메뉴 건너뛰기




Volumn 98, Issue 19, 2014, Pages 8191-8200

Engineering class I cytochrome P450 by gene fusion with NADPH-dependent reductase and S. avermitilis host development for daidzein biotransformation

Author keywords

Cytochrome P450; Daidzein; Fusion enzyme; Redox partner; S. avermitilis host

Indexed keywords

CATALYSIS; EFFICIENCY; ELECTRON TRANSITIONS; ENZYMES; HYDROXYLATION; PORPHYRINS;

EID: 84920253529     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-014-5706-7     Document Type: Article
Times cited : (32)

References (45)
  • 1
    • 18844381164 scopus 로고    scopus 로고
    • Minireview: cellular redox state regulates hydroxysteroid dehydrogenase activity and intracellular hormone potency
    • PID: 15774561, COI: 1:CAS:528:DC%2BD2MXksleitbo%3D
    • Agarwal AK, Auchus RJ (2005) Minireview: cellular redox state regulates hydroxysteroid dehydrogenase activity and intracellular hormone potency. Endocrinology 146(6):2531–2538
    • (2005) Endocrinology , vol.146 , Issue.6 , pp. 2531-2538
    • Agarwal, A.K.1    Auchus, R.J.2
  • 2
    • 77950891988 scopus 로고    scopus 로고
    • Importance of NADPH supply for improved L-valine formation in Corynebacterium glutamicum
    • PID: 20014412, COI: 1:CAS:528:DC%2BC3cXlsVSnsrs%3D
    • Bartek T, Blombach B, Zonnchen E, Makus P, Lang S, Eikmanns BJ, Oldiges M (2010) Importance of NADPH supply for improved L-valine formation in Corynebacterium glutamicum. Biotechnol Prog 26(2):361–371
    • (2010) Biotechnol Prog , vol.26 , Issue.2 , pp. 361-371
    • Bartek, T.1    Blombach, B.2    Zonnchen, E.3    Makus, P.4    Lang, S.5    Eikmanns, B.J.6    Oldiges, M.7
  • 3
    • 33744520321 scopus 로고    scopus 로고
    • Cytochromes P450 as versatile biocatalysts
    • PID: 16516322, COI: 1:CAS:528:DC%2BD28Xltl2isLw%3D
    • 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
  • 4
    • 77954141406 scopus 로고    scopus 로고
    • Redox biocatalysis and metabolism: molecular mechanisms and metabolic network analysis
    • PID: 20059399, COI: 1:CAS:528:DC%2BC3cXnvV2ku70%3D
    • Blank LM, Ebert BE, Buehler K, Buhler B (2010) Redox biocatalysis and metabolism: molecular mechanisms and metabolic network analysis. Antioxid Redox Signal 13(3):349–394
    • (2010) Antioxid Redox Signal , vol.13 , Issue.3 , pp. 349-394
    • Blank, L.M.1    Ebert, B.E.2    Buehler, K.3    Buhler, B.4
  • 5
    • 11244302709 scopus 로고    scopus 로고
    • Cloning, expression and characterisation of CYP102A2, a self-sufficient P450 monooxygenase from Bacillus subtilis
    • PID: 15375636, COI: 1:CAS:528:DC%2BD2cXpvFKlsbk%3D
    • Budde M, Maurer SC, Schmid RD, Urlacher VB (2004) Cloning, expression and characterisation of CYP102A2, a self-sufficient P450 monooxygenase from Bacillus subtilis. Appl Microbiol Biotechnol 66(2):180–186
    • (2004) Appl Microbiol Biotechnol , vol.66 , Issue.2 , pp. 180-186
    • Budde, M.1    Maurer, S.C.2    Schmid, R.D.3    Urlacher, V.B.4
  • 6
    • 40549093298 scopus 로고    scopus 로고
