메뉴 건너뛰기




Volumn 24, Issue 7, 2006, Pages 324-330

Cytochrome P450 monooxygenases: perspectives for synthetic application

Author keywords

[No Author keywords available]

Indexed keywords

BIOREMEDIATION; COSTS; ENZYME KINETICS; OPTIMIZATION; PHARMACOKINETICS; SYNTHESIS (CHEMICAL);

EID: 33745652737     PISSN: 01677799     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibtech.2006.05.002     Document Type: Review
Times cited : (254)

References (62)
  • 1
    • 0025895757 scopus 로고
    • Reactions and significance of cytochrome P-450 enzymes
    • Guengerich F.P. Reactions and significance of cytochrome P-450 enzymes. J. Biol. Chem. 266 (1991) 10019-10022
    • (1991) J. Biol. Chem. , vol.266 , pp. 10019-10022
    • Guengerich, F.P.1
  • 2
    • 23844442197 scopus 로고    scopus 로고
    • Biodiversity of cytochrome P450 redox systems
    • McLean K.J., et al. Biodiversity of cytochrome P450 redox systems. Biochem. Soc. Trans. 33 (2005) 796-801
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 796-801
    • McLean, K.J.1
  • 3
    • 0041513426 scopus 로고    scopus 로고
    • Reactions catalyzed by bacterial cytochromes P450
    • Cryle M.J., et al. Reactions catalyzed by bacterial cytochromes P450. Aust. J. Chem. 56 (2003) 749-762
    • (2003) Aust. J. Chem. , vol.56 , pp. 749-762
    • Cryle, M.J.1
  • 4
    • 0034706012 scopus 로고    scopus 로고
    • Oxidation of 1,2,4,5-tetramethoxybenzene to a cation radical by cytochrome P450
    • Sato H., and Guengerich F.P. Oxidation of 1,2,4,5-tetramethoxybenzene to a cation radical by cytochrome P450. J. Am. Chem. Soc. 122 (2000) 8099-8100
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 8099-8100
    • Sato, H.1    Guengerich, F.P.2
  • 5
    • 21144439895 scopus 로고    scopus 로고
    • The biosynthesis of vancomycin-type glycopeptide antibiotics - a model for oxidative side-chain cross-linking by oxygenases coupled to the action of peptide synthetases
    • Bischoff D., et al. The biosynthesis of vancomycin-type glycopeptide antibiotics - a model for oxidative side-chain cross-linking by oxygenases coupled to the action of peptide synthetases. ChemBioChem 6 (2005) 267-272
    • (2005) ChemBioChem , vol.6 , pp. 267-272
    • Bischoff, D.1
  • 6
    • 0029954699 scopus 로고    scopus 로고
    • The mechanism of the acyl-carbon bond cleavage reaction catalyzed by recombinant sterol 14 alpha-demethylase of Candida albicans (other names are: lanosterol 14 alpha-demethylase, P-45014DM, and CYP51)
    • Shyadehi A.Z., et al. The mechanism of the acyl-carbon bond cleavage reaction catalyzed by recombinant sterol 14 alpha-demethylase of Candida albicans (other names are: lanosterol 14 alpha-demethylase, P-45014DM, and CYP51). J. Biol. Chem. 271 (1996) 12445-12450
    • (1996) J. Biol. Chem. , vol.271 , pp. 12445-12450
    • Shyadehi, A.Z.1
  • 7
    • 0036400373 scopus 로고    scopus 로고
    • Evolution of drug metabolism: hitchhiking the technology bandwagon
    • Miners J.O. Evolution of drug metabolism: hitchhiking the technology bandwagon. Clin. Exp. Pharmacol. Physiol. 29 (2002) 1040-1044
    • (2002) Clin. Exp. Pharmacol. Physiol. , vol.29 , pp. 1040-1044
    • Miners, J.O.1
  • 8
    • 0036560522 scopus 로고    scopus 로고
