메뉴 건너뛰기




Volumn 110, Issue 11, 2013, Pages 2815-2825

Semi-rational engineering of cytochrome P450sca-2 in a hybrid system for enhanced catalytic activity: Insights into the important role of electron transfer

Author keywords

Cytochrome P450sca 2; Electron transfer; Iterative saturation mutagenesis; Pravastatin; Redox partner; Site directed saturation mutagenesis

Indexed keywords

BIOTRANSFORMATION PROCESS; ELECTRON TRANSFER; ENHANCED CATALYTIC ACTIVITY; KINETIC CHARACTERIZATION; PRAVASTATIN; REDOX PARTNERS; SATURATION MUTAGENESIS; WHOLE-CELL BIOTRANSFORMATIONS;

EID: 84884533513     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.24960     Document Type: Article
Times cited : (46)

References (74)
  • 2
    • 0029074117 scopus 로고
    • Active-site analysis of ferric P450 enzymes: Hydrogen-bonding effects on the circular dichroism spectra
    • Andersson LA, Peterson JA. 1995. Active-site analysis of ferric P450 enzymes: Hydrogen-bonding effects on the circular dichroism spectra. Biochem Biophys Res Commun 211(2):389-395.
    • (1995) Biochem Biophys Res Commun , vol.211 , Issue.2 , pp. 389-395
    • Andersson, L.A.1    Peterson, J.A.2
  • 4
    • 33744520321 scopus 로고    scopus 로고
    • Cytochromes P450 as versatile biocatalysts
    • Bernhardt R. 2006. Cytochromes P450 as versatile biocatalysts. J Biotechnol 124(1):128-145.
    • (2006) J Biotechnol , vol.124 , Issue.1 , pp. 128-145
    • Bernhardt, R.1
  • 5
    • 34047200917 scopus 로고    scopus 로고
    • A new application of the yeast two-hybrid system in protein engineering
    • Bichet A, Hannemann F, Rekowski M, Bernhardt R. 2007. A new application of the yeast two-hybrid system in protein engineering. Protein Eng Des Sel 20(3):117-123.
    • (2007) Protein Eng Des Sel , vol.20 , Issue.3 , pp. 117-123
    • Bichet, A.1    Hannemann, F.2    Rekowski, M.3    Bernhardt, R.4
  • 7
    • 34547118130 scopus 로고    scopus 로고
    • Electron transport pathway for a Streptomyces cytochrome P450: Cytochrome P450 105D5-catalyzed fatty acid hydroxylation in Streptomyces coelicolor A3 (2)
    • Chun YJ, Shimada T, Sanchez-Ponce R, Martin MV, Lei L, Zhao B, Kelly SL, Waterman MR, Lamb DC, Guengerich FP. 2007. Electron transport pathway for a Streptomyces cytochrome P450: Cytochrome P450 105D5-catalyzed fatty acid hydroxylation in Streptomyces coelicolor A3 (2). J Biol Chem 282(24):17486-17500.
    • (2007) J Biol Chem , vol.282 , Issue.24 , pp. 17486-17500
    • Chun, Y.J.1    Shimada, T.2    Sanchez-Ponce, R.3    Martin, M.V.4    Lei, L.5    Zhao, B.6    Kelly, S.L.7    Waterman, M.R.8    Lamb, D.C.9    Guengerich, F.P.10
  • 8
    • 80052102623 scopus 로고    scopus 로고
    • Strategy and success for the directed evolution of enzymes
    • Dalby PA. 2011. Strategy and success for the directed evolution of enzymes. Curr Opin Struct Biol 21(4):473-480.
    • (2011) Curr Opin Struct Biol , vol.21 , Issue.4 , pp. 473-480
    • Dalby, P.A.1
  • 9
    • 78650909062 scopus 로고    scopus 로고
    • Construction of a novel expression vector in Pseudonocardia autotrophica and its application to efficient biotransformation of compactin to pravastatin, a specific HMG-CoA reductase inhibitor
    • Fujii Y, Norihisa K, Fujii T, Aritoku Y, Kagawa Y, Sallam K, Jodo O, Arisawa A, Tamura T. 2011. Construction of a novel expression vector in Pseudonocardia autotrophica and its application to efficient biotransformation of compactin to pravastatin, a specific HMG-CoA reductase inhibitor. Biochem Biophys Res Commun 404(1):511-516.
