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Volumn 280, Issue 13, 2013, Pages 3094-3108

Double site saturation mutagenesis of the human cytochrome P450 2D6 results in regioselective steroid hydroxylation

Author keywords

biocatalysis; high throughput Pichia transformation; MuteinDB; Pichia pastoris; protein engineering; regioselectivity; steroid hydroxylation; testosterone; whole cell biotransformation

Indexed keywords

6BETA HYDROXYTESTOSTERONE; CYTOCHROME P450 2D6; STEROID MONOOXYGENASE; TESTOSTERONE; TESTOSTERONE DERIVATIVE; TESTOSTERONE HYDROXYLASE; UNCLASSIFIED DRUG;

EID: 84879198581     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12270     Document Type: Conference Paper
Times cited : (20)

References (37)
  • 2
    • 0034973773 scopus 로고    scopus 로고
    • Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity
    • Guengerich F, (2001) Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity. Chem Res Toxicol 14, 611-650. (Pubitemid 32565712)
    • (2001) Chemical Research in Toxicology , vol.14 , Issue.6 , pp. 611-650
    • Guengerich, F.P.1
  • 3
    • 33745652737 scopus 로고    scopus 로고
    • Cytochrome P450 monooxygenases: perspectives for synthetic application
    • DOI 10.1016/j.tibtech.2006.05.002, PII S0167779906001259
    • Urlacher VB, &, Eiben S, (2006) Cytochrome P450 monooxygenases: perspectives for synthetic application. Trends Biotechnol 24, 324-330. (Pubitemid 43975576)
    • (2006) Trends in Biotechnology , vol.24 , Issue.7 , pp. 324-330
    • Urlacher, V.B.1    Eiben, S.2
  • 4
    • 34547690799 scopus 로고    scopus 로고
    • Extending the capabilities of nature's most versatile catalysts: Directed evolution of mammalian xenobiotic-metabolizing P450s
    • DOI 10.1016/j.abb.2007.04.033, PII S0003986107002366
    • Gillam EMJ, (2007) Extending the capabilities of nature's most versatile catalysts: directed evolution of mammalian xenobiotic-metabolizing P450s. Arch Biochem Biophys 464, 176-186. (Pubitemid 47210934)
    • (2007) Archives of Biochemistry and Biophysics , vol.464 , Issue.2 , pp. 176-186
    • Gillam, E.M.J.1
  • 6
    • 70350044889 scopus 로고    scopus 로고
    • New insights into the structural characteristics and functional relevance of the human cytochrome P450 2D6 enzyme
    • Wang B, Yang L, Zhang X, Huang S, Bartlam M, &, Zhou S, (2009) New insights into the structural characteristics and functional relevance of the human cytochrome P450 2D6 enzyme. Drug Metab Rev 41, 573-643.
    • (2009) Drug Metab Rev , vol.41 , pp. 573-643
    • Wang, B.1    Yang, L.2    Zhang, X.3    Huang, S.4    Bartlam, M.5    Zhou, S.6
  • 7
    • 0742286803 scopus 로고    scopus 로고
    • Cytochrome P450 2D6: Overview and update on pharmacology, genetics, biochemistry
    • DOI 10.1007/s00210-003-0832-2
    • Zanger UM, Raimundo S, &, Eichelbaum M, (2004) Cytochrome P450 2D6: overview and update on pharmacology, genetics, biochemistry. Naunyn Schmiedebergs Arch Pharmacol 369, 23-37. (Pubitemid 38161221)
    • (2004) Naunyn-Schmiedeberg's Archives of Pharmacology , vol.369 , Issue.1 , pp. 23-37
    • Zanger, U.M.1    Raimundo, S.2    Eichelbaum, M.3
  • 8
    • 0034962557 scopus 로고    scopus 로고
    • Pharmacophore and three-dimensional quantitative structure activity relationship methods for modeling cytochrome p450 active sites
    • Ekins S, de Groot MJ, &, Jones JP, (2001) Pharmacophore and three-dimensional quantitative structure activity relationship methods for modeling cytochrome p450 active sites. Drug Metab Dispos 29, 936-944. (Pubitemid 32605906)