    • Cytochrome P450 enzymes in the generation of commercial products
    • Guengerich F.P. Cytochrome P450 enzymes in the generation of commercial products. Nat. Rev. Drug Discov. 1 (2002) 359-366
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 359-366
    • Guengerich, F.P.1
  • 9
    • 0242500462 scopus 로고    scopus 로고
    • Practical issues in the application of oxygenases
    • van Beilen J.B., et al. Practical issues in the application of oxygenases. Trends Biotechnol. 21 (2003) 170-177
    • (2003) Trends Biotechnol. , vol.21 , pp. 170-177
    • van Beilen, J.B.1
  • 10
    • 33745636088 scopus 로고    scopus 로고
    • Petzoldt, K. et al. Schering Aktiengesellschaft (Berlin, Germany). Process for the preparation of 11-beta-hydroxy steroids. Patent 4353985
  • 11
    • 0001298438 scopus 로고
    • Microbial transformation of steroids. Introduction of oxygen at carbon-11 of progesterone
    • Peterson D.H. Microbial transformation of steroids. Introduction of oxygen at carbon-11 of progesterone. J. Am. Chem. Soc. 74 (1952) 5933-5936
    • (1952) J. Am. Chem. Soc. , vol.74 , pp. 5933-5936
    • Peterson, D.H.1
  • 12
    • 0027050071 scopus 로고
    • Steroids, the steroid community, and Upjohn in perspective: a profile of innovation
    • Hogg J.A. Steroids, the steroid community, and Upjohn in perspective: a profile of innovation. Steroids 57 (1992) 593-616
    • (1992) Steroids , vol.57 , pp. 593-616
    • Hogg, J.A.1
  • 13
    • 0344961885 scopus 로고    scopus 로고
    • Bioconversion of compactin into pravastatin by Streptomyces sp
    • Park J.W., et al. Bioconversion of compactin into pravastatin by Streptomyces sp. Biotechnol. Lett. 25 (2003) 1827-1831
    • (2003) Biotechnol. Lett. , vol.25 , pp. 1827-1831
    • Park, J.W.1
  • 14
    • 0027512258 scopus 로고
    • Substrate specificity of 6-deoxyerythronolide B hydroxylase, a bacterial cytochrome P450 of erythromycin A biosynthesis
    • Andersen J.F., et al. Substrate specificity of 6-deoxyerythronolide B hydroxylase, a bacterial cytochrome P450 of erythromycin A biosynthesis. Biochemistry 32 (1993) 1905-1913
    • (1993) Biochemistry , vol.32 , pp. 1905-1913
    • Andersen, J.F.1
  • 15
    • 0347298786 scopus 로고    scopus 로고
    • Crystal structure of OxyB, a cytochrome P450 implicated in an oxidative phenol coupling reaction during vancomycin biosynthesis
    • Zerbe K., et al. Crystal structure of OxyB, a cytochrome P450 implicated in an oxidative phenol coupling reaction during vancomycin biosynthesis. J. Biol. Chem. 277 (2002) 47476-47485
    • (2002) J. Biol. Chem. , vol.277 , pp. 47476-47485
    • Zerbe, K.1
  • 16
    • 0345306647 scopus 로고    scopus 로고
    • Crystal structure of OxyC, a cytochrome P450 implicated in an oxidative C-C coupling reaction during vancomycin biosynthesis
    • Pylypenko O., et al. Crystal structure of OxyC, a cytochrome P450 implicated in an oxidative C-C coupling reaction during vancomycin biosynthesis. J. Biol. Chem. 278 (2003) 46727-46733
    • (2003) J. Biol. Chem. , vol.278 , pp. 46727-46733
    • Pylypenko, O.1
  • 17
    • 20444491589 scopus 로고    scopus 로고
    • Crystal structures of the ferrous dioxygen complex of wild-type cytochrome P450eryF and its mutants, A245S and A245T: investigation of the proton transfer system in P450eryF
