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Volumn 53, Issue 48, 2014, Pages 7531-7540

Epoxidation activities of human cytochromes P450c17 and P450c21

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CARBON; CHEMICAL BONDS; ENZYMES; HYDROXYLATION; OXYGEN;

EID: 84916211937     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi5011865     Document Type: Article
Times cited : (10)

References (34)
  • 1
    • 79951665862 scopus 로고    scopus 로고
    • The molecular biology, biochemistry, and physiology of human steroidogenesis and its disorders
    • Miller, W. L., and Auchus, R. J. (2011) The molecular biology, biochemistry, and physiology of human steroidogenesis and its disorders. Endocr. Rev. 32, 81-151.
    • (2011) Endocr. Rev. , vol.32 , pp. 81-151
    • Miller, W.L.1    Auchus, R.J.2
  • 2
    • 84866133140 scopus 로고    scopus 로고
    • Minor activities and transition state properties of the human steroid hydroxylases cytochromes P450c17 and P450c21, from reactions observed with deuterium-labeled substrates
    • Yoshimoto, F. K., Zhou, Y., Peng, H. M., Stidd, D., Yoshimoto, J. A., Sharma, K. K., Matthew, S., and Auchus, R. J. (2012) Minor activities and transition state properties of the human steroid hydroxylases cytochromes P450c17 and P450c21, from reactions observed with deuterium-labeled substrates. Biochemistry 51, 7064-7077.
    • (2012) Biochemistry , vol.51 , pp. 7064-7077
    • Yoshimoto, F.K.1    Zhou, Y.2    Peng, H.M.3    Stidd, D.4    Yoshimoto, J.A.5    Sharma, K.K.6    Matthew, S.7    Auchus, R.J.8
  • 3
    • 0027313314 scopus 로고
    • Progesterone 16 α-hydroxylase activity is catalyzed by human cytochrome P450 17α-hydroxylase
    • Swart, P., Swart, A. C., Waterman, M. R., Estabrook, R. W., and Mason, J. I. (1993) Progesterone 16 α-hydroxylase activity is catalyzed by human cytochrome P450 17α-hydroxylase. J. Clin. Endocrinol. Metab. 77, 98-102.
    • (1993) J. Clin. Endocrinol. Metab. , vol.77 , pp. 98-102
    • Swart, P.1    Swart, A.C.2    Waterman, M.R.3    Estabrook, R.W.4    Mason, J.I.5
  • 4
    • 77950244867 scopus 로고    scopus 로고
    • A single amino acid residue, Ala 105, confers 16α-hydroxylase activity to human cytochrome P450 17α-hydroxylase/17,20 lyase
    • Swart, A. C., Storbeck, K. H., and Swart, P. (2010) A single amino acid residue, Ala 105, confers 16α-hydroxylase activity to human cytochrome P450 17α-hydroxylase/17,20 lyase. J. Steroid Biochem. Mol. Biol. 119, 112-120.
    • (2010) J. Steroid Biochem. Mol. Biol. , vol.119 , pp. 112-120
    • Swart, A.C.1    Storbeck, K.H.2    Swart, P.3
  • 6
    • 0026564816 scopus 로고
    • Cytochrome P450: Progress and predictions
    • Coon, M. J., Ding, X. X., Pernecky, S. J., and Vaz, A. D. (1992) Cytochrome P450: progress and predictions. FASEB J. 6, 669-673.
    • (1992) FASEB J. , vol.6 , pp. 669-673
    • Coon, M.J.1    Ding, X.X.2    Pernecky, S.J.3    Vaz, A.D.4
  • 7
    • 0034973773 scopus 로고    scopus 로고
    • Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity
    • Guengerich, F. P. (2001) Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity. Chem. Res. Toxicol. 14, 611-650.
