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Volumn 36, Issue 6, 2014, Pages 1329-1333

Bioreduction and disproportionation of cyclohex-2-enone catalyzed by ene-reductase OYE-1 in 'micro-aqueous' organic solvents

Author keywords

Bioreduction; Cyclohex 2 enone; Cyclohexanone; Disproportionation; Ene reductase; Micro aqueous systems; Old yellow enzyme; Phenol

Indexed keywords

CATALYSIS; ENZYMES; PHENOLS;

EID: 84899940988     PISSN: 01415492     EISSN: 15736776     Source Type: Journal    
DOI: 10.1007/s10529-014-1494-5     Document Type: Article
Times cited : (16)

References (28)
  • 1
    • 76649087954 scopus 로고    scopus 로고
    • Biocatalysis with thermostable enzymes: structure and properties of a thermophilic 'ene'-reductase related to Old Yellow Enzyme
    • Adalbjörnsson BV, Toogood HS, Fryszkowska A, Pudney CR, Jowitt TA, Leys D, Scrutton NS (2010) Biocatalysis with thermostable enzymes: structure and properties of a thermophilic 'ene'-reductase related to Old Yellow Enzyme. ChemBioChem 11: 197-207.
    • (2010) ChemBioChem , vol.11 , pp. 197-207
    • Adalbjörnsson, B.V.1    Toogood, H.S.2    Fryszkowska, A.3    Pudney, C.R.4    Jowitt, T.A.5    Leys, D.6    Scrutton, N.S.7
  • 2
    • 79953318587 scopus 로고    scopus 로고
    • Status of protein engineering for biocatalysts: how to design an industrially useful biocatalyst
    • Bommarius AS, Blum JK, Abrahamson MJ (2011) Status of protein engineering for biocatalysts: how to design an industrially useful biocatalyst. Curr Opin Chem Biol 15: 194-200.
    • (2011) Curr Opin Chem Biol , vol.15 , pp. 194-200
    • Bommarius, A.S.1    Blum, J.K.2    Abrahamson, M.J.3
  • 3
    • 78149432876 scopus 로고    scopus 로고
    • Towards preparative-scale, biocatalytic alkene reductions
    • Bougioukou DJ, Walton AZ, Stewart JD (2010) Towards preparative-scale, biocatalytic alkene reductions. Chem Commun 46: 8558-8560.
    • (2010) Chem Commun , vol.46 , pp. 8558-8560
    • Bougioukou, D.J.1    Walton, A.Z.2    Stewart, J.D.3
  • 4
    • 0032484145 scopus 로고    scopus 로고
    • On the active site of old yellow enzyme. Role of histidine 191 and asparagine 194
    • Brown BJ, Deng Z, Karplus PA, Massey V (1998) On the active site of old yellow enzyme. Role of histidine 191 and asparagine 194. J Biol Chem 273: 32753-32762.
    • (1998) J Biol Chem , vol.273 , pp. 32753-32762
    • Brown, B.J.1    Deng, Z.2    Karplus, P.A.3    Massey, V.4
  • 5
    • 0041152088 scopus 로고    scopus 로고
    • Properties and synthetic applications of enzymes in organic solvents
    • Carrea G, Riva S (2000) Properties and synthetic applications of enzymes in organic solvents. Angew Chem Int Ed 39: 2226-2254.
    • (2000) Angew Chem Int Ed , vol.39 , pp. 2226-2254
    • Carrea, G.1    Riva, S.2
  • 6
    • 34250679762 scopus 로고    scopus 로고
    • Enzymatic reduction of ketones in "micro-aqueous" media catalyzed by ADH-A from Rhodococcus ruber
    • de Gonzalo G, Lavandera I, Faber K, Kroutil K (2007) Enzymatic reduction of ketones in "micro-aqueous" media catalyzed by ADH-A from Rhodococcus ruber. Org Lett 9: 2163-2166.
    • (2007) Org Lett , vol.9 , pp. 2163-2166
    • de Gonzalo, G.1    Lavandera, I.2    Faber, K.3    Kroutil, K.4
  • 7
    • 0024655878 scopus 로고
    • Enzymatic catalysis in monophasic organic solvents