    • NADH availability limits asymmetric biocatalytic epoxidation in a growing recombinant Escherichia coli strain
    • PID: 18192422
    • Buhler B, Park JB, Blank LM, Schmid A (2008) NADH availability limits asymmetric biocatalytic epoxidation in a growing recombinant Escherichia coli strain. Appl Environ Microbiol 74(5):1436–1446
    • (2008) Appl Environ Microbiol , vol.74 , Issue.5 , pp. 1436-1446
    • Buhler, B.1    Park, J.B.2    Blank, L.M.3    Schmid, A.4
  • 7
    • 79954423939 scopus 로고    scopus 로고
    • Improved NADPH supply for xylitol production by engineered Escherichia coli with glycolytic mutations
    • PID: 21344680, COI: 1:CAS:528:DC%2BC3MXls1Gis7g%3D
    • Chin JW, Cirino PC (2011) Improved NADPH supply for xylitol production by engineered Escherichia coli with glycolytic mutations. Biotechnol Prog 27(2):333–341
    • (2011) Biotechnol Prog , vol.27 , Issue.2 , pp. 333-341
    • Chin, J.W.1    Cirino, P.C.2
  • 8
    • 58149238062 scopus 로고    scopus 로고
    • Analysis of NADPH supply during xylitol production by engineered Escherichia coli
    • PID: 18698648, COI: 1:CAS:528:DC%2BD1MXitlWk
    • Chin JW, Khankal R, Monroe CA, Maranas CD, Cirino PC (2009) Analysis of NADPH supply during xylitol production by engineered Escherichia coli. Biotechnol Bioeng 102(1):209–220
    • (2009) Biotechnol Bioeng , vol.102 , Issue.1 , pp. 209-220
    • Chin, J.W.1    Khankal, R.2    Monroe, C.A.3    Maranas, C.D.4    Cirino, P.C.5
  • 10
    • 84862806452 scopus 로고    scopus 로고
    • Cloning, expression and characterization of CYP102D1, a self-sufficient P450 monooxygenase from Streptomyces avermitilis
    • PID: 22188665, COI: 1:CAS:528:DC%2BC38XmvFegs7s%3D
    • Choi KY, Jung E, Jung DH, Pandey BP, Yun H, Park HY, Kazlauskas RJ, Kim BG (2012b) Cloning, expression and characterization of CYP102D1, a self-sufficient P450 monooxygenase from Streptomyces avermitilis. FEBS J 279(9):1650–1662
    • (2012) FEBS J , vol.279 , Issue.9 , pp. 1650-1662
    • Choi, K.Y.1    Jung, E.2    Jung, D.H.3    Pandey, B.P.4    Yun, H.5    Park, H.Y.6    Kazlauskas, R.J.7    Kim, B.G.8
  • 11
    • 73449085517 scopus 로고    scopus 로고
    • A-ring ortho-specific monohydroxylation of daidzein by cytochrome P450s of Nocardia farcinica IFM10152
    • PID: 19918785, COI: 1:CAS:528:DC%2BD1MXhsVKnsbnN
    • Choi KY, Kim TJ, Koh SK, Roh CH, Pandey BP, Lee N, Kim BG (2009) A-ring ortho-specific monohydroxylation of daidzein by cytochrome P450s of Nocardia farcinica IFM10152. Biotechnol J 4(11):1586–1595
    • (2009) Biotechnol J , vol.4 , Issue.11 , pp. 1586-1595
    • Choi, K.Y.1    Kim, T.J.2    Koh, S.K.3    Roh, C.H.4    Pandey, B.P.5    Lee, N.6    Kim, B.G.7
  • 12
    • 36049044576 scopus 로고    scopus 로고
    • Cloning, expression and characterization of a fast self-sufficient P450: CYP102A5 from Bacillus cereus
    • PID: 17945181, COI: 1:CAS:528:DC%2BD2sXhtlajsLzN
    • Chowdhary PK, Alemseghed M, Haines DC (2007) Cloning, expression and characterization of a fast self-sufficient P450: CYP102A5 from Bacillus cereus. Arch Biochem Biophys 468(1):32–43