    • (2011) Biochem Biophys Res Commun , vol.404 , Issue.1 , pp. 511-516
    • Fujii, Y.1    Norihisa, K.2    Fujii, T.3    Aritoku, Y.4    Kagawa, Y.5    Sallam, K.6    Jodo, O.7    Arisawa, A.8    Tamura, T.9
  • 10
    • 69949189242 scopus 로고    scopus 로고
    • Comparison of two vectors for functional expression of a bacterial cytochrome P450 gene in Escherichia coli using CYP153 genes
    • Fujita N, Sumisa F, Shindo K, Kabumoto H, Arisawa A, Ikenaga H, Misawa N. 2009. Comparison of two vectors for functional expression of a bacterial cytochrome P450 gene in Escherichia coli using CYP153 genes. Biosci Biotechnol Biochem 73(8):1825-1830.
    • (2009) Biosci Biotechnol Biochem , vol.73 , Issue.8 , pp. 1825-1830
    • Fujita, N.1    Sumisa, F.2    Shindo, K.3    Kabumoto, H.4    Arisawa, A.5    Ikenaga, H.6    Misawa, N.7
  • 11
    • 79953297687 scopus 로고    scopus 로고
    • Cytochromes P450: Exploiting diversity and enabling application as biocatalysts
    • Grogan G. 2011. Cytochromes P450: Exploiting diversity and enabling application as biocatalysts. Curr Opin Chem Biol 15(2):241-248.
    • (2011) Curr Opin Chem Biol , vol.15 , Issue.2 , pp. 241-248
    • Grogan, G.1
  • 12
    • 0036803924 scopus 로고    scopus 로고
    • Rate-limiting steps in cytochrome P450 catalysis
    • Guengerich FP. 2002. Rate-limiting steps in cytochrome P450 catalysis. Biol Chem 383(10):1553-1564.
    • (2002) Biol Chem , vol.383 , Issue.10 , pp. 1553-1564
    • Guengerich, F.P.1
  • 13
    • 36048939609 scopus 로고    scopus 로고
    • Mechanisms of cytochrome P450 substrate oxidation: MiniReview
    • Guengerich FP. 2007. Mechanisms of cytochrome P450 substrate oxidation: MiniReview. J Biochem Mol Toxicol 21(4):163-168.
    • (2007) J Biochem Mol Toxicol , vol.21 , Issue.4 , pp. 163-168
    • Guengerich, F.P.1
  • 14
    • 0017831786 scopus 로고
    • Bacterial P-450cam methylene monooxygenase components: Cytochrome m, putidaredoxin, and putidaredoxin reductase
    • Sidney F, Lester P, editors. New York: Academic Press.
    • Gunsalus IC, Wagner GC. 1978. Bacterial P-450cam methylene monooxygenase components: Cytochrome m, putidaredoxin, and putidaredoxin reductase. In: Sidney F, Lester P, editors. Methods in enzymology. New York: Academic Press. p 166-188.
    • (1978) Methods in enzymology , pp. 166-188
    • Gunsalus, I.C.1    Wagner, G.C.2
  • 15
    • 33846473252 scopus 로고    scopus 로고
    • Cytochrome P450 systems-Biological variations of electron transport chains
    • Hannemann F, Bichet A, Ewen K, Bernhardt R. 2007. Cytochrome P450 systems-Biological variations of electron transport chains. Biochim Biophys Acta 1770(3):330-344.
    • (2007) Biochim Biophys Acta , vol.1770 , Issue.3 , pp. 330-344
    • Hannemann, F.1    Bichet, A.2    Ewen, K.3    Bernhardt, R.4
  • 16
    • 0029643786 scopus 로고
    • Structure and function of cytochromes P450: A comparative analysis of three crystal structures
    • Hasemann CA, Kurumbail RG, Boddupalli SS, Peterson JA, Deisenhofer J. 1995. Structure and function of cytochromes P450: A comparative analysis of three crystal structures. Structure 3(1):41-62.
    • (1995) Structure , vol.3 , Issue.1 , pp. 41-62
    • Hasemann, C.A.1    Kurumbail, R.G.2    Boddupalli, S.S.3    Peterson, J.A.4    Deisenhofer, J.5
  • 17
    • 58149472888 scopus 로고    scopus 로고
    • Assembly of non-natural electron transfer conduits in the cytochrome P450 system: A critical assessment and update of artificial redox constructs amenable to exploitation in biotechnological areas
    • Hlavica P. 2009. Assembly of non-natural electron transfer conduits in the cytochrome P450 system: A critical assessment and update of artificial redox constructs amenable to exploitation in biotechnological areas. Biotechnol Adv 27(2):103-121.