    • Dordick JS (1989) Enzymatic catalysis in monophasic organic solvents. Enzyme Microb Technol 11: 194-211.
    • (1989) Enzyme Microb Technol , vol.11 , pp. 194-211
    • Dordick, J.S.1
  • 8
    • 33845374385 scopus 로고
    • Asymmetric oxidoreductions catalyzed by alcohol dehydrogenase in organic solvents
    • Grunwald J, Wirz B, Scollar MP, Klibanov AM (1986) Asymmetric oxidoreductions catalyzed by alcohol dehydrogenase in organic solvents. J Am Chem Soc 108: 6732-6734.
    • (1986) J Am Chem Soc , vol.108 , pp. 6732-6734
    • Grunwald, J.1    Wirz, B.2    Scollar, M.P.3    Klibanov, A.M.4
  • 9
    • 3042807068 scopus 로고    scopus 로고
    • Enzymes in organic media: forms, functions and applications
    • Gupta MN, Roy I (2004) Enzymes in organic media: forms, functions and applications. Eur J Biochem 271: 2575-2583.
    • (2004) Eur J Biochem , vol.271 , pp. 2575-2583
    • Gupta, M.N.1    Roy, I.2
  • 10
    • 53849094459 scopus 로고    scopus 로고
    • Asymmetric bioreduction of activated C=C bonds using Zymomonas mobilis NCR enoate reductase and old yellow enzymes OYE 1-3 from yeasts
    • Hall M, Stueckler C, Hauer B, Stuermer R, Friedrich T, Breuer M, Kroutil W, Faber K (2008) Asymmetric bioreduction of activated C=C bonds using Zymomonas mobilis NCR enoate reductase and old yellow enzymes OYE 1-3 from yeasts. Eur J Org Chem 9: 1511-1516.
    • (2008) Eur J Org Chem , vol.9 , pp. 1511-1516
    • Hall, M.1    Stueckler, C.2    Hauer, B.3    Stuermer, R.4    Friedrich, T.5    Breuer, M.6    Kroutil, W.7    Faber, K.8
  • 11
    • 34047189417 scopus 로고    scopus 로고
    • Asymmetric bioreduction of activated C=C bonds using enoate reductases from the old yellow enzyme family
    • Hauer B, Stuermer R, Hall M, Faber K (2007) Asymmetric bioreduction of activated C=C bonds using enoate reductases from the old yellow enzyme family. Curr Opin Chem Biol 11: 203-213.
    • (2007) Curr Opin Chem Biol , vol.11 , pp. 203-213
    • Hauer, B.1    Stuermer, R.2    Hall, M.3    Faber, K.4
  • 14
    • 0032483986 scopus 로고    scopus 로고
    • The oxidative half-reaction of Old Yellow Enzyme: the role of tyrosine 196
    • Kohli RM, Massey V (1998) The oxidative half-reaction of Old Yellow Enzyme: the role of tyrosine 196. J Biol Chem 273: 32763-32770.
    • (1998) J Biol Chem , vol.273 , pp. 32763-32770
    • Kohli, R.M.1    Massey, V.2
  • 15
    • 70350509060 scopus 로고    scopus 로고
    • Ionic liquids as performance additives for electroenzymatic syntheses
    • Kohlmann C, Greiner L, Leitner W, Wandrey C, Lütz S (2009) Ionic liquids as performance additives for electroenzymatic syntheses. Chem Eur J 15: 11692-11700.
    • (2009) Chem Eur J , vol.15 , pp. 11692-11700
    • Kohlmann, C.1    Greiner, L.2    Leitner, W.3    Wandrey, C.4    Lütz, S.5
  • 17
    • 0027112225 scopus 로고
    • Reductive biotransformation by wild type and mutant strains of Saccharomyces cerevisiae in aqueous-organic solvent biphasic systems
    • Nikolova P, Ward OP (1992) Reductive biotransformation by wild type and mutant strains of Saccharomyces cerevisiae in aqueous-organic solvent biphasic systems. Biotechnol Bioeng 39: 870-876.
    • (1992) Biotechnol Bioeng , vol.39 , pp. 870-876
    • Nikolova, P.1    Ward, O.P.2
  • 18
    • 82755197021 scopus 로고    scopus 로고
    • +-reducing soluble [NiFe]-hydrogenase from Ralstonia eutropha H16 through modification with methoxy-poly(ethylene) glycol