    • (2007) Arch Biochem Biophys , vol.468 , Issue.1 , pp. 32-43
    • Chowdhary, P.K.1    Alemseghed, M.2    Haines, D.C.3
  • 13
    • 0036844477 scopus 로고    scopus 로고
    • A novel class of self-sufficient cytochrome P450 monooxygenases in prokaryotes
    • PID: 12419614
    • De Mot R, Parret AH (2002) A novel class of self-sufficient cytochrome P450 monooxygenases in prokaryotes. Trends Microbiol 10(11):502–508
    • (2002) Trends Microbiol , vol.10 , Issue.11 , pp. 502-508
    • De Mot, R.1    Parret, A.H.2
  • 14
    • 46149102464 scopus 로고    scopus 로고
    • Cloning, expression and characterisation of CYP102A7, a self-sufficient P450 monooxygenase from Bacillus licheniformis
    • PID: 18483737, COI: 1:CAS:528:DC%2BD1cXnslKgsLY%3D
    • 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(6):931–940
    • (2008) Appl Microbiol Biotechnol , vol.79 , Issue.6 , pp. 931-940
    • Dietrich, M.1    Eiben, S.2    Asta, C.3    Do, T.A.4    Pleiss, J.5    Urlacher, V.B.6
  • 15
    • 33748366369 scopus 로고    scopus 로고
    • Engineering human cytochrome P450 enzymes into catalytically self-sufficient chimeras using molecular Lego
    • PID: 16862439, COI: 1:CAS:528:DC%2BD28XptVWrt74%3D
    • 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(7):903–916
    • (2006) J Biol Inorg Chem , vol.11 , Issue.7 , pp. 903-916
    • Dodhia, V.R.1    Fantuzzi, A.2    Gilardi, G.3
  • 16
    • 36148958632 scopus 로고    scopus 로고
    • Engineered alkane-hydroxylating cytochrome P450(BM3) exhibiting nativelike catalytic properties
    • PID: 17886313, COI: 1:CAS:528:DC%2BD2sXhtlOks77E
    • Fasan R, Chen MM, Crook NC, Arnold FH (2007) Engineered alkane-hydroxylating cytochrome P450(BM3) exhibiting nativelike catalytic properties. Angew Chem Int Ed Engl 46(44):8414–8418
    • (2007) Angew Chem Int Ed Engl , vol.46 , Issue.44 , pp. 8414-8418
    • Fasan, R.1    Chen, M.M.2    Crook, N.C.3    Arnold, F.H.4
  • 17
    • 78751476638 scopus 로고    scopus 로고
    • Improved product-per-glucose yields in P450-dependent propane biotransformations using engineered Escherichia coli
    • PID: 21246504, COI: 1:CAS:528:DC%2BC3MXmsVOmsA%3D%3D
    • Fasan R, Crook NC, Peters MW, Meinhold P, Buelter T, Landwehr M, Cirino PC, Arnold FH (2011) Improved product-per-glucose yields in P450-dependent propane biotransformations using engineered Escherichia coli. Biotechnol Bioeng 108(3):500–510
    • (2011) Biotechnol Bioeng , vol.108 , Issue.3 , pp. 500-510
    • Fasan, R.1    Crook, N.C.2    Peters, M.W.3    Meinhold, P.4    Buelter, T.5    Landwehr, M.6    Cirino, P.C.7    Arnold, F.H.8
  • 18
    • 33846958772 scopus 로고    scopus 로고
    • Structural and spectroscopic characterization of P450 BM3 mutants with unprecedented P450 heme iron ligand sets. New heme ligation states influence conformational equilibria in P450 BM3
    • PID: 17077084, COI: 1:CAS:528:DC%2BD2sXkslai