    • (2001) Drug Metabolism and Disposition , vol.29 , Issue.7 , pp. 936-944
    • Ekins, S.1    De Groot, M.J.2    Jones, J.P.3
  • 9
    • 0034869539 scopus 로고    scopus 로고
    • Progesterone oxidation by cytochrome P450 2D isoforms in the brain
    • DOI 10.1210/en.142.9.3901
    • Hiroi T, Kishimoto W, Chow T, Imaoka S, Igarashi T, &, Funae Y, (2001) Progesterone oxidation by cytochrome P450 2D isoforms in the brain. Endocrinology 142, 3901-3908. (Pubitemid 32802662)
    • (2001) Endocrinology , vol.142 , Issue.9 , pp. 3901-3908
    • Hiroi, T.1    Kishimoto, W.2    Chow, T.3    Imaoka, S.4    Igarashi, T.5    Funae, Y.6
  • 12
    • 34047138077 scopus 로고    scopus 로고
    • Better library design: Data-driven protein engineering
    • DOI 10.1002/biot.200600170
    • Chaparro-Riggers JF, Polizzi KM, &, Bommarius AS, (2007) Better library design: data-driven protein engineering. Biotechnol J 2, 180-191. (Pubitemid 46738870)
    • (2007) Biotechnology Journal , vol.2 , Issue.2 , pp. 180-191
    • Chaparro-Riggers, J.F.1    Polizzi, K.M.2    Bommarius, A.S.3
  • 13
    • 0032080291 scopus 로고    scopus 로고
    • Determinants of the substrate specificity of human cytochrome P-450 CYP2D6: Design and construction of a mutant with testosterone hydroxylase activity
    • Smith G, Modi S, Pillai I, Lian LY, Sutcliffe MJ, Pritchard MP, Friedberg T, Roberts GC, &, Wolf CR, (1998) Determinants of the substrate specificity of human cytochrome P-450 CYP2D6: design and construction of a mutant with testosterone hydroxylase activity. Biochem J 331, 783-792. (Pubitemid 28211900)
    • (1998) Biochemical Journal , vol.331 , Issue.3 , pp. 783-792
    • Smith, G.1    Modi, S.2    Pillai, I.3    Lian, L.-Y.4    Sutcliffe, M.J.5    Pritchard, M.P.6    Friedberg, T.7    Roberts, G.C.K.8    Wolf, C.R.9
  • 14
    • 0037423276 scopus 로고    scopus 로고
    • Residues glutamate 216 and aspartate 301 are key determinants of substrate specificity and product regioselectivity in cytochrome P450 2D6
    • DOI 10.1074/jbc.M209519200
    • Paine MJI, McLaughlin L, Flanagan JU, Kemp C, Sutcliffe MJ, Roberts GCK, &, Wolf CR, (2003) Residues glutamate 216 and aspartate 301 are key determinants of substrate specificity and product regioselectivity in cytochrome P450 2D6. J Biol Chem 278, 4021-4027. (Pubitemid 36801135)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.6 , pp. 4021-4027
    • Paine, M.J.I.1    McLaughlin, L.A.2    Flanagan, J.U.3    Kemp, C.A.4    Sutcliffe, M.J.5    Roberts, G.C.K.6    Wolf, C.R.7
  • 15
    • 84868633712 scopus 로고    scopus 로고
    • Production of human cytochrome P450 2D6 drug metabolites with recombinant microbes - A comparative study
    • Geier M, Braun A, Emmerstorfer A, Pichler H, &, Glieder A, (2012) Production of human cytochrome P450 2D6 drug metabolites with recombinant microbes-a comparative study. Biotechnol J 7, 1346-1358.
    • (2012) Biotechnol J , vol.7 , pp. 1346-1358
    • Geier, M.1    Braun, A.2    Emmerstorfer, A.3    Pichler, H.4    Glieder, A.5
  • 16
    • 0037432069 scopus 로고    scopus 로고
    • Role of glutamic acid 216 in cytochrome P450 2D6 substrate binding and catalysis
    • DOI 10.1021/bi027085w
    • Guengerich FP, Hanna IH, Martin MV, &, Gillam EMJ, (2003) Role of glutamic acid 216 in cytochrome P450 2D6 substrate binding and catalysis. Biochemistry 42, 1245-1253. (Pubitemid 36184065)