    • (2009) Biotechnol Adv , vol.27 , Issue.2 , pp. 103-121
    • Hlavica, P.1
  • 19
  • 20
    • 70349694356 scopus 로고    scopus 로고
    • Directed evolution of the actinomycete cytochrome P450moxA (CYP105) for enhanced activity
    • Kabumoto H, Miyazaki K, Arisawa A. 2009. Directed evolution of the actinomycete cytochrome P450moxA (CYP105) for enhanced activity. Biosci Biotechnol Biochem 73(9):1922-1927.
    • (2009) Biosci Biotechnol Biochem , vol.73 , Issue.9 , pp. 1922-1927
    • Kabumoto, H.1    Miyazaki, K.2    Arisawa, A.3
  • 21
    • 66449088011 scopus 로고    scopus 로고
    • Generation of the human metabolite piceatannol from the anticancer-preventive agent resveratrol by bacterial cytochrome P450 BM3
    • Kim DH, Ahn T, Jung HC, Pan JG, Yun CH. 2009. Generation of the human metabolite piceatannol from the anticancer-preventive agent resveratrol by bacterial cytochrome P450 BM3. Drug Metab Dispos 37(5):932-936.
    • (2009) Drug Metab Dispos , vol.37 , Issue.5 , pp. 932-936
    • Kim, D.H.1    Ahn, T.2    Jung, H.C.3    Pan, J.G.4    Yun, C.H.5
  • 22
    • 0025286202 scopus 로고
    • Tissue-selective inhibition of cholesterol synthesis in vivo by pravastatin sodium, a 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitor
    • Koga T, Shimada Y, Kuroda M, Tsujita Y, Hasegawa K, Yamazaki M. 1990. Tissue-selective inhibition of cholesterol synthesis in vivo by pravastatin sodium, a 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitor. Biochim Biophys Acta 1045(2):115-120.
    • (1990) Biochim Biophys Acta , vol.1045 , Issue.2 , pp. 115-120
    • Koga, T.1    Shimada, Y.2    Kuroda, M.3    Tsujita, Y.4    Hasegawa, K.5    Yamazaki, M.6
  • 23
    • 0037157130 scopus 로고    scopus 로고
    • Enhanced electron transfer and lauric acid hydroxylation by site-directed mutagenesis of CYP119
    • Koo LS, Immoos CE, Cohen MS, Farmer PJ, de Montellano PRO. 2002. Enhanced electron transfer and lauric acid hydroxylation by site-directed mutagenesis of CYP119. J Am Chem Soc 124(20):5684-5691.
    • (2002) J Am Chem Soc , vol.124 , Issue.20 , pp. 5684-5691
    • Koo, L.S.1    Immoos, C.E.2    Cohen, M.S.3    Farmer, P.J.4    de Montellano, P.R.O.5
  • 24
    • 0036902235 scopus 로고    scopus 로고
    • Close-range electrostatic interactions in proteins
    • Kumar S, Nussinov R. 2002. Close-range electrostatic interactions in proteins. ChemBioChem 3(7):604-617.
    • (2002) ChemBioChem , vol.3 , Issue.7 , pp. 604-617
    • Kumar, S.1    Nussinov, R.2
  • 25
    • 33749333744 scopus 로고    scopus 로고
    • Putidaredoxin-to-cytochrome P450cam electron transfer: Differences between the two reductive steps required for catalysis
    • Kuznetsov V, Poulos T, Sevrioukova I. 2006. Putidaredoxin-to-cytochrome P450cam electron transfer: Differences between the two reductive steps required for catalysis. Biochemistry 45(39):11934-11944.
    • (2006) Biochemistry , vol.45 , Issue.39 , pp. 11934-11944
    • Kuznetsov, V.1    Poulos, T.2    Sevrioukova, I.3
  • 26
    • 61749090940 scopus 로고    scopus 로고
    • Heterologous expression, purification, and characterization of cytochrome P450sca-2 and mutants with improved solubility in Escherichia coli
    • Li P, Guan H, Li J, Lin Z. 2009. Heterologous expression, purification, and characterization of cytochrome P450sca-2 and mutants with improved solubility in Escherichia coli. Protein Expr Purif 65(2):196-203.
    • (2009) Protein Expr Purif , vol.65 , Issue.2 , pp. 196-203
    • Li, P.1    Guan, H.2    Li, J.3    Lin, Z.4
  • 28
    • 84876333285 scopus 로고    scopus 로고
    • Two-substrate reactions
    • Marangoni AG, editor. Hoboken, NJ: John Wiley & Sons.