    • (2001) Chem. Res. Toxicol. , vol.14 , pp. 611-650
    • Guengerich, F.P.1
  • 9
    • 0029954699 scopus 로고    scopus 로고
    • The mechanism of the acyl-carbon bond cleavage reaction catalyzed by recombinant sterol 14 α-demethylase of Candida albicans (other names are: Lanosterol 14α-demethylase, P-45014DM, and CYP51)
    • Shyadehi, A. Z., Lamb, D. C., Kelly, S. L., Kelly, D. E., Schunck, W. H., Wright, J. N., Corina, D., and Akhtar, M. (1996) The mechanism of the acyl-carbon bond cleavage reaction catalyzed by recombinant sterol 14 α-demethylase of Candida albicans (other names are: lanosterol 14α-demethylase, P-45014DM, and CYP51). J. Biol. Chem. 271, 12445-12450.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12445-12450
    • Shyadehi, A.Z.1    Lamb, D.C.2    Kelly, S.L.3    Kelly, D.E.4    Schunck, W.H.5    Wright, J.N.6    Corina, D.7    Akhtar, M.8
  • 10
    • 79951833485 scopus 로고    scopus 로고
    • Genome mining in Streptomyces. Discovery of an unprecedented P450-catalyzed oxidative rearrangement that is the final step in the biosynthesis of pentalenolactone
    • Zhu, D., Seo, M. J., Ikeda, H., and Cane, D. E. (2011) Genome mining in Streptomyces. Discovery of an unprecedented P450-catalyzed oxidative rearrangement that is the final step in the biosynthesis of pentalenolactone. J. Am. Chem. Soc. 133, 2128-2131.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 2128-2131
    • Zhu, D.1    Seo, M.J.2    Ikeda, H.3    Cane, D.E.4
  • 11
    • 78049407027 scopus 로고    scopus 로고
    • Cyclization of a cellular dipentaenone by Streptomyces coelicolor cytochrome P450 154A1 without oxidation/reduction
    • Cheng, Q., Lamb, D. C., Kelly, S. L., Lei, L., and Guengerich, F. P. (2010) Cyclization of a cellular dipentaenone by Streptomyces coelicolor cytochrome P450 154A1 without oxidation/reduction. J. Am. Chem. Soc. 132 , 15173-15175.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 15173-15175
    • Cheng, Q.1    Lamb, D.C.2    Kelly, S.L.3    Lei, L.4    Guengerich, F.P.5
  • 12
    • 84872495336 scopus 로고    scopus 로고
    • Olefin cyclopropanation via carbene transfer catalyzed by engineered cytochrome P450 enzymes
    • Coelho, P. S., Brustad, E. M., Kannan, A., and Arnold, F. H. (2013) Olefin cyclopropanation via carbene transfer catalyzed by engineered cytochrome P450 enzymes. Science 339, 307-310.
    • (2013) Science , vol.339 , pp. 307-310
    • Coelho, P.S.1    Brustad, E.M.2    Kannan, A.3    Arnold, F.H.4
  • 13
    • 84902664223 scopus 로고    scopus 로고
    • Enantioselective imidation of sulfides via enzyme-catalyzed intermolecular nitrogen-atom transfer
    • Farwell, C. C., McIntosh, J. A., Hyster, T. K., Wang, Z. J., and Arnold, F. H. (2014) Enantioselective imidation of sulfides via enzyme-catalyzed intermolecular nitrogen-atom transfer. J. Am. Chem. Soc. 136, 8766-8771.
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 8766-8771
    • Farwell, C.C.1    McIntosh, J.A.2    Hyster, T.K.3    Wang, Z.J.4    Arnold, F.H.5
  • 14
    • 0032488666 scopus 로고    scopus 로고
    • 5 augments the 17,20 lyase activity of human P450c17 without direct electron transfer
    • 5 augments the 17,20 lyase activity of human P450c17 without direct electron transfer. J. Biol. Chem. 273, 3158-3165.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3158-3165
    • Auchus, R.J.1    Lee, T.C.2    Miller, W.L.3
  • 16
    • 82755187500 scopus 로고    scopus 로고
    • Synthesis of halogenated pregnanes, mechanistic probes of steroid hydroxylases CYP17A1 and CYP21A2
    • Yoshimoto, F. K., Desilets, M. C., and Auchus, R. J. (2012) Synthesis of halogenated pregnanes, mechanistic probes of steroid hydroxylases CYP17A1 and CYP21A2. J. Steroid Biochem. Mol. Biol. 128, 38-50.
