Substitution of lysine with glutamic acid at position 193 in bovine CYP11A1 significantly affects protein oligomerization and solubility but not enzymatic activity

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1814, Issue 1, 2011, Pages 126-131

  Janocha, Simon ^a   Bichet, Andreas ^a   Zöllner, Andy ^a   Bernhardt, Rita ^a  

^a SAARLAND UNIVERSITY   (Germany)

Author keywords

CYP11A1; Cytochrome P450; Heterologous expression; Oligomerization; Protein protein interaction; Site directed mutagenesis

Indexed keywords

AMINO ACID; CHOLESTEROL MONOOXYGENASE (SIDE CHAIN CLEAVING); GLUTAMIC ACID; LYSINE;

ARTICLE; BIOTECHNOLOGICAL PROCEDURES; COW; CRYSTALLIZATION; ENZYME ACTIVITY; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PURIFICATION; SOLUBILITY;

AMINO ACID SUBSTITUTION; ANIMALS; BIOCATALYSIS; BIOSENSING TECHNIQUES; CATALYTIC DOMAIN; CATTLE; CHOLESTEROL SIDE-CHAIN CLEAVAGE ENZYME; GLUTAMIC ACID; KINETICS; LYSINE; MODELS, MOLECULAR; MUTATION; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY; SOLUBILITY; SUBSTRATE SPECIFICITY;

BOVINAE; MAMMALIA;

EID: 78649450676     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2010.06.002     Document Type: Article

References (30)

