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Volumn 279, Issue 9, 2012, Pages 1650-1662

Cloning, expression and characterization of CYP102D1, a self-sufficient P450 monooxygenase from Streptomyces avermitilis

Author keywords

CYP102D1; cytochrome P450 monooxygenases; isoflavone; ortho specific hydroxylation; self sufficient P450

Indexed keywords

CYTOCHROME P450 102D1; CYTOCHROME P450 BM3; CYTOCHROME P450 REDUCTASE; DAIDZEIN; FATTY ACID; MYRISTOLEIC ACID; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

EID: 84862806452     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08462.x     Document Type: Article
Times cited : (45)

References (39)
  • 1
    • 0001045385 scopus 로고
    • A new cytochrome in liver michromes
    • Omura T, &, Sato R, (1962) A new cytochrome in liver michromes. J Biol Chem 237, 1375-1376.
    • (1962) J Biol Chem , vol.237 , pp. 1375-1376
    • Omura, T.1    Sato, R.2
  • 2
    • 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
  • 3
    • 33744520321 scopus 로고    scopus 로고
    • Cytochromes P450 as versatile biocatalysts
    • DOI 10.1016/j.jbiotec.2006.01.026, PII S016816560600085X
    • Bernhardt R, (2006) Cytochromes P450 as versatile biocatalysts. J Biotechnol 124, 128-145. (Pubitemid 43816140)
    • (2006) Journal of Biotechnology , vol.124 , Issue.1 , pp. 128-145
    • Bernhardt, R.1
  • 4
    • 0036898132 scopus 로고    scopus 로고
    • Biotransformations using prokaryotic P450 monooxygenases
    • DOI 10.1016/S0958-1669(02)00357-9
    • Urlacher VB, &, Schmid RD, (2002) Biotransformations using prokaryotic P450 monooxygenases: review article. Curr Opin Biotechnol 13, 557-564. (Pubitemid 35448056)
    • (2002) Current Opinion in Biotechnology , vol.13 , Issue.6 , pp. 557-564
    • Urlacher, V.1    Schmid, R.D.2
  • 5
    • 78650008114 scopus 로고    scopus 로고
    • Towards practical Baeyer-Villiger-monooxygenases: Design of cyclohexanone monooxygenase mutants with enhanced oxidative stability
    • Opperman DJ, &, Reetz MT, (2010) Towards practical Baeyer-Villiger-monooxygenases: design of cyclohexanone monooxygenase mutants with enhanced oxidative stability. Chembiochem 11, 2589-2596.
    • (2010) Chembiochem , vol.11 , pp. 2589-2596
    • Opperman, D.J.1    Reetz, M.T.2
  • 6
  • 7
    • 79952268861 scopus 로고    scopus 로고
    • Cytochromes P450 as useful biocatalysts: Addressing the limitations
    • O'Reilly E, Kohler V, Flitsch SL, &, Turner NJ, (2011) Cytochromes P450 as useful biocatalysts: addressing the limitations. Chem Commun (Camb) 47, 2490-2501.
    • (2011) Chem Commun (Camb) , vol.47 , pp. 2490-2501
    • O'Reilly, E.1    Kohler, V.2    Flitsch, S.L.3    Turner, N.J.4
  • 8
    • 33748366369 scopus 로고    scopus 로고
    • Engineering human cytochrome P450 enzymes into catalytically self-sufficient chimeras using molecular Lego
    • DOI 10.1007/s00775-006-0144-3
    • Dodhia VR, Fantuzzi A, &, Gilardi G, (2006) Engineering human cytochrome P450 enzymes into catalytically self-sufficient chimeras using molecular Lego. J Biol Inorg Chem 11, 903-916. (Pubitemid 44337591)
    • (2006) Journal of Biological Inorganic Chemistry , vol.11 , Issue.7 , pp. 903-916
    • Dodhia, V.R.1    Fantuzzi, A.2    Gilardi, G.3
  • 11
    • 0042819974 scopus 로고    scopus 로고
    • Electron transfer in flavocytochrome P450 BM3: Kinetics of flavin reduction and oxidation, the role of cysteine 999, and relationships with mammalian cytochrome P450 reductase
    • DOI 10.1021/bi034562h
    • Roitel O, Scrutton NS, &, Munro AW, (2003) Electron transfer in flavocytochrome P450 BM3: kinetics of flavin reduction and oxidation, the role of cysteine 999, and relationships with mammalian cytochrome P450 reductase. Biochemistry 42, 10809-10821. (Pubitemid 37102121)