    • Marangoni AG. 2003. Two-substrate reactions. In: Marangoni AG, editor. Enzyme kinetics: a modern approach. Hoboken, NJ: John Wiley & Sons. p 90-101.
    • (2003) Enzyme kinetics: a modern approach , pp. 90-101
    • Marangoni, A.G.1
  • 29
    • 0024442346 scopus 로고
    • Purification and characterization of cytochrome P-450sca from Streptomyces carbophilus. ML-236B (compactin) induces a cytochrome P-450sca in Streptomyces carbophilus that hydroxylates ML-236B to pravastatin sodium (CS-514), a tissue-selective inhibitor of 3-hydroxy-3-methylglutaryl-coenzyme-A reductase
    • Matsuoka T, Miyakoshi S, Tanzawa K, Nakahara K, Hosobuchi M, Serizawa N. 1989. Purification and characterization of cytochrome P-450sca from Streptomyces carbophilus. ML-236B (compactin) induces a cytochrome P-450sca in Streptomyces carbophilus that hydroxylates ML-236B to pravastatin sodium (CS-514), a tissue-selective inhibitor of 3-hydroxy-3-methylglutaryl-coenzyme-A reductase. Eur J Biochem 184(3):707-713.
    • (1989) Eur J Biochem , vol.184 , Issue.3 , pp. 707-713
    • Matsuoka, T.1    Miyakoshi, S.2    Tanzawa, K.3    Nakahara, K.4    Hosobuchi, M.5    Serizawa, N.6
  • 30
    • 0031404684 scopus 로고    scopus 로고
    • The dimerization of Pseudomonas putida cytochrome P450cam: Practical consequences and engineering of a monomeric enzyme
    • Nickerson D, Wong L. 1997. The dimerization of Pseudomonas putida cytochrome P450cam: Practical consequences and engineering of a monomeric enzyme. Protein Eng 10(12):1357-1361.
    • (1997) Protein Eng , vol.10 , Issue.12 , pp. 1357-1361
    • Nickerson, D.1    Wong, L.2
  • 32
    • 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
  • 33
    • 23044506105 scopus 로고    scopus 로고
    • Kinetic determinations of molecular interactions using Biacore-Minimum data requirements for efficient experimental design
    • Önell A, Andersson K. 2005. Kinetic determinations of molecular interactions using Biacore-Minimum data requirements for efficient experimental design. J Mol Recognit 18(4):307-317.
    • (2005) J Mol Recognit , vol.18 , Issue.4 , pp. 307-317
    • Önell, A.1    Andersson, K.2
  • 34
    • 0141888967 scopus 로고    scopus 로고
    • High-throughput carbon monoxide binding assay for cytochrome P450
    • Arnold FH, Georgiou G, editors. Totowa, NJ: Humana Press.
    • Otey CR. 2003. High-throughput carbon monoxide binding assay for cytochrome P450. In: Arnold FH, Georgiou G, editors. Directed enzyme evolution: screening and selection methods. Totowa, NJ: Humana Press. p 137-139.
    • (2003) Directed enzyme evolution: screening and selection methods , pp. 137-139
    • Otey, C.R.1
  • 35
    • 77449114845 scopus 로고    scopus 로고
    • Regioselective hydroxylation of daidzein using P450 (CYP105D7) from Streptomyces avermitilis MA4680
    • Pandey B, Roh C, Choi K, Lee N, Kim E, Ko S, Kim T, Yun H, Kim B. 2009. Regioselective hydroxylation of daidzein using P450 (CYP105D7) from Streptomyces avermitilis MA4680. Biotechnol Bioeng 105(4):697-704.
    • (2009) Biotechnol Bioeng , vol.105 , Issue.4 , pp. 697-704
    • Pandey, B.1    Roh, C.2    Choi, K.3    Lee, N.4    Kim, E.5    Ko, S.6    Kim, T.7    Yun, H.8    Kim, B.9
  • 36
    • 0037145075 scopus 로고    scopus 로고
    • Thermophilic cytochrome P450 (CYP119) from Sulfolobus solfataricus: High resolution structure and functional properties
    • Park SY, Yamane K, Adachi S, Shiro Y, Weiss KE, Maves SA, Sligar SG. 2002. Thermophilic cytochrome P450 (CYP119) from Sulfolobus solfataricus: High resolution structure and functional properties. J Inorg Biochem 91(4):491-501.