    • Girvan HM, Seward HE, Toogood HS, Cheesman MR, Leys D, Munro AW (2007) Structural and spectroscopic characterization of P450 BM3 mutants with unprecedented P450 heme iron ligand sets. New heme ligation states influence conformational equilibria in P450 BM3. J Biol Chem 282(1):564–572
    • (2007) J Biol Chem , vol.282 , Issue.1 , pp. 564-572
    • Girvan, H.M.1    Seward, H.E.2    Toogood, H.S.3    Cheesman, M.R.4    Leys, D.5    Munro, A.W.6
  • 19
    • 0035001145 scopus 로고    scopus 로고
    • Evaluation of hepatic subcellular fractions for Alamar blue and MTT reductase activity
    • PID: 11377098, COI: 1:CAS:528:DC%2BD3MXjslSitrk%3D
    • Gonzalez RJ, Tarloff JB (2001) Evaluation of hepatic subcellular fractions for Alamar blue and MTT reductase activity. Toxicol In Vitro 15(3):257–259
    • (2001) Toxicol In Vitro , vol.15 , Issue.3 , pp. 257-259
    • Gonzalez, R.J.1    Tarloff, J.B.2
  • 20
    • 65349173511 scopus 로고    scopus 로고
    • Synthesis of various kinds of isoflavones, isoflavanes, and biphenyl-ketones and their 1,1-diphenyl-2-picrylhydrazyl radical-scavenging activities
    • COI: 1:CAS:528:DC%2BD1MXmtl2gt7g%3D
    • Goto H, Terao Y, Akai S (2009) Synthesis of various kinds of isoflavones, isoflavanes, and biphenyl-ketones and their 1,1-diphenyl-2-picrylhydrazyl radical-scavenging activities. Chem Pharm Bull (Tokyo) 57(4):346–360
    • (2009) Chem Pharm Bull (Tokyo) , vol.57 , Issue.4 , pp. 346-360
    • Goto, H.1    Terao, Y.2    Akai, S.3
  • 21
    • 79953297687 scopus 로고    scopus 로고
    • Cytochromes P450: exploiting diversity and enabling application as biocatalysts
    • PID: 21145278, COI: 1:CAS:528:DC%2BC3MXksFKnt7k%3D
    • 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
  • 22
    • 84883535579 scopus 로고    scopus 로고
    • Fine tuning of spatial arrangement of enzymes in a PCNA-mediated multienzyme complex using a rigid poly-L-proline linker
    • PID: 24040392, COI: 1:CAS:528:DC%2BC3sXhsVGiu73E
    • Haga T, Hirakawa H, Nagamune T (2013) Fine tuning of spatial arrangement of enzymes in a PCNA-mediated multienzyme complex using a rigid poly-L-proline linker. PLoS ONE 8(9):e75114
    • (2013) PLoS ONE , vol.8 , Issue.9 , pp. e75114
    • Haga, T.1    Hirakawa, H.2    Nagamune, T.3
  • 23
    • 33846473252 scopus 로고    scopus 로고
    • Cytochrome P450 systems—biological variations of electron transport chains
    • PID: 16978787, COI: 1:CAS:528:DC%2BD2sXpvVyqtg%3D%3D
    • Hannemann F, Bichet A, Ewen KM, 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.M.3    Bernhardt, R.4
  • 24
    • 33646408415 scopus 로고    scopus 로고
    • Enhanced clavulanic acid production in Streptomyces clavuligerus NRRL3585 by overexpression of regulatory genes
    • COI: 1:CAS:528:DC%2BD28Xks1Ojuro%3D
    • Hung TV, Ishida K, Parajuli N, Liou K, Lee HC, Sohng JK (2006) Enhanced clavulanic acid production in Streptomyces clavuligerus NRRL3585 by overexpression of regulatory genes. Biotechnol Bioproc Eng 11(2):116–120
    • (2006) Biotechnol Bioproc Eng , vol.11 , Issue.2 , pp. 116-120
    • Hung, T.V.1    Ishida, K.2    Parajuli, N.3    Liou, K.4    Lee, H.C.5    Sohng, J.K.6