    • (2003) Biochemistry , vol.42 , Issue.5 , pp. 1245-1253
    • Guengerich, F.P.1    Hanna, I.H.2    Martin, M.V.3    Gillama, E.M.J.4
  • 18
    • 77949832008 scopus 로고    scopus 로고
    • Towards preparative scale steroid hydroxylation with cytochrome P450 monooxygenase CYP106A2
    • Zehentgruber D, Hannemann F, Bleif S, Bernhardt R, &, Lütz S, (2010) Towards preparative scale steroid hydroxylation with cytochrome P450 monooxygenase CYP106A2. ChemBioChem 11, 713-721.
    • (2010) ChemBioChem , vol.11 , pp. 713-721
    • Zehentgruber, D.1    Hannemann, F.2    Bleif, S.3    Bernhardt, R.4    Lütz, S.5
  • 19
    • 77950457805 scopus 로고    scopus 로고
    • Challenges of steroid biotransformation with human cytochrome P450 monooxygenase CYP21 using resting cells of recombinant Schizosaccharomyces pombe
    • Zehentgruber D, Drǎgan C-A, Bureik M, &, Lütz S, (2010) Challenges of steroid biotransformation with human cytochrome P450 monooxygenase CYP21 using resting cells of recombinant Schizosaccharomyces pombe. J Biotechnol 146, 179-185.
    • (2010) J Biotechnol , vol.146 , pp. 179-185
    • Zehentgruber, D.1    Drǎgan, C.-A.2    Bureik, M.3    Lütz, S.4
  • 20
    • 78149432825 scopus 로고    scopus 로고
    • Laboratory evolution of stereoselective enzymes: A prolific source of catalysts for asymmetric reactions
    • Reetz M, (2011) Laboratory evolution of stereoselective enzymes: a prolific source of catalysts for asymmetric reactions. Angew Chem Int Ed 50, 138-174.
    • (2011) Angew Chem Int Ed , vol.50 , pp. 138-174
    • Reetz, M.1
  • 22
    • 0023929834 scopus 로고
    • Cytochrome P-450 steroid hormone metabolism catalyzed by human liver microsomes
    • Waxman D, Attisano C, Guengerich F, &, Lapenson D, (1988) Cytochrome P-450 steroid hormone metabolism catalyzed by human liver microsomes. Arch Biochem Biophys 263, 424-436.
    • (1988) Arch Biochem Biophys , vol.263 , pp. 424-436
    • Waxman, D.1    Attisano, C.2    Guengerich, F.3    Lapenson, D.4
  • 23
    • 84855938911 scopus 로고    scopus 로고
    • Heterologous expression of human cytochromes P450 2D6 and CYP3A4 in Escherichia coli and their functional characterization
    • Pan Y, Abd-Rashid BA, Ismail Z, Ismail R, Mak JW, &, Ong CE, (2011) Heterologous expression of human cytochromes P450 2D6 and CYP3A4 in Escherichia coli and their functional characterization. Protein J 30, 581-591.
    • (2011) Protein J , vol.30 , pp. 581-591
    • Pan, Y.1    Abd-Rashid, B.A.2    Ismail, Z.3    Ismail, R.4    Mak, J.W.5    Ong, C.E.6
  • 24
    • 77957162186 scopus 로고    scopus 로고
    • Molecular cloning, expression, and initial characterization of members of the CYP3A family in horses
    • Knych HKD, Mckemie DS, &, Stanley SD, (2010) Molecular cloning, expression, and initial characterization of members of the CYP3A family in horses. Pharmacology 38, 1820-1827.
    • (2010) Pharmacology , vol.38 , pp. 1820-1827
    • Knych, H.K.D.1    McKemie, D.S.2    Stanley, S.D.3
  • 28
    • 80052135332 scopus 로고    scopus 로고
    • Regio- and stereoselectivity of P450-catalysed hydroxylation of steroids controlled by laboratory evolution
    • Kille S, Zilly FE, Acevedo JP, &, Reetz MT, (2011) Regio- and stereoselectivity of P450-catalysed hydroxylation of steroids controlled by laboratory evolution. Nat Chem 3, 738-743.
    • (2011) Nat Chem , vol.3 , pp. 738-743
    • Kille, S.1    Zilly, F.E.2    Acevedo, J.P.3    Reetz, M.T.4
  • 29
    • 84863090270 scopus 로고    scopus 로고