    • (2012) J. Steroid Biochem. Mol. Biol. , vol.128 , pp. 38-50
    • Yoshimoto, F.K.1    Desilets, M.C.2    Auchus, R.J.3
  • 17
    • 77950233252 scopus 로고    scopus 로고
    • Human cytochrome P450c17: Single step purification and phosphorylation of serine 258 by protein kinase A
    • Wang, Y. H., Tee, M. K., and Miller, W. L. (2010) Human cytochrome P450c17: single step purification and phosphorylation of serine 258 by protein kinase A. Endocrinology 151, 1677-1684.
    • (2010) Endocrinology , vol.151 , pp. 1677-1684
    • Wang, Y.H.1    Tee, M.K.2    Miller, W.L.3
  • 18
    • 79959408522 scopus 로고    scopus 로고
    • High-yield expression of a catalytically active membrane-bound protein: Human P450 oxidoreductase
    • Sandee, D., and Miller, W. L. (2011) High-yield expression of a catalytically active membrane-bound protein: human P450 oxidoreductase. Endocrinology 152, 2904-2908.
    • (2011) Endocrinology , vol.152 , pp. 2904-2908
    • Sandee, D.1    Miller, W.L.2
  • 19
    • 33646030623 scopus 로고    scopus 로고
    • Purification and characterization of bovine steroid 21-hydroxylase (P450c21) efficiently expressed in Escherichia coli
    • Arase, M., Waterman, M. R., and Kagawa, N. (2006) Purification and characterization of bovine steroid 21-hydroxylase (P450c21) efficiently expressed in Escherichia coli. Biochem. Biophys. Res. Commun. 344, 400-405.
    • (2006) Biochem. Biophys. Res. Commun. , vol.344 , pp. 400-405
    • Arase, M.1    Waterman, M.R.2    Kagawa, N.3
  • 20
    • 1542782363 scopus 로고    scopus 로고
    • CYP17 mutation E305G causes isolated 17,20-lyase deficiency by selectively altering substrate binding
    • Sherbet, D. P., Tiosano, D., Kwist, K. M., Hochberg, Z., and Auchus, R. J. (2003) CYP17 mutation E305G causes isolated 17,20-lyase deficiency by selectively altering substrate binding. J. Biol. Chem. 278, 48563-48569.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48563-48569
    • Sherbet, D.P.1    Tiosano, D.2    Kwist, K.M.3    Hochberg, Z.4    Auchus, R.J.5
  • 21
    • 33749189648 scopus 로고    scopus 로고
    • Synthesis of some novel pregnane derivatives and its glycoside as possible anticancer agents
    • Pandey, A. K., Tiwari, V., Srivastava, S., and Sethi, A. (2006) Synthesis of some novel pregnane derivatives and its glycoside as possible anticancer agents. Ind. J. Heterocycl. Chem. 15, 353-358.
    • (2006) Ind. J. Heterocycl. Chem. , vol.15 , pp. 353-358
    • Pandey, A.K.1    Tiwari, V.2    Srivastava, S.3    Sethi, A.4
  • 22
    • 84858976886 scopus 로고    scopus 로고
    • A three-dimensional structure of steroid 21-hydroxylase (Cytochrome P450 21A2) with two substrates reveals locations of disease-associated variants
    • Zhao, B., Lei, L., Kagawa, N., Sundaramoorthy, M., Banerjee, S., Nagy, L. D., Guengerich, F. P., and Waterman, M. R. (2012) A three-dimensional structure of steroid 21-hydroxylase (Cytochrome P450 21A2) with two substrates reveals locations of disease-associated variants. J. Biol. Chem. 287, 10613-10622.
    • (2012) J. Biol. Chem. , vol.287 , pp. 10613-10622
    • Zhao, B.1    Lei, L.2    Kagawa, N.3    Sundaramoorthy, M.4    Banerjee, S.5    Nagy, L.D.6    Guengerich, F.P.7    Waterman, M.R.8
  • 24
    • 0037228101 scopus 로고    scopus 로고
    • The enantiomer of progesterone (ent-progesterone) is a competitive inhibitor of human cytochromes P450c17 and P450c21
    • Auchus, R. J., Kumar, A. S., Boswell, C. A., Gupta, M. K., Bruce, K., Rath, N. P., and Covey, D. F. (2003) The enantiomer of progesterone (ent-progesterone) is a competitive inhibitor of human cytochromes P450c17 and P450c21. Arch. Biochem. Biophys. 409, 134-144.