    • Nagano S., et al. Crystal structures of the ferrous dioxygen complex of wild-type cytochrome P450eryF and its mutants, A245S and A245T: investigation of the proton transfer system in P450eryF. J. Biol. Chem. 280 (2005) 22102-22107
    • (2005) J. Biol. Chem. , vol.280 , pp. 22102-22107
    • Nagano, S.1
  • 18
    • 15944383707 scopus 로고    scopus 로고
    • Coexpression in yeast of Taxus cytochrome P450 reductase with cytochrome P450 oxygenases involved in Taxol biosynthesis
    • Jennewein S., et al. Coexpression in yeast of Taxus cytochrome P450 reductase with cytochrome P450 oxygenases involved in Taxol biosynthesis. Biotechnol. Bioeng. 89 (2005) 588-598
    • (2005) Biotechnol. Bioeng. , vol.89 , pp. 588-598
    • Jennewein, S.1
  • 19
    • 17444405636 scopus 로고    scopus 로고
    • Biocatalytic production of perillyl alcohol from limonene by using a novel Mycobacterium sp. cytochrome P450 alkane hydroxylase expressed in Pseudomonas putida
    • van Beilen J.B., et al. Biocatalytic production of perillyl alcohol from limonene by using a novel Mycobacterium sp. cytochrome P450 alkane hydroxylase expressed in Pseudomonas putida. Appl. Environ. Microbiol. 71 (2005) 1737-1744
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 1737-1744
    • van Beilen, J.B.1
  • 20
    • 0029163161 scopus 로고
    • Cytochrome P450 proteins and potential utilization in biodegradation
    • Guengerich F.P. Cytochrome P450 proteins and potential utilization in biodegradation. Environ. Health Perspect. 103 Suppl. 5 (1995) 25-28
    • (1995) Environ. Health Perspect. , vol.103 , Issue.SUPPL. 5 , pp. 25-28
    • Guengerich, F.P.1
  • 21
    • 0030918730 scopus 로고    scopus 로고
    • Engineering cytochrome P450s for bioremediation
    • Kellner D.G., et al. Engineering cytochrome P450s for bioremediation. Curr. Opin. Biotechnol. 8 (1997) 274-278
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 274-278
    • Kellner, D.G.1
  • 22
    • 0035081039 scopus 로고    scopus 로고
    • Oxidation of polychlorinated benzenes by genetically engineered CYP101 (cytochrome P450(cam))
    • Jones J.P., et al. Oxidation of polychlorinated benzenes by genetically engineered CYP101 (cytochrome P450(cam)). Eur. J. Biochem. 268 (2001) 1460-1467
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1460-1467
    • Jones, J.P.1
  • 23
    • 0036578528 scopus 로고    scopus 로고
    • Biodegradation of polychlorinated dibenzo-p-dioxins by recombinant yeast expressing rat CYP1A subfamily
    • Sakaki T., et al. Biodegradation of polychlorinated dibenzo-p-dioxins by recombinant yeast expressing rat CYP1A subfamily. Arch. Biochem. Biophys. 401 (2002) 91-98
    • (2002) Arch. Biochem. Biophys. , vol.401 , pp. 91-98
    • Sakaki, T.1
  • 24
    • 13244265817 scopus 로고    scopus 로고
    • Metabolism of polychlorinated dibenzo-p-dioxins by cytochrome P450 BM-3 and its mutant
    • Sulistyaningdyah W.T., et al. Metabolism of polychlorinated dibenzo-p-dioxins by cytochrome P450 BM-3 and its mutant. Biotechnol. Lett. 26 (2004) 1857-1860
    • (2004) Biotechnol. Lett. , vol.26 , pp. 1857-1860
    • Sulistyaningdyah, W.T.1
  • 25