  • 26
    • 80052135332 scopus 로고    scopus 로고
    • Regio- and stereoselectivity of P450-catalysed hydroxylation of steroids controlled by laboratory evolution
    • PID: 21860465, COI: 1:CAS:528:DC%2BC3MXhtVars7rL
    • 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(9):738–743
    • (2011) Nat Chem , vol.3 , Issue.9 , pp. 738-743
    • Kille, S.1    Zilly, F.E.2    Acevedo, J.P.3    Reetz, M.T.4
  • 27
    • 0042672547 scopus 로고    scopus 로고
    • Cytochrome p450 complement (CYPome) of the avermectin-producer Streptomyces avermitilis and comparison to that of Streptomyces coelicolor A3(2)
    • PID: 12893267, COI: 1:CAS:528:DC%2BD3sXlvVCrs7k%3D
    • Lamb DC, Ikeda H, Nelson DR, Ishikawa J, Skaug T, Jackson C, Omura S, Waterman MR, Kelly SL (2003) Cytochrome p450 complement (CYPome) of the avermectin-producer Streptomyces avermitilis and comparison to that of Streptomyces coelicolor A3(2). Biochem Biophys Res Commun 307(3):610–619
    • (2003) Biochem Biophys Res Commun , vol.307 , Issue.3 , pp. 610-619
    • Lamb, D.C.1    Ikeda, H.2    Nelson, D.R.3    Ishikawa, J.4    Skaug, T.5    Jackson, C.6    Omura, S.7    Waterman, M.R.8    Kelly, S.L.9
  • 28
    • 84876674407 scopus 로고    scopus 로고
    • Engineering of NADPH regenerators in Escherichia coli for enhanced biotransformation
    • PID: 23420268, COI: 1:CAS:528:DC%2BC3sXkt1Kis7s%3D
    • Lee WH, Kim MD, Jin YS, Seo JH (2013) Engineering of NADPH regenerators in Escherichia coli for enhanced biotransformation. Appl Microbiol Biotechnol 97(7):2761–2772
    • (2013) Appl Microbiol Biotechnol , vol.97 , Issue.7 , pp. 2761-2772
    • Lee, W.H.1    Kim, M.D.2    Jin, Y.S.3    Seo, J.H.4
  • 29
    • 37349117637 scopus 로고    scopus 로고
    • Cytochrome P450/redox partner fusion enzymes: biotechnological and toxicological prospects
    • PID: 18028029, COI: 1:CAS:528:DC%2BD2sXhtlCls7fP
    • McLean KJ, Girvan HM, Munro AW (2007) Cytochrome P450/redox partner fusion enzymes: biotechnological and toxicological prospects. Expert Opin Drug Metab Toxicol 3(6):847–863
    • (2007) Expert Opin Drug Metab Toxicol , vol.3 , Issue.6 , pp. 847-863
    • McLean, K.J.1    Girvan, H.M.2    Munro, A.W.3
  • 31
    • 33846356640 scopus 로고    scopus 로고
    • Cytochrome P450—redox partner fusion enzymes
    • PID: 17023115, COI: 1:CAS:528:DC%2BD2sXpvVyqtw%3D%3D
    • Munro AW, Girvan HM, McLean KJ (2007) Cytochrome P450—redox partner fusion enzymes. Biochim Biophys Acta 1770(3):345–359
    • (2007) Biochim Biophys Acta , vol.1770 , Issue.3 , pp. 345-359
    • Munro, A.W.1    Girvan, H.M.2    McLean, K.J.3
  • 32
    • 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(9):2490–2501
    • (2011) Chem Commun (Camb) , vol.47 , Issue.9 , pp. 2490-2501
    • O’Reilly, E.1    Kohler, V.2    Flitsch, S.L.3    Turner, N.J.4
  • 33
    • 50449100139 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. II. Solubilization, purification, and properties
    • PID: 14209972, COI: 1:CAS:528:DyaF2cXktF2gur8%3D