    • +-reducing soluble [NiFe]-hydrogenase from Ralstonia eutropha H16 through modification with methoxy-poly(ethylene) glycol. J Mol Catal B Enzym 74: 219-223.
    • (2012) J Mol Catal B Enzym , vol.74 , pp. 219-223
    • Ratzka, J.1    Lauterbach, L.2    Lenz, O.3    Ansorge-Schumacher, M.B.4
  • 20
    • 37349126715 scopus 로고    scopus 로고
    • Enzyme activation for organic solvents made easy
    • Serdakowski AL, Dordick JS (2008) Enzyme activation for organic solvents made easy. Trends Biotechnol 26: 48-54.
    • (2008) Trends Biotechnol , vol.26 , pp. 48-54
    • Serdakowski, A.L.1    Dordick, J.S.2
  • 21
    • 9944235432 scopus 로고    scopus 로고
    • Asymmetric reduction of 2-substituted 2-butenolides with reductase from Marchantia polymorpha
    • Shimoda K, Kubota N (2004) Asymmetric reduction of 2-substituted 2-butenolides with reductase from Marchantia polymorpha. Tetrahedron Asymmetry 15: 3827-3829.
    • (2004) Tetrahedron Asymmetry , vol.15 , pp. 3827-3829
    • Shimoda, K.1    Kubota, N.2
  • 23
    • 77956316535 scopus 로고    scopus 로고
    • Bioreduction of α-methylcinnamaldehyde derivatives: chemo-enzymatic asymmetric synthesis of Lilial and Helional
    • Stueckler C, Mueller NJ, Winkler CK, Glueck SM, Gruber K, Steinkellner G, Faber K (2010a) Bioreduction of α-methylcinnamaldehyde derivatives: chemo-enzymatic asymmetric synthesis of Lilial and Helional. Dalton Trans 39: 8472-8476.
    • (2010) Dalton Trans , vol.39 , pp. 8472-8476
    • Stueckler, C.1    Mueller, N.J.2    Winkler, C.K.3    Glueck, S.M.4    Gruber, K.5    Steinkellner, G.6    Faber, K.7
  • 24
    • 71649109063 scopus 로고    scopus 로고
    • Nicotinamide-independent asymmetric bioreduction of C=C-bonds via disproportionation of enones catalyzed by enoate reductases
    • Stueckler C, Reiter TC, Baudendistel N, Faber K (2010b) Nicotinamide-independent asymmetric bioreduction of C=C-bonds via disproportionation of enones catalyzed by enoate reductases. Tetrahedron 66: 663-667.
    • (2010) Tetrahedron , vol.66 , pp. 663-667
    • Stueckler, C.1    Reiter, T.C.2    Baudendistel, N.3    Faber, K.4
  • 25
    • 78149436277 scopus 로고    scopus 로고
    • Biocatalytic reductions and chemical versatility of the Old Yellow Enzyme family of flavoprotein oxidoreductases
    • Toogood HS, Gardiner JM, Scrutton NS (2010) Biocatalytic reductions and chemical versatility of the Old Yellow Enzyme family of flavoprotein oxidoreductases. ChemCatChem 11: 892-914.
    • (2010) ChemCatChem , vol.11 , pp. 892-914
    • Toogood, H.S.1    Gardiner, J.M.2    Scrutton, N.S.3
  • 26
    • 0042808596 scopus 로고    scopus 로고
    • Is logP a convenient criterion to guide the choice of solvents for biphasic enzymatic reactions?
    • Villela Filho M, Stillger T, Müller M, Liese A, Wandrey C (2003) Is logP a convenient criterion to guide the choice of solvents for biphasic enzymatic reactions? Angew Chem Int Ed 42: 2993-2996.
    • (2003) Angew Chem Int Ed , vol.42 , pp. 2993-2996
    • Villela Filho, M.1    Stillger, T.2    Müller, M.3    Liese, A.4    Wandrey, C.5
  • 27
    • 84886293347 scopus 로고    scopus 로고
    • Overcoming co-product inhibition in the nicotinamide independent asymmetric bioreduction of activated C=C-bonds using flavin-dependent ene-reductases
    • Winkler CK, Clay D, van Heerden E, Faber