    • (2002) J Inorg Biochem , vol.91 , Issue.4 , pp. 491-501
    • Park, S.Y.1    Yamane, K.2    Adachi, S.3    Shiro, Y.4    Weiss, K.E.5    Maves, S.A.6    Sligar, S.G.7
  • 38
    • 0344824425 scopus 로고    scopus 로고
    • Cytochrome P450 flexibility
    • Poulos TL. 2003. Cytochrome P450 flexibility. Proc Natl Acad Sci USA 100(23):13121-13122.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.23 , pp. 13121-13122
    • Poulos, T.L.1
  • 39
    • 0027113109 scopus 로고
    • Cytochrome P450cam: Crystallography, oxygen activation, and electron transfer
    • Poulos T, Raag R. 1992. Cytochrome P450cam: Crystallography, oxygen activation, and electron transfer. FASEB J 6(2):674-679.
    • (1992) FASEB J , vol.6 , Issue.2 , pp. 674-679
    • Poulos, T.1    Raag, R.2
  • 40
    • 0023645035 scopus 로고
    • High-resolution crystal structure of cytochrome P450cam
    • Poulos TL, Finzel BC, Howard AJ. 1987. High-resolution crystal structure of cytochrome P450cam. J Mol Biol 195(3):687-700.
    • (1987) J Mol Biol , vol.195 , Issue.3 , pp. 687-700
    • Poulos, T.L.1    Finzel, B.C.2    Howard, A.J.3
  • 41
    • 78149432825 scopus 로고    scopus 로고
    • Laboratory evolution of stereoselective enzymes: A prolific source of catalysts for asymmetric reactions
    • Reetz MT. 2011. Laboratory evolution of stereoselective enzymes: A prolific source of catalysts for asymmetric reactions. Angew Chem Int Ed 50(1):138-174.
    • (2011) Angew Chem Int Ed , vol.50 , Issue.1 , pp. 138-174
    • Reetz, M.T.1
  • 42
    • 34248567845 scopus 로고    scopus 로고
    • Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes
    • Reetz MT, Carballeira JD. 2007. Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes. Nat Protoc 2(4):891-903.
    • (2007) Nat Protoc , vol.2 , Issue.4 , pp. 891-903
    • Reetz, M.T.1    Carballeira, J.D.2
  • 44
    • 54349090614 scopus 로고    scopus 로고
    • Addressing the numbers problem in directed evolution
    • Reetz MT, Kahakeaw D, Lohmer R. 2008. Addressing the numbers problem in directed evolution. ChemBioChem 9(11):1797-1804.
    • (2008) ChemBioChem , vol.9 , Issue.11 , pp. 1797-1804
    • Reetz, M.T.1    Kahakeaw, D.2    Lohmer, R.3
  • 45
    • 84892590749 scopus 로고    scopus 로고
    • Application of a new versatile electron transfer system for cytochrome P450-based Escherichia coli whole-cell bioconversions
    • doi: 10.1007/s00253-012-4612-0
    • Ringle M, Khatri Y, Zapp J, Hannemann F, Bernhardt R. 2012. Application of a new versatile electron transfer system for cytochrome P450-based Escherichia coli whole-cell bioconversions. Appl Microbiol Biotechnol. doi: 10.1007/s00253-012-4612-0
    • (2012) Appl Microbiol Biotechnol.
    • Ringle, M.1    Khatri, Y.2    Zapp, J.3    Hannemann, F.4    Bernhardt, R.5
  • 46
    • 65349121795 scopus 로고    scopus 로고
    • Engineering and improvement of the efficiency of a chimeric [P450cam-RhFRed reductase domain] enzyme
    • Robin A, Roberts G, Kisch J, Sabbadin F, Grogan G, Bruce N, Turner N, Flitsch S. 2009. Engineering and improvement of the efficiency of a chimeric [P450cam-RhFRed reductase domain] enzyme. Chem Commun 2009(18):2478-2480.
    • (2009) Chem Commun , vol.2009 , Issue.18 , pp. 2478-2480
    • Robin, A.1    Roberts, G.2    Kisch, J.3    Sabbadin, F.4    Grogan, G.5    Bruce, N.6    Turner, N.7    Flitsch, S.8
  • 47
    • 67349234459 scopus 로고    scopus 로고
    • Hydroxylation of daidzein by CYP107H1 from Bacillus subtilis 168
    • Roh C, Choi K, Pandey B, Kim B. 2009. Hydroxylation of daidzein by CYP107H1 from Bacillus subtilis 168. J Mol Catal B Enzym 59(4):248-253.