    • (2003) Biochemistry , vol.42 , Issue.36 , pp. 10809-10821
    • Roitel, O.1    Scrutton, N.S.2    Munro, A.W.3
  • 12
    • 77955168936 scopus 로고    scopus 로고
    • Molecular assembly of P450 with ferredoxin and ferredoxin reductase by fusion to PCNA
    • Hirakawa H, &, Nagamune T, (2010) Molecular assembly of P450 with ferredoxin and ferredoxin reductase by fusion to PCNA. Chembiochem 11, 1517-1520.
    • (2010) Chembiochem , vol.11 , pp. 1517-1520
    • Hirakawa, H.1    Nagamune, T.2
  • 13
    • 40649086027 scopus 로고    scopus 로고
    • Electrochemistry of cytochrome P450 enzyme on nanoparticle-containing membrane-coated electrode and its applications for drug sensing
    • Liu S, Peng L, Yang X, Wu Y, &, He L, (2008) Electrochemistry of cytochrome P450 enzyme on nanoparticle-containing membrane-coated electrode and its applications for drug sensing. Anal Biochem 375, 209-216.
    • (2008) Anal Biochem , vol.375 , pp. 209-216
    • Liu, S.1    Peng, L.2    Yang, X.3    Wu, Y.4    He, L.5
  • 14
    • 11244302709 scopus 로고    scopus 로고
    • Cloning, expression and characterisation of CYP102A2, a self-sufficient P450 monooxygenase from Bacillus subtilis
    • DOI 10.1007/s00253-004-1719-y
    • Budde M, Morr M, Schmid RD, &, Urlacher VB, (2004) Cloning, expression and characterisation of CYP102A2, a self-sufficient P450 monooxygenase from Bacillus subtilis. Appl Microbiol Biotechnol 66, 180-186. (Pubitemid 40064312)
    • (2004) Applied Microbiology and Biotechnology , vol.66 , Issue.2 , pp. 180-186
    • Budde, M.1    Maurer, S.C.2    Schmid, R.D.3    Urlacher, V.B.4
  • 15
    • 33646806119 scopus 로고    scopus 로고
    • Selective hydroxylation of highly branched fatty acids and their derivatives by CYP102A1 from Bacillus megaterium
    • DOI 10.1002/cbic.200500444
    • Budde M, Morr M, Schmid RD, &, Urlacher VB, (2006) Selective hydroxylation of highly branched fatty acids and their derivatives by CYP102A1 from Bacillus megaterium. Chembiochem 7, 789-794. (Pubitemid 43764188)
    • (2006) ChemBioChem , vol.7 , Issue.5 , pp. 789-794
    • Budde, M.1    Morr, M.2    Schmid, R.D.3    Urlacher, V.B.4
  • 16
    • 36049044576 scopus 로고    scopus 로고
    • Cloning, expression and characterization of a fast self-sufficient P450: CYP102A5 from Bacillus cereus
    • DOI 10.1016/j.abb.2007.09.010, PII S0003986107004675
    • Chowdhary PK, Alemseqhed M, &, Haines DC, (2007) Cloning, expression and characterization of a fast self-sufficient P450: CYP102A5 from Bacillus cereus. Arch Biochem Biophys 468, 32-43. (Pubitemid 350087848)
    • (2007) Archives of Biochemistry and Biophysics , vol.468 , Issue.1 , pp. 32-43
    • Chowdhary, P.K.1    Alemseghed, M.2    Haines, D.C.3
  • 17
    • 46149102464 scopus 로고    scopus 로고
    • Cloning, expression and characterisation of CYP102A7, a self-sufficient P450 monooxygenase from Bacillus licheniformis
    • Dietrich M, Eiben S, Asta C, Do TA, Pleiss J, &, Urlacher VB, (2008) Cloning, expression and characterisation of CYP102A7, a self-sufficient P450 monooxygenase from Bacillus licheniformis. Appl Microbiol Biotechnol 79, 931-940.
    • (2008) Appl Microbiol Biotechnol , vol.79 , pp. 931-940
    • Dietrich, M.1    Eiben, S.2    Asta, C.3    Do, T.A.4    Pleiss, J.5    Urlacher, V.B.6
  • 18
    • 2442552990 scopus 로고    scopus 로고
    • Expression, Purification, and Characterization of Bacillus subtilis Cytochromes P450 CYP102A2 and CYP102A3: Flavocytochrome Homologues of P450 BM3 from Bacillus megaterium
    • DOI 10.1021/bi035904m