    • Deletion of the Pichia pastoris KU70 homologue facilitates platform strain generation for gene expression and synthetic biology
    • Näätsaari L, Mistlberger B, Ruth C, Hajek T, Hartner FS, &, Glieder A, (2012) Deletion of the Pichia pastoris KU70 homologue facilitates platform strain generation for gene expression and synthetic biology. PLoS One 7, e39720.
    • (2012) PLoS One , vol.7
    • Näätsaari, L.1    Mistlberger, B.2    Ruth, C.3    Hajek, T.4    Hartner, F.S.5    Glieder, A.6
  • 30
    • 27744441015 scopus 로고    scopus 로고
    • Recombinant production of human microsomal cytochrome P450 2D6 in the methylotrophic yeast Pichia pastoris
    • DOI 10.1002/cbic.200500200
    • Dietrich M, Grundmann L, Kurr K, Valinotto L, Saussele T, Schmid RD, &, Lange S, (2005) Recombinant production of human microsomal cytochrome P450 2D6 in the methylotrophic yeast Pichia pastoris. ChemBioChem 6, 2014-2022. (Pubitemid 41598177)
    • (2005) ChemBioChem , vol.6 , Issue.11 , pp. 2014-2022
    • Dietrich, M.1    Grundmann, L.2    Kurr, K.3    Valinotto, L.4    Saussele, T.5    Schmid, R.D.6    Lange, S.7
  • 31
    • 12344321400 scopus 로고    scopus 로고
    • Condensed protocol for competent cell preparation and transformation of the methylotrophic yeast Pichia pastoris
    • Lin-Cereghino J, Wong WW, Xiong S, Giang W, Luong LT, Vu J, Johnson SD, &, Lin-Cereghino GP, (2005) Condensed protocol for competent cell preparation and transformation of the methylotrophic yeast Pichia pastoris. Biotechniques 38, 44-48. (Pubitemid 40139412)
    • (2005) BioTechniques , vol.38 , Issue.1 , pp. 44-48
    • Lin-Cereghino, J.1    Wong, W.W.2    Xiong, S.3    Giang, W.4    Luong, L.T.5    Vu, J.6    Johnson, S.D.7    Lin-Cereghino, G.P.8
  • 33
    • 5444226007 scopus 로고    scopus 로고
    • Reliable high-throughput screening with Pichia pastoris by limiting yeast cell death phenomena
    • DOI 10.1016/j.femsyr.2004.06.016, PII S1567135604001023
    • Weis R, Luiten R, Skranc W, Schwab H, Wubbolts M, &, Glieder A, (2004) Reliable high-throughput screening with Pichia pastoris by limiting yeast cell death phenomena. FEMS Yeast Res 5, 179-189. (Pubitemid 39360920)
    • (2004) FEMS Yeast Research , vol.5 , Issue.2 , pp. 179-189
    • Weis, R.1    Luiten, R.2    Skranc, W.3    Schwab, H.4    Wubbolts, M.5    Glieder, A.6
  • 34
    • 18644375497 scopus 로고    scopus 로고
    • Use of methylotropic yeast Pichia pastoris for expression of cytochromes P450
    • DOI 10.1016/S0076-6879(02)57691-6
    • Andersen MD, &, Møller BL, (2002) Use of methylotropic yeast Pichia pastoris for expression of cytochromes P450. Methods Enzymol 357, 333-342. (Pubitemid 35231369)
    • (2002) Methods in Enzymology , vol.357 , pp. 333-342
    • Andersen, M.D.1    Moller, B.L.2
  • 35
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • Omura T, &, Sato R, (1964) The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature. J Biol Chem 239, 2370-2378.
    • (1964) J Biol Chem , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 36
    • 77954293798 scopus 로고    scopus 로고
    • CPHmodels-3.0 - Remote homology modeling using structure-guided sequence profiles
    • Nielsen M, Lundegaard C, Lund O, &, Petersen TN, (2010) CPHmodels-3.0-remote homology modeling using structure-guided sequence profiles. Nucleic Acids Res 38, W576-W581.
    • (2010) Nucleic Acids Res , vol.38
    • Nielsen, M.1    Lundegaard, C.2    Lund, O.3    Petersen, T.N.4


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