    • (2009) J Mol Catal B Enzym , vol.59 , Issue.4 , pp. 248-253
    • Roh, C.1    Choi, K.2    Pandey, B.3    Kim, B.4
  • 48
    • 0032500339 scopus 로고    scopus 로고
    • Binding and electron transfer between putidaredoxin and cytochrome P450cam. Theory and experiments
    • Roitberg AE, Holden MJ, Mayhew MP, Kurnikov IV, Beratan DN, Vilker VL. 1998. Binding and electron transfer between putidaredoxin and cytochrome P450cam. Theory and experiments. J Am Chem Soc 120(35):8927-8932.
    • (1998) J Am Chem Soc , vol.120 , Issue.35 , pp. 8927-8932
    • Roitberg, A.E.1    Holden, M.J.2    Mayhew, M.P.3    Kurnikov, I.V.4    Beratan, D.N.5    Vilker, V.L.6
  • 49
    • 0021111647 scopus 로고
    • Purification and properties of putidaredoxin reductase
    • Roome P Jr, Philley J, Peterson J. 1983. Purification and properties of putidaredoxin reductase. J Biol Chem 258(4):2593-2598.
    • (1983) J Biol Chem , vol.258 , Issue.4 , pp. 2593-2598
    • Roome Jr., P.1    Philley, J.2    Peterson, J.3
  • 51
    • 84861868170 scopus 로고    scopus 로고
    • Practical application of cytochrome P450
    • Sakaki T. 2012. Practical application of cytochrome P450. Biol Pharm Bull 35(6):844-849.
    • (2012) Biol Pharm Bull , vol.35 , Issue.6 , pp. 844-849
    • Sakaki, T.1
  • 52
    • 79952572516 scopus 로고    scopus 로고
    • Characterization of cytochrome P450 monooxygenase CYP154H1 from the thermophilic soil bacterium Thermobifida fusca
    • Schallmey A, den Besten G, Teune IGP, Kembaren RF, Janssen DB. 2011. Characterization of cytochrome P450 monooxygenase CYP154H1 from the thermophilic soil bacterium Thermobifida fusca. Appl Microbiol Biotechnol 89(5):1475-1485.
    • (2011) Appl Microbiol Biotechnol , vol.89 , Issue.5 , pp. 1475-1485
    • Schallmey, A.1    den Besten, G.2    Teune, I.G.P.3    Kembaren, R.F.4    Janssen, D.B.5
  • 53
    • 65549113338 scopus 로고    scopus 로고
    • Rational design of a minimal and highly enriched CYP102A1 mutant library with improved regio-, stereo- and chemoselectivity
    • Seifert A, Vomund S, Grohmann K, Kriening S, Urlacher VB, Laschat S, Pleiss J. 2009. Rational design of a minimal and highly enriched CYP102A1 mutant library with improved regio-, stereo- and chemoselectivity. ChemBioChem 10(5):853-861.
    • (2009) ChemBioChem , vol.10 , Issue.5 , pp. 853-861
    • Seifert, A.1    Vomund, S.2    Grohmann, K.3    Kriening, S.4    Urlacher, V.B.5    Laschat, S.6    Pleiss, J.7
  • 54
    • 0025767694 scopus 로고
    • A two component-type cytochrome P-450 monooxygenase system in a prokaryote that catalyzes hydroxylation of ML-236B to pravastatin, a tissue-selective inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • Serizawa N, Matsuoka T. 1991. A two component-type cytochrome P-450 monooxygenase system in a prokaryote that catalyzes hydroxylation of ML-236B to pravastatin, a tissue-selective inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase. Biochim Biophys Acta 1084(1):35-40.
    • (1991) Biochim Biophys Acta , vol.1084 , Issue.1 , pp. 35-40
    • Serizawa, N.1    Matsuoka, T.2
  • 55
    • 0037067760 scopus 로고    scopus 로고
    • Putidaredoxin reductase, a new function for an old protein
    • Sevrioukova IF, Poulos TL. 2002. Putidaredoxin reductase, a new function for an old protein. J Biol Chem 277(28):25831-25839.
    • (2002) J Biol Chem , vol.277 , Issue.28 , pp. 25831-25839
    • Sevrioukova, I.F.1    Poulos, T.L.2
  • 56
    • 79951574727 scopus 로고    scopus 로고
    • Structural biology of redox partner interactions in P450cam monooxygenase: A fresh look at an old system
    • Sevrioukova I, Poulos T. 2011. Structural biology of redox partner interactions in P450cam monooxygenase: A fresh look at an old system. Arch Biochem Biophys 507(1):66-74.