1. C. Duport, R. Spagnoli, E. Degryse, and D. Pompon Self-sufficient biosynthesis of pregnenolone and progesterone in engineered yeast Nat. Biotechnol. 16 1998 186 189
2. S.B. Mahato, and S. Garai Advances in microbial steroid biotransformation Steroids 62 1997 332 345
3. H.C. Murray, D.H. Peterson, Oxygenation of steroids by Mucorales fungi, U.S. Patent 2602769 (1952) (Upjohn Co., Kalamazoo, Michigan, USA).
4. R. Bernhardt, and M.R. Waterman Cytochrome P450 and steroid hormone biosynthesis A. Sigel, H. Sigel, R.K.O. Sigel, The Ubiquitous Roles of Cytochrome P450 Proteins 2007 John Wiley & Sons, Ltd 361 396
5. A.V. Grinberg, F. Hannemann, B. Schiffler, J. Müller, U. Heinemann, and R. Bernhardt Adrenodoxin: structure, stability, and electron transfer properties Proteins 40 2000 590 612
6. M.J. Headlam, M.C. Wilce, and R.C. Tuckey The F-G loop region of cytochrome P450scc (CYP11A1) interacts with the phospholipid membrane Biochim. Biophys. Acta 1617 2004 96 108
7. F.P. Guengerich, E.M. Gillam, and T. Shimada New applications of bacterial systems to problems in toxicology Crit. Rev. Toxicol. 26 1996 551 583
8. I.A. Pikuleva Putative F-G loop is involved in association with the membrane in P450scc (P450 11A1) Mol. Cell. Endocrinol. 215 2004 161 164
9. J. Cosme, and E.F. Johnson Engineering microsomal cytochrome P450 2C5 to be a soluble, monomeric enzyme J. Biol. Chem. 275 2000 2545 2553
10. V.L. Chashchin, I.V. Turko, A.A. Akhrem, and S.A. Usanov Cross-linking studies of adrenocortical cytochrome P-450scc. Evidence for a covalent complex with adrenodoxin and localization of the adrenodoxin-binding domain Biochim. Biophys. Acta 828 1985 313 324
11. D. Schwarz, V. Krüger, A.A. Chernogolov, S.A. Usanov, and A. Stier Rotation of cytochrome P450SCC (CYP11A1) in proteoliposomes studied by delayed fluorescence depolarization Biochem. Biophys. Res. Commun. 195 1993 889 896
12. S.A. Usanov, S.E. Graham, G.I. Lepesheva, T.N. Azeva, N.V. Strushkevich, A.A. Gilep, R.W. Estabrook, and J.A. Peterson Probing the interaction of bovine cytochrome P450scc (CYP11A1) with adrenodoxin: evaluating site-directed mutations by molecular modeling Biochemistry 41 2002 8310 8320
13. K.L. Maxwell, A.K. Mittermaier, J.D. Forman-Kay, and A.R. Davidson A simple in vivo assay for increased protein solubility Protein Sci. 8 1999 1908 1911
14. F. Hannemann, C. Virus, and R. Bernhardt Design of an Escherichia coli system for whole cell mediated steroid synthesis and molecular evolution of steroid hydroxylases J. Biotechnol. 124 2006 172 181
15. H. Uhlmann, V. Beckert, D. Schwarz, and R. Bernhardt Expression of bovine adrenodoxin in E. coli and site-directed mutagenesis of (2Fe-2S) cluster ligands Biochem. Biophys. Res. Commun. 188 1992 1131 1138
16. Y. Sagara, A. Wada, Y. Takata, M.R. Waterman, K. Sekimizu, and T. Horiuchi Direct expression of adrenodoxin reductase in Escherichia coli and the functional characterization Biol. Pharm. Bull. 16 1993 627 630 (Pubitemid 23275905)
17. T. Kimura C.K. Jorgensen, J.B. Neilands, R.S. Nyholm, D. Reinen, R.J.P. Williams, Structure and Bonding Vol. 5 1968 Springer-Verlag Berlin 1 40
18. A. Hiwatashi, Y. Ichikawa, N. Maruya, T. Yamano, and K. Aki Properties of crystalline reduced nicotinamide adenine dinucleotide phosphate-adrenodoxin reductase from bovine adrenocortical mitochonria. I. Physicochemical properties of holo- and apo-NADPH-adrenodoxin reductase and interaction between non-heme iron proteins and the reductase Biochemistry 15 1976 3082 3090
19. T. Omura, and R. Sato The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature J. Biol. Chem. 239 1964 2370 2378
20. K. Nishihara, M. Kanemori, M. Kitagawa, H. Yanagi, and T. Yura Chaperone coexpression plasmids: differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli Appl. Environ. Microbiol. 64 1998 1694 1699
21. S. Sugano, N. Morishima, H. Ikeda, and S. Horie Sensitive assay of cytochrome-P450scc activity by high-performance liquid-chromatography Anal. Biochem. 182 1989 327 333
22. A. Slominski, J. Zjawiony, J. Wortsman, I. Semak, J. Stewart, A. Pisarchik, T. Sweatman, J. Marcos, C. Dunbar, and R. Tuckey A novel pathway for sequential transformation of 7-dehydrocholesterol and expression of the P450scc system in mammalian skin Eur. J. Biochem. 271 2004 4178 4188
23. A. Zöllner, M.A. Pasquinelli, R. Bernhardt, and D.N. Beratan Protein phosphorylation and intermolecular electron transfer: a joint experimental and computational study of a hormone biosynthesis pathway J. Am. Chem. Soc. 129 2007 4206 4216
24. E.C. Müller, A. Lapko, A. Otto, J.J. Müller, K. Ruckpaul, and U. Heinemann Covalently crosslinked complexes of bovine adrenodoxin with adrenodoxin reductase and cytochrome P450scc. Mass spectrometry and Edman degradation of complexes of the steroidogenic hydroxylase system Eur. J. Biochem. 268 2001 1837 1843
25. A. Wada, and M.R. Waterman Identification by site-directed mutagenesis of two lysine residues in cholesterol side chain cleavage cytochrome P450 that are essential for adrenodoxin binding J. Biol. Chem. 267 1992 22877 22882
26. S.T. Woods, J. Sadleir, T. Downs, T. Triantopoulos, M.J. Headlam, and R.C. Tuckey Expression of catalytically active human cytochrome p450scc in Escherichia coli and mutagenesis of isoleucine-462 Arch. Biochem. Biophys. 353 1998 109 115
27. A. Wada, P.A. Mathew, H.J. Barnes, D. Sanders, R.W. Estabrook, and M.R. Waterman Expression of functional bovine cholesterol side chain cleavage cytochrome P450 (P450scc) in Escherichia coli Arch. Biochem. Biophys. 290 1991 376 380
28. R. Bernhardt Cytochromes P450 as versatile biocatalysts J. Biotechnol. 124 2006 128 145
29. A. Glieder, E.T. Farinas, and F.H. Arnold Laboratory evolution of a soluble, self-sufficient, highly active alkane hydroxylase Nat. Biotechnol. 20 2002 1135 1139
30. W. Humphrey, A. Dalke, and K. Schulten VMD - visual molecular dynamics J. Mol. Graph. 14 1996 33 38