    • Omura T, Sato R (1964) The carbon monoxide-binding pigment of liver microsomes. II. Solubilization, purification, and properties. J Biol Chem 239:2379–2385
    • (1964) J Biol Chem , vol.239 , pp. 2379-2385
    • Omura, T.1    Sato, R.2
  • 34
    • 33646753362 scopus 로고    scopus 로고
    • Structure-guided recombination creates an artificial family of cytochromes P450
    • PID: 16594730
    • Otey CR, Landwehr M, Endelman JB, Hiraga K, Bloom JD, Arnold FH (2006) Structure-guided recombination creates an artificial family of cytochromes P450. PLoS Biol 4(5):e112
    • (2006) PLoS Biol , vol.4 , Issue.5 , pp. e112
    • Otey, C.R.1    Landwehr, M.2    Endelman, J.B.3    Hiraga, K.4    Bloom, J.D.5    Arnold, F.H.6
  • 35
    • 77449114845 scopus 로고    scopus 로고
    • Regioselective hydroxylation of daidzein using P450 (CYP105D7) from Streptomyces avermitilis MA4680
    • PID: 19845003, COI: 1:CAS:528:DC%2BC3cXhtVKjt78%3D
    • Pandey BP, Roh C, Choi KY, Lee N, Kim EJ, Ko S, Kim T, Yun H, Kim BG (2010) Regioselective hydroxylation of daidzein using P450 (CYP105D7) from Streptomyces avermitilis MA4680. Biotechnol Bioeng 105(4):697–704
    • (2010) Biotechnol Bioeng , vol.105 , Issue.4 , pp. 697-704
    • Pandey, B.P.1    Roh, C.2    Choi, K.Y.3    Lee, N.4    Kim, E.J.5    Ko, S.6    Kim, T.7    Yun, H.8    Kim, B.G.9
  • 36
    • 74049104179 scopus 로고    scopus 로고
    • Natural ortho-dihydroxyisoflavone derivatives from aged Korean fermented soybean paste as potent tyrosinase and melanin formation inhibitors
    • PID: 20022495, COI: 1:CAS:528:DC%2BC3cXhtVGrtr0%3D
    • Park JS, Kim DH, Lee JK, Lee JY, Kim HK, Lee HJ, Kim HC (2010) Natural ortho-dihydroxyisoflavone derivatives from aged Korean fermented soybean paste as potent tyrosinase and melanin formation inhibitors. Bioorg Med Chem Lett 20(3):1162–1164
    • (2010) Bioorg Med Chem Lett , vol.20 , Issue.3 , pp. 1162-1164
    • Park, J.S.1    Kim, D.H.2    Lee, J.K.3    Lee, J.Y.4    Kim, H.K.5    Lee, H.J.6    Kim, H.C.7
  • 37
    • 51349101082 scopus 로고    scopus 로고
    • Ortho-dihydroxyisoflavone derivatives from aged Doenjang (Korean fermented soypaste) and its radical scavenging activity
    • PID: 18722771, COI: 1:CAS:528:DC%2BD1cXhtFelsrrI
    • Park JS, Park HY, Kim DH, Kim HK (2008) Ortho-dihydroxyisoflavone derivatives from aged Doenjang (Korean fermented soypaste) and its radical scavenging activity. Bioorg Med Chem Lett 18(18):5006–5009
    • (2008) Bioorg Med Chem Lett , vol.18 , Issue.18 , pp. 5006-5009
    • Park, J.S.1    Park, H.Y.2    Kim, D.H.3    Kim, H.K.4
  • 38
    • 0242330792 scopus 로고    scopus 로고
    • Regio- and enantioselective alkane hydroxylation with engineered cytochromes P450 BM-3
    • PID: 14583039, COI: 1:CAS:528:DC%2BD3sXnvFOitrc%3D
    • Peters MW, Meinhold P, Glieder A, Arnold FH (2003) Regio- and enantioselective alkane hydroxylation with engineered cytochromes P450 BM-3. J Am Chem Soc 125(44):13442–13450
    • (2003) J Am Chem Soc , vol.125 , Issue.44 , pp. 13442-13450