    • (2011) Arch Biochem Biophys , vol.507 , Issue.1 , pp. 66-74
    • Sevrioukova, I.1    Poulos, T.2
  • 57
    • 0141869098 scopus 로고    scopus 로고
    • Crystal structure of putidaredoxin, the [2Fe-2S] component of the P450cam monooxygenase system from Pseudomonas putida
    • Sevrioukova I, Garcia C, Li H, Bhaskar B, Poulos T. 2003. Crystal structure of putidaredoxin, the [2Fe-2S] component of the P450cam monooxygenase system from Pseudomonas putida. J Mol Biol 333(2):377-392.
    • (2003) J Mol Biol , vol.333 , Issue.2 , pp. 377-392
    • Sevrioukova, I.1    Garcia, C.2    Li, H.3    Bhaskar, B.4    Poulos, T.5
  • 58
    • 1042264042 scopus 로고    scopus 로고
    • Crystal structure of putidaredoxin reductase from Pseudomonas putida, the final structural component of the cytochrome P450cam monooxygenase
    • Sevrioukova IF, Li H, Poulos TL. 2004. Crystal structure of putidaredoxin reductase from Pseudomonas putida, the final structural component of the cytochrome P450cam monooxygenase. J Mol Biol 336(4):889-902.
    • (2004) J Mol Biol , vol.336 , Issue.4 , pp. 889-902
    • Sevrioukova, I.F.1    Li, H.2    Poulos, T.L.3
  • 59
    • 0030924503 scopus 로고    scopus 로고
    • Properties of cytochrome P450 isoenzymes and their substrates Part 1: Active site characteristics
    • Smith DA, Ackland MJ, Jones BC. 1997a. Properties of cytochrome P450 isoenzymes and their substrates Part 1: Active site characteristics. Drug Discovery Today 2(10):406-414.
    • (1997) Drug Discovery Today , vol.2 , Issue.10 , pp. 406-414
    • Smith, D.A.1    Ackland, M.J.2    Jones, B.C.3
  • 60
    • 0030763355 scopus 로고    scopus 로고
    • Properties of cytochrome P450 isoenzymes and their substrates, part 2: Properties of cytochrome P450 substrates
    • Smith DA, Ackland MJ, Jones BC. 1997b. Properties of cytochrome P450 isoenzymes and their substrates, part 2: Properties of cytochrome P450 substrates. Drug Discovery Today 2(11):479-486.
    • (1997) Drug Discovery Today , vol.2 , Issue.11 , pp. 479-486
    • Smith, D.A.1    Ackland, M.J.2    Jones, B.C.3
  • 62
    • 0022485201 scopus 로고
    • CS-514, a competitive inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase: Tissue-selective inhibition of sterol synthesis and hypolipidemic effect on various animal species
    • Tsujita Y, Kuroda M, Shimada Y, Tanzawa K, Arai M, Kaneko I, Tanaka M, Masuda H, Tarumi C, Watanabe Y. 1986. CS-514, a competitive inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase: Tissue-selective inhibition of sterol synthesis and hypolipidemic effect on various animal species. Biochim Biophys Acta 877(1):50-60.
    • (1986) Biochim Biophys Acta , vol.877 , Issue.1 , pp. 50-60
    • Tsujita, Y.1    Kuroda, M.2    Shimada, Y.3    Tanzawa, K.4    Arai, M.5    Kaneko, I.6    Tanaka, M.7    Masuda, H.8    Tarumi, C.9    Watanabe, Y.10
  • 63
    • 57149131662 scopus 로고    scopus 로고
    • Molecular evolution of a steroid hydroxylating cytochrome P450 using a versatile steroid detection system for screening
    • Virus C, Bernhardt R. 2008. Molecular evolution of a steroid hydroxylating cytochrome P450 using a versatile steroid detection system for screening. Lipids 43(12):1133-1141.
    • (2008) Lipids , vol.43 , Issue.12 , pp. 1133-1141
    • Virus, C.1    Bernhardt, R.2
  • 64
    • 58149168714 scopus 로고    scopus 로고
    • Electron transfer in the P450cam/PDX complex. The QM/MM e-pathway
    • Wallrapp F, Masone D, Guallar V. 2008. Electron transfer in the P450cam/PDX complex. The QM/MM e-pathway. J Phys Chem A 112(50):12989-12994.