    • (2003) Arch. Biochem. Biophys. , vol.409 , pp. 134-144
    • Auchus, R.J.1    Kumar, A.S.2    Boswell, C.A.3    Gupta, M.K.4    Bruce, K.5    Rath, N.P.6    Covey, D.F.7
  • 25
    • 0032584090 scopus 로고    scopus 로고
    • Epoxidation of olefins by cytochrome P450: Evidence from site-specific mutagenesis for hydroperoxo-iron as an electrophilic oxidant
    • Vaz, A. D., McGinnity, D. F., and Coon, M. J. (1998) Epoxidation of olefins by cytochrome P450: evidence from site-specific mutagenesis for hydroperoxo-iron as an electrophilic oxidant. Proc. Natl. Acad. Sci. U. S. A. 95, 3555-3560.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 3555-3560
    • Vaz, A.D.1    McGinnity, D.F.2    Coon, M.J.3
  • 27
    • 0037009994 scopus 로고    scopus 로고
    • What factors affect the regioselectivity of oxidation by cytochrome P450? A DFT study of allylic hydroxylation and double bond epoxidation in a model reaction
    • de Visser, S. P., Ogliaro, F., Sharma, P. K., and Shaik, S. (2002) What factors affect the regioselectivity of oxidation by cytochrome P450? A DFT study of allylic hydroxylation and double bond epoxidation in a model reaction. J. Am. Chem. Soc. 124, 11809-11826.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11809-11826
    • De Visser, S.P.1    Ogliaro, F.2    Sharma, P.K.3    Shaik, S.4
  • 28
    • 0037139511 scopus 로고    scopus 로고
    • Searching for the second oxidant in the catalytic cycle of cytochrome P450: A theoretical investigation of the iron(III)-hydroperoxo species and its epoxidation pathways
    • Ogliaro, F., de Visser, S. P., Cohen, S., Sharma, P. K., and Shaik, S. (2002) Searching for the second oxidant in the catalytic cycle of cytochrome P450: a theoretical investigation of the iron(III)-hydroperoxo species and its epoxidation pathways. J. Am. Chem. Soc. 124, 2806-2817.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 2806-2817
    • Ogliaro, F.1    De Visser, S.P.2    Cohen, S.3    Sharma, P.K.4    Shaik, S.5
  • 29
    • 18444406884 scopus 로고    scopus 로고
    • Multistate reactivity in styrene epoxidation by compound I of cytochrome P450: Mechanisms of products and side products formation
    • Kumar, D., de Visser, S. P., and Shaik, S. (2005) Multistate reactivity in styrene epoxidation by compound I of cytochrome P450: mechanisms of products and side products formation. Chemistry 11, 2825-2835.
    • (2005) Chemistry , vol.11 , pp. 2825-2835
    • Kumar, D.1    De Visser, S.P.2    Shaik, S.3
  • 30
    • 0032430067 scopus 로고    scopus 로고
    • Multiple activated oxygen species in P450 catalysis: Contributions to specificity in drug metabolism
    • Coon, M. J., Vaz, A. D., McGinnity, D. F., and Peng, H. M. (1998) Multiple activated oxygen species in P450 catalysis: Contributions to specificity in drug metabolism. Drug Metab. Dispos. 26, 1190-1193.
    • (1998) Drug Metab. Dispos. , vol.26 , pp. 1190-1193
    • Coon, M.J.1    Vaz, A.D.2    McGinnity, D.F.3    Peng, H.M.4
  • 33
    • 0028325281 scopus 로고
    • Effect of the antiglucocorticoid RU486 on adrenal steroidogenic enzyme activity and steroidogenesis
    • Albertson, B. D., Hill, R. B., Sprague, K. A., Wood, K. E., Nieman, L. K., and Loriaux, D. L. (1994) Effect of the antiglucocorticoid RU486 on adrenal steroidogenic enzyme activity and steroidogenesis. Eur. J. Endocrinol. 130, 195-200.
    • (1994) Eur. J. Endocrinol. , vol.130 , pp. 195-200
    • Albertson, B.D.1    Hill, R.B.2    Sprague, K.A.3    Wood, K.E.4    Nieman, L.K.5    Loriaux, D.L.6


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