    • Gustafsson MC, Roitel O, Marshall KR, Noble MA, Chapman SK, Pessegueiro A, Fulco AJ, Cheesman MR, von Wachenfeldt C, &, Munro AW, (2004) Expression, purification, and characterization of Bacillus subtilis cytochromes P450 CYP102A2 and CYP102A3: flavocytochrome homologues of P450 BM3 from Bacillus megaterium. Biochemistry 43, 5474-5487. (Pubitemid 38620939)
    • (2004) Biochemistry , vol.43 , Issue.18 , pp. 5474-5487
    • Gustafsson, M.C.U.1    Roitel, O.2    Marshall, K.R.3    Noble, M.A.4    Chapman, S.K.5    Pessegueiro, A.6    Fulco, A.J.7    Cheesman, M.R.8    Von Wachenfeldt, C.9    Munro, A.W.10
  • 22
    • 0036844477 scopus 로고    scopus 로고
    • A novel class of self-sufficient cytochrome P450 monooxygenases in prokaryotes
    • DOI 10.1016/S0966-842X(02)02458-7, PII S0966842X02024587
    • De Mot R, &, Parret AH, (2002) A novel class of self-sufficient cytochrome P450 monooxygenases in prokaryotes. Trends Microbiol 10, 502-508. (Pubitemid 35284796)
    • (2002) Trends in Microbiology , vol.10 , Issue.11 , pp. 502-508
    • De Mot, R.1    Parret, A.H.A.2
  • 23
    • 51349101082 scopus 로고    scopus 로고
    • Ortho-Dihydroxyisoflavone derivatives from aged Doenjang (Korean fermented soypaste) and its radical scavenging activity
    • Park JS, Park HY, Kim DH, Kim DH, &, Kim HK, (2008) ortho-Dihydroxyisoflavone derivatives from aged Doenjang (Korean fermented soypaste) and its radical scavenging activity. Bioorg Med Chem Lett 18, 5006-5009.
    • (2008) Bioorg Med Chem Lett , vol.18 , pp. 5006-5009
    • Park, J.S.1    Park, H.Y.2    Kim, D.H.3    Kim, D.H.4    Kim, H.K.5
  • 24
    • 0034827198 scopus 로고    scopus 로고
    • Synthesis, electrophilic substitution and structure-activity relationship studies of polycyclic aromatic compounds towards the development of anticancer agents
    • Banik BK, &, Becker FF, (2001) Synthesis, electrophilic substitution and structure-activity relationship studies of polycyclic aromatic compounds towards the development of anticancer agents. Curr Med Chem 8, 1513-1533. (Pubitemid 32894013)
    • (2001) Current Medicinal Chemistry , vol.8 , Issue.12 , pp. 1513-1533
    • Banik, B.K.1    Becker, F.F.2
  • 25
    • 18044383127 scopus 로고    scopus 로고
    • Engineering the substrate specificity of cytochrome P450 CYP102A2 by directed evolution: Production of an efficient enzyme for bioconversion of fine chemicals
    • DOI 10.1016/j.bioeng.2004.11.003, Directed Enzyme Evolution
    • Axarli I, Prigipaki A, &, Labrou NE, (2005) Engineering the substrate specificity of cytochrome P450 CYP102A2 by directed evolution: production of an efficient enzyme for bioconversion of fine chemicals. Biomol Eng 22, 81-88. (Pubitemid 40602597)
    • (2005) Biomolecular Engineering , vol.22 , Issue.1-3 , pp. 81-88
    • Axarli, I.1    Prigipaki, A.2    Labrou, N.E.3
  • 27
    • 40749104246 scopus 로고    scopus 로고
    • Cytochrome P450 BM-3 evolved by random and saturation mutagenesis as an effective indole-hydroxylating catalyst
    • DOI 10.1007/s12010-007-8002-5
    • Li HM, Mei LH, Urlacher VB, &, Schmid RD, (2008) Cytochrome P450 BM-3 evolved by random and saturation mutagenesis as an effective indole-hydroxylating catalyst. Appl Biochem Biotechnol 144, 27-36. (Pubitemid 351378028)
    • (2008) Applied Biochemistry and Biotechnology , vol.144 , Issue.1 , pp. 27-36
    • Li, H.-M.1    Mei, L.-H.2    Urlacher, V.B.3    Schmid, R.D.4
  • 28
    • 0034819837 scopus 로고    scopus 로고
    • Protein engineering of Bacillus megaterium CYP102: The oxidation of polycyclic aromatic hydrocarbons
    • DOI 10.1046/j.1432-1327.2001.02212.x