    • (2008) J Phys Chem A , vol.112 , Issue.50 , pp. 12989-12994
    • Wallrapp, F.1    Masone, D.2    Guallar, V.3
  • 65
    • 0031034657 scopus 로고    scopus 로고
    • Combinatorial manipulation of three key active site residues in glycinamide ribonucleotide transformylase
    • Warren MS, Benkovic SJ. 1997. Combinatorial manipulation of three key active site residues in glycinamide ribonucleotide transformylase. Protein Eng 10(1):63-68.
    • (1997) Protein Eng , vol.10 , Issue.1 , pp. 63-68
    • Warren, M.S.1    Benkovic, S.J.2
  • 66
    • 0029133802 scopus 로고
    • in2 from Streptomyces carbophilus involved in production of pravastatin, a specific HMG-CoA reductase inhibitor
    • in2 from Streptomyces carbophilus involved in production of pravastatin, a specific HMG-CoA reductase inhibitor. Gene 163(1):81-85.
    • (1995) Gene , vol.163 , Issue.1 , pp. 81-85
    • Watanabe, I.1    Nara, F.2    Serizawa, N.3
  • 67
    • 0025082684 scopus 로고
    • Additivity of mutational effects in proteins
    • Wells JA. 1990. Additivity of mutational effects in proteins. Biochemistry 29(37):8509-8517.
    • (1990) Biochemistry , vol.29 , Issue.37 , pp. 8509-8517
    • Wells, J.A.1
  • 70
    • 77952754570 scopus 로고    scopus 로고
    • Regio-and stereospecificity of filipin hydroxylation sites revealed by crystal structures of cytochrome P450 105P1 and 105D6 from Streptomyces avermitilis
    • Xu L, Fushinobu S, Takamatsu S, Wakagi T, Ikeda H, Shoun H. 2010. Regio-and stereospecificity of filipin hydroxylation sites revealed by crystal structures of cytochrome P450 105P1 and 105D6 from Streptomyces avermitilis. J Biol Chem 285(22):16844-16853.
    • (2010) J Biol Chem , vol.285 , Issue.22 , pp. 16844-16853
    • Xu, L.1    Fushinobu, S.2    Takamatsu, S.3    Wakagi, T.4    Ikeda, H.5    Shoun, H.6
  • 71
    • 77956240069 scopus 로고    scopus 로고
    • Molecular characterization of a class I P450 electron transfer system from Novosphingobium aromaticivorans DSM12444
    • Yang W, Bell SG, Wang H, Zhou W, Hoskins N, Dale A, Bartlam M, Wong LL, Rao Z. 2010. Molecular characterization of a class I P450 electron transfer system from Novosphingobium aromaticivorans DSM12444. J Biol Chem 285(35):27372-27384.
    • (2010) J Biol Chem , vol.285 , Issue.35 , pp. 27372-27384
    • Yang, W.1    Bell, S.G.2    Wang, H.3    Zhou, W.4    Hoskins, N.5    Dale, A.6    Bartlam, M.7    Wong, L.L.8    Rao, Z.9
  • 73
    • 77957814994 scopus 로고    scopus 로고
    • Structural evidence for enhancement of sequential vitamin D3 hydroxylation activities by directed evolution of cytochrome P450 vitamin D3 hydroxylase
    • Yasutake Y, Fujii Y, Nishioka T, Cheon WK, Arisawa A, Tamura T. 2010. Structural evidence for enhancement of sequential vitamin D3 hydroxylation activities by directed evolution of cytochrome P450 vitamin D3 hydroxylase. J Biol Chem 285(41):31193-31201.
    • (2010) J Biol Chem , vol.285 , Issue.41 , pp. 31193-31201
    • Yasutake, Y.1    Fujii, Y.2    Nishioka, T.3    Cheon, W.K.4    Arisawa, A.5    Tamura, T.6
  • 74
    • 0034687092 scopus 로고    scopus 로고
    • Rate-determining steps in phenacetin oxidations by human cytochrome P450 1A2 and selected mutants
    • Yun CH, Miller GP, Guengerich FP. 2000. Rate-determining steps in phenacetin oxidations by human cytochrome P450 1A2 and selected mutants. Biochemistry 39(37):11319-11329.
    • (2000) Biochemistry , vol.39 , Issue.37 , pp. 11319-11329
    • Yun, C.H.1    Miller, G.P.2    Guengerich, F.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.