    • 0034819837 scopus 로고    scopus 로고
    • Protein engineering of Bacillus megaterium CYP102. The oxidation of polycyclic aromatic hydrocarbons
    • Carmichael A.B., and Wong L.L. Protein engineering of Bacillus megaterium CYP102. The oxidation of polycyclic aromatic hydrocarbons. Eur. J. Biochem. 268 (2001) 3117-3125
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3117-3125
    • Carmichael, A.B.1    Wong, L.L.2
  • 26
    • 0142136150 scopus 로고    scopus 로고
    • Identification and characterization of the CYP52 family of Candida tropicalis ATCC 20336, important for the conversion of fatty acids and alkanes to α, ω-dicarboxylic acids
    • Craft D.L., et al. Identification and characterization of the CYP52 family of Candida tropicalis ATCC 20336, important for the conversion of fatty acids and alkanes to α, ω-dicarboxylic acids. Appl. Environ. Microbiol. 69 (2003) 5983-5991
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 5983-5991
    • Craft, D.L.1
  • 27
    • 0026636011 scopus 로고
    • Metabolic engineering of Candida tropicalis for the production of long-chain dicarboxylic acids
    • Picataggio S., et al. Metabolic engineering of Candida tropicalis for the production of long-chain dicarboxylic acids. Biotechnology (N. Y.) 10 (1992) 894-898
    • (1992) Biotechnology (N. Y.) , vol.10 , pp. 894-898
    • Picataggio, S.1
  • 28
    • 3042607977 scopus 로고    scopus 로고
    • CYP175A1 from Thermus thermophilus HB27, the first beta-carotene hydroxylase of the P450 superfamily
    • Blasco F., et al. CYP175A1 from Thermus thermophilus HB27, the first beta-carotene hydroxylase of the P450 superfamily. Appl. Microbiol. Biotechnol. 64 (2004) 671-674
    • (2004) Appl. Microbiol. Biotechnol. , vol.64 , pp. 671-674
    • Blasco, F.1
  • 29
    • 0037065720 scopus 로고    scopus 로고
    • Hydroxylation of specifically deuterated limonene enantiomers by cytochrome p450 limonene-6-hydroxylase reveals the mechanism of multiple product formation
    • Wust M., and Croteau R.B. Hydroxylation of specifically deuterated limonene enantiomers by cytochrome p450 limonene-6-hydroxylase reveals the mechanism of multiple product formation. Biochemistry 41 (2002) 1820-1827
    • (2002) Biochemistry , vol.41 , pp. 1820-1827
    • Wust, M.1    Croteau, R.B.2
  • 30
    • 0036332286 scopus 로고    scopus 로고
    • Indirubin and meisoindigo in the treatment of chronic myelogenous leukemia in China
    • Xiao Z., et al. Indirubin and meisoindigo in the treatment of chronic myelogenous leukemia in China. Leuk. Lymphoma 43 (2002) 1763-1768
    • (2002) Leuk. Lymphoma , vol.43 , pp. 1763-1768
    • Xiao, Z.1
  • 31
    • 15744398069 scopus 로고    scopus 로고
    • Indole hydroxylation by bacterial cytochrome P450 BM-3 and modulation of activity by cumene hydroperoxide
    • Li Q.S., et al. Indole hydroxylation by bacterial cytochrome P450 BM-3 and modulation of activity by cumene hydroperoxide. Biosci. Biotechnol. Biochem. 69 (2005) 293-300
    • (2005) Biosci. Biotechnol. Biochem. , vol.69 , pp. 293-300
    • Li, Q.S.1
  • 32
    • 0035498833 scopus 로고    scopus 로고
    • Random mutagenesis of human cytochrome p450 2A6 and screening with indole oxidation products
    • Nakamura K., et al. Random mutagenesis of human cytochrome p450 2A6 and screening with indole oxidation products. Arch. Biochem. Biophys. 395 (2001) 25-31
    • (2001) Arch. Biochem. Biophys. , vol.395 , pp. 25-31
    • Nakamura, K.1
  • 33
    • 28844494791 scopus 로고    scopus 로고
    • Expansion of substrate specificity of cytochrome P450 2A6 by random and site-directed mutagenesis
    • Wu Z.L., et al. Expansion of substrate specificity of cytochrome P450 2A6 by random and site-directed mutagenesis. J. Biol. Chem. 280 (2005) 41090-41100
    • (2005) J. Biol. Chem. , vol.280 , pp. 41090-41100
    • Wu, Z.L.1
  • 35
    • 0037460184 scopus 로고    scopus 로고
    • Molecular recognition in (+)-alpha-pinene oxidation by cytochrome P450(cam)
    • Bell S.G., et al. Molecular recognition in (+)-alpha-pinene oxidation by cytochrome P450(cam). J. Am. Chem. Soc. 125 (2003) 705-714
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 705-714
    • Bell, S.G.1
  • 38
    • 21244475208 scopus 로고    scopus 로고
    • cam can be engineered to oxidize ethane to ethanol
    • cam can be engineered to oxidize ethane to ethanol. Angew. Chem. Int. Ed. Engl. 44 (2005) 4029-4032
    • (2005) Angew. Chem. Int. Ed. Engl. , vol.44 , pp. 4029-4032
    • Xu, F.1
  • 39
    • 0036842594 scopus 로고    scopus 로고
    • Laboratory evolution of a soluble, self-sufficient, highly active alkane hydroxylase
    • Glieder A., et al. Laboratory evolution of a soluble, self-sufficient, highly active alkane hydroxylase. Nat. Biotechnol. 20 (2002) 1135-1139
    • (2002) Nat. Biotechnol. , vol.20 , pp. 1135-1139
    • Glieder, A.1
  • 40
    • 0242330792 scopus 로고    scopus 로고
    • Regio- and enantioselective alkane hydroxylation with engineered cytochromes P450 BM-3
    • Peters M.W., et al. Regio- and enantioselective alkane hydroxylation with engineered cytochromes P450 BM-3. J. Am. Chem. Soc. 125 (2003) 13442-13450
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13442-13450
    • Peters, M.W.1
  • 41
    • 26944470771 scopus 로고    scopus 로고
    • Direct conversion of ethane to ethanol by engineered cytochrome P450BM3
    • Meinhold P., et al. Direct conversion of ethane to ethanol by engineered cytochrome P450BM3. ChemBioChem 6 (2005) 1765-1768
    • (2005) ChemBioChem , vol.6 , pp. 1765-1768
    • Meinhold, P.1
  • 42
    • 32544456896 scopus 로고    scopus 로고
    • Biotransformation of beta-ionone by engineered cytochrome P450 BM-3
    • Urlacher V.B., et al. Biotransformation of beta-ionone by engineered cytochrome P450 BM-3. Appl. Microbiol. Biotechnol. 70 (2005) 53-59
    • (2005) Appl. Microbiol. Biotechnol. , vol.70 , pp. 53-59
    • Urlacher, V.B.1
  • 43
    • 4043109994 scopus 로고    scopus 로고
    • Functional evolution and structural conservation in chimeric cytochromes p450: calibrating a structure-guided approach
    • Otey C.R., et al. Functional evolution and structural conservation in chimeric cytochromes p450: calibrating a structure-guided approach. Chem. Biol. 11 (2004) 309-318
    • (2004) Chem. Biol. , vol.11 , pp. 309-318
    • Otey, C.R.1
  • 44
    • 7044239768 scopus 로고    scopus 로고
    • Enhancement of 7-methoxyresorufin O-demethylation activity of human cytochrome P450 1A2 by molecular breeding
    • Kim D., and Guengerich F.P. Enhancement of 7-methoxyresorufin O-demethylation activity of human cytochrome P450 1A2 by molecular breeding. Arch. Biochem. Biophys. 432 (2004) 102-108
    • (2004) Arch. Biochem. Biophys. , vol.432 , pp. 102-108
    • Kim, D.1    Guengerich, F.P.2
  • 45
    • 20544450570 scopus 로고    scopus 로고
    • Catalytic hydroxylation in biphasic systems using CYP102A1 mutants
    • Maurer S.C., et al. Catalytic hydroxylation in biphasic systems using CYP102A1 mutants. Adv. Synth. Catal. 347 (2005) 1090-1098
    • (2005) Adv. Synth. Catal. , vol.347 , pp. 1090-1098
    • Maurer, S.C.1
  • 46
    • 0842278671 scopus 로고    scopus 로고
    • Laboratory evolution of cytochrome p450 BM-3 monooxygenase for organic cosolvents
    • Seng Wong T., et al. Laboratory evolution of cytochrome p450 BM-3 monooxygenase for organic cosolvents. Biotechnol. Bioeng. 85 (2004) 351-358
    • (2004) Biotechnol. Bioeng. , vol.85 , pp. 351-358
    • Seng Wong, T.1
  • 47
    • 0141460411 scopus 로고    scopus 로고
    • Thermostabilization of a cytochrome p450 peroxygenase
    • Salazar O., et al. Thermostabilization of a cytochrome p450 peroxygenase. ChemBioChem 4 (2003) 891-893
    • (2003) ChemBioChem , vol.4 , pp. 891-893
    • Salazar, O.1
  • 48
    • 0037157130 scopus 로고    scopus 로고
    • Enhanced electron transfer and lauric acid hydroxylation by site-directed mutagenesis of CYP119
    • Koo L.S., et al. Enhanced electron transfer and lauric acid hydroxylation by site-directed mutagenesis of CYP119. J. Am. Chem. Soc. 124 (2002) 5684-5691
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 5684-5691
    • Koo, L.S.1
  • 49
    • 11144270960 scopus 로고    scopus 로고
    • The Sulfolobus solfataricus electron donor partners of thermophilic CYP119: an unusual non-NAD(P)H-dependent cytochrome P450 system
    • Puchkaev A.V., and Ortiz de Montellano P.R. The Sulfolobus solfataricus electron donor partners of thermophilic CYP119: an unusual non-NAD(P)H-dependent cytochrome P450 system. Arch. Biochem. Biophys. 434 (2005) 169-177
    • (2005) Arch. Biochem. Biophys. , vol.434 , pp. 169-177
    • Puchkaev, A.V.1    Ortiz de Montellano, P.R.2
  • 50
    • 0347927627 scopus 로고    scopus 로고
    • Preliminary characterization and crystal structure of a thermostable cytochrome P450 from Thermus thermophilus
    • Yano J.K., et al. Preliminary characterization and crystal structure of a thermostable cytochrome P450 from Thermus thermophilus. J. Biol. Chem. 278 (2003) 608-616
    • (2003) J. Biol. Chem. , vol.278 , pp. 608-616
    • Yano, J.K.1
  • 51
    • 28144461935 scopus 로고    scopus 로고
    • Reconstitution of beta-carotene hydroxylase activity of thermostable CYP175A1 monooxygenase
    • Momoi K., et al. Reconstitution of beta-carotene hydroxylase activity of thermostable CYP175A1 monooxygenase. Biochem. Biophys. Res. Commun. 339 (2006) 331-336
    • (2006) Biochem. Biophys. Res. Commun. , vol.339 , pp. 331-336
    • Momoi, K.1
  • 52
    • 0033823623 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of a cytochrome P450 (CYP119) from Sulfolobus solfataricus
    • Park S.Y., et al. Crystallization and preliminary X-ray diffraction analysis of a cytochrome P450 (CYP119) from Sulfolobus solfataricus. Acta Crystallogr. D Biol. Crystallogr. 56 (2000) 1173-1175
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , pp. 1173-1175
    • Park, S.Y.1
  • 54
    • 33747691082 scopus 로고    scopus 로고
    • cam monooxygenase system coupled with enzymatic cofactor regeneration. Appl. Microbiol. Biotechnol. DOI 10.1007/s00253-005-0289-y (http://www.springer.com/uk/home?SGWID=3-102-70-1039601-detailsPage=journal|description)
  • 55
    • 0035908212 scopus 로고    scopus 로고
    • Practical, enantiospecific syntheses of 14,15-EET and leukotoxin B (vernolic acid)
    • Falck J.R., et al. Practical, enantiospecific syntheses of 14,15-EET and leukotoxin B (vernolic acid). Tetrahedron Lett. 42 (2001) 4131-4133
    • (2001) Tetrahedron Lett. , vol.42 , pp. 4131-4133
    • Falck, J.R.1
  • 56
    • 0034719132 scopus 로고    scopus 로고
    • Trp-676 facilitates nicotinamide coenzyme exchange in the reductive half-reaction of human cytochrome P450 reductase: properties of the soluble W676H and W676A mutant reductases
    • Gutierrez A., et al. Trp-676 facilitates nicotinamide coenzyme exchange in the reductive half-reaction of human cytochrome P450 reductase: properties of the soluble W676H and W676A mutant reductases. Biochemistry 39 (2000) 15990-15999
    • (2000) Biochemistry , vol.39 , pp. 15990-15999
    • Gutierrez, A.1
  • 57
    • 23844434591 scopus 로고    scopus 로고
    • Switching pyridine nucleotide specificity in P450 BM3: mechanistic analysis of the W1046H and W1046A enzymes
    • Neeli R., et al. Switching pyridine nucleotide specificity in P450 BM3: mechanistic analysis of the W1046H and W1046A enzymes. J. Biol. Chem. 280 (2005) 17634-17644
    • (2005) J. Biol. Chem. , vol.280 , pp. 17634-17644
    • Neeli, R.1
  • 58
    • 0043269709 scopus 로고    scopus 로고
    • A self-sufficient peroxide-driven hydroxylation biocatalyst
    • Cirino P.C., and Arnold F.H. A self-sufficient peroxide-driven hydroxylation biocatalyst. Angew. Chem. Int. Ed. Engl. 42 (2003) 3299-3301
    • (2003) Angew. Chem. Int. Ed. Engl. , vol.42 , pp. 3299-3301
    • Cirino, P.C.1    Arnold, F.H.2
  • 59
    • 0033578095 scopus 로고    scopus 로고
    • Laboratory evolution of peroxide-mediated cytochrome P450 hydroxylation
    • Joo H., et al. Laboratory evolution of peroxide-mediated cytochrome P450 hydroxylation. Nature 399 (1999) 670-673
    • (1999) Nature , vol.399 , pp. 670-673
    • Joo, H.1
  • 61
    • 0034727799 scopus 로고    scopus 로고
    • P450 in biotechnology: zinc-driven omega-hydroxylation of p-nitrophenoxydodecanoic acid using P450 BM-3 F87A as a catalyst
    • Schwaneberg U., et al. P450 in biotechnology: zinc-driven omega-hydroxylation of p-nitrophenoxydodecanoic acid using P450 BM-3 F87A as a catalyst. J. Biotechnol. 84 (2000) 249-257
    • (2000) J. Biotechnol. , vol.84 , pp. 249-257
    • Schwaneberg, U.1
  • 62
    • 0035856545 scopus 로고    scopus 로고
    • Pivotal role of water in the mechanism of P450BM-3
    • Haines D.C., et al. Pivotal role of water in the mechanism of P450BM-3. Biochemistry 40 (2001) 13456-13465
    • (2001) Biochemistry , vol.40 , pp. 13456-13465
    • Haines, D.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.