure of lanosterol 14alpha-demethylase (CYP51) of fungi. Bioorg. Med. Chem. Lett. 16 (2006) 5285-5289
20. Stromstedt M., Rozman D., and Waterman M.R. The ubiquitously expressed human CYP51 encodes lanosterol 14 alpha-demethylase, a cytochrome P450 whose expression is regulated by oxysterols. Arch. Biochem. Biophys. 329 (1996) 73-81
21. von Wachenfeldt C., Richardson T.H., Cosme J., and Johnson E.F. Microsomal P450 2C3 is expressed as a soluble dimer in Escherichia coli following modification of its N-terminus. Arch. Biochem. Biophys. 339 (1997) 107-114
22. Matsuura K., Yoshioka S., Tosha T., Hori H., Ishimori K., Kitagawa T., Morishima I., Kagawa N., and Waterman M.R. Structural diversities of active site in clinical azole-bound forms between sterol 14alpha-demethylases (CYP51s) from human and Mycobacterium tuberculosis. J. Biol. Chem. 280 (2005) 9088-9096