    • Peters, M.W.1    Meinhold, P.2    Glieder, A.3    Arnold, F.H.4
  • 40
    • 84874048801 scopus 로고    scopus 로고
    • Chimeric P450 enzymes: activity of artificial redox fusions driven by different reductases for biotechnological applications
    • PID: 23586997, COI: 1:CAS:528:DC%2BC3sXjtVCqtbc%3D
    • Sadeghi SJGG (2013) Chimeric P450 enzymes: activity of artificial redox fusions driven by different reductases for biotechnological applications. Biotechnol Appl Biochem 60(1):102–110
    • (2013) Biotechnol Appl Biochem , vol.60 , Issue.1 , pp. 102-110
    • Sadeghi, S.J.G.G.1
  • 41
    • 84871197071 scopus 로고    scopus 로고
    • A gene-fusion approach to enabling plant cytochromes p450 for biocatalysis
    • PID: 23129550
    • Schuckel J, Rylott EL, Grogan G, Bruce NC (2012) A gene-fusion approach to enabling plant cytochromes p450 for biocatalysis. Chembiochem 13(18):2758–2763
    • (2012) Chembiochem , vol.13 , Issue.18 , pp. 2758-2763
    • Schuckel, J.1    Rylott, E.L.2    Grogan, G.3    Bruce, N.C.4
  • 42
    • 33747885449 scopus 로고    scopus 로고
    • A screening system for the directed evolution of epoxygenases: importance of position 184 in P450 BM3 for stereoselective styrene epoxidation
    • PID: 16847856, COI: 1:CAS:528:DC%2BD28Xosleltb0%3D
    • Tee KL, Schwaneberg U (2006) A screening system for the directed evolution of epoxygenases: importance of position 184 in P450 BM3 for stereoselective styrene epoxidation. Angew Chem Int Ed Engl 45(32):5380–5383
    • (2006) Angew Chem Int Ed Engl , vol.45 , Issue.32 , pp. 5380-5383
    • Tee, K.L.1    Schwaneberg, U.2
  • 43
    • 33745652737 scopus 로고    scopus 로고
    • Cytochrome P450 monooxygenases: perspectives for synthetic application
    • PID: 16759725, COI: 1:CAS:528:DC%2BD28XmslyltL8%3D
    • Urlacher VB, Eiben S (2006) Cytochrome P450 monooxygenases: perspectives for synthetic application. Trends Biotechnol 24(7):324–330
    • (2006) Trends Biotechnol , vol.24 , Issue.7 , pp. 324-330
    • Urlacher, V.B.1    Eiben, S.2
  • 44
    • 37549068090 scopus 로고    scopus 로고
    • +/NADPH in cellular functions and cell death: regulation and biological consequences
    • +/NADPH in cellular functions and cell death: regulation and biological consequences. Antioxid Redox Signal 10(2):179–206
    • (2008) Antioxid Redox Signal , vol.10 , Issue.2 , pp. 179-206
    • Ying, W.1
  • 45
    • 79956120945 scopus 로고    scopus 로고
    • Synthesis of optically pure S-sulfoxide by Escherichia coli transformant cells coexpressing the P450 monooxygenase and glucose dehydrogenase genes
    • Zhang JD, Li AT, Yu HL, Imanaka T, Xu JH (2011) Synthesis of optically pure S-sulfoxide by Escherichia coli transformant cells coexpressing the P450 monooxygenase and glucose dehydrogenase genes. J Ind Microbiol Biotechnol 38(5):633–641
    • (2011) J Ind Microbiol Biotechnol , vol.38 , Issue.5 , pp. 633-641
    • Zhang, J.D.1    Li, A.T.2    Yu, H.L.3    Imanaka, T.4    Xu, J.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.