    • Carmichael AB, &, Wong LL, (2001) Protein engineering of Bacillus megaterium CYP102. The oxidation of polycyclic aromatic hydrocarbons. Eur J Biochem 268, 3117-3125. (Pubitemid 32862999)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.10 , pp. 3117-3125
    • Carmichael, A.B.1    Wong, L.-L.2
  • 29
    • 44549086314 scopus 로고    scopus 로고
    • The effect of mutation of F87 on the properties of CYP102A1-CYP4C7 chimeras: Altered regiospecificity and substrate selectivity
    • Chen CK, Shokhireva T, Berry RE, Zhang H, &, Walker FA, (2008) The effect of mutation of F87 on the properties of CYP102A1-CYP4C7 chimeras: altered regiospecificity and substrate selectivity. J Biol Inorg Chem 13, 813-824.
    • (2008) J Biol Inorg Chem , vol.13 , pp. 813-824
    • Chen, C.K.1    Shokhireva, T.2    Berry, R.E.3    Zhang, H.4    Walker, F.A.5
  • 32
    • 77950941685 scopus 로고    scopus 로고
    • Engineering bacterial cytochrome P450 (P450) BM3 into a prototype with human P450 enzyme activity using indigo formation
    • Park SH, Kim DH, Kim D, Kim DH, Jung HC, Pan JG, Ahn T, Kim D, &, Yun CH, (2010) Engineering bacterial cytochrome P450 (P450) BM3 into a prototype with human P450 enzyme activity using indigo formation. Drug Metab Dispos 38, 732-739.
    • (2010) Drug Metab Dispos , vol.38 , pp. 732-739
    • Park, S.H.1    Kim, D.H.2    Kim, D.3    Kim, D.H.4    Jung, H.C.5    Pan, J.G.6    Ahn, T.7    Kim, D.8    Yun, C.H.9
  • 33
    • 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, 853-861.
    • (2009) Chembiochem , vol.10 , 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
  • 34
    • 0029892430 scopus 로고    scopus 로고
    • Cytochrome P450foxy, a catalytically self-sufficient fatty acid hydroxylase of the fungus Fusarium oxysporum
    • Nakayama N, Takemae A, &, Shoun H, (1996) Cytochrome P450foxy, a catalytically self-sufficient fatty acid hydroxylase of the fungus Fusarium oxysporum. J Biochem 119, 435-443.
    • (1996) J Biochem , vol.119 , pp. 435-443
    • Nakayama, N.1    Takemae, A.2    Shoun, H.3
  • 35
    • 33749161882 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of a self-sufficient cytochrome P450 monooxygenase from Rhodococcus ruber DSM 44319
    • DOI 10.1007/s00253-006-0355-0
    • Liu L, Schmid RD, &, Urlacher VB, (2006) Cloning, expression, and characterization of a self-sufficient cytochrome P450 monoxygenases from Rhodococcus ruber DSM 44319. Appl Microbiol Biotechnol 72, 876-882. (Pubitemid 44477363)
    • (2006) Applied Microbiology and Biotechnology , vol.72 , Issue.5 , pp. 876-882
    • Liu, L.1    Schmid, R.D.2    Urlacher, V.B.3
  • 36
    • 0022878676 scopus 로고
    • Characterization of a catalytically self-sufficient 119,000-dalton cytochrome P-450 monooxygenase induced by barbiturates in Bacillus megaterium
    • Narhi LO, &, Fulco AJ, (1986) Characterization of a catalytically self-sufficient 119,000-dalton cytochrome P-450 monooxygenase induced by barbiturates in Bacillus megaterium. J Biol Chem 261, 7160-7169. (Pubitemid 17224707)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.16 , pp. 7160-7169
    • Narhi, L.O.1    Fulco, A.J.2
  • 37
    • 0037027817 scopus 로고    scopus 로고
    • Production of cytidine 5'-monophosphate N-acetylneuraminic acid using recombinant Escherichia coli as a biocatalyst
    • Lee SG, Lee JO, Yi JK, &, Kim BG, (2002) Production of cytidine 5'-monophosphate N-acetylneuraminic acid using recombinant Escherichia coli as a biocatalyst. Biotechnol Bioeng 80, 516-524.
    • (2002) Biotechnol Bioeng , vol.80 , pp. 516-524
    • Lee, S.G.1    Lee, J.O.2    Yi, J.K.3    Kim, B.G.4
  • 38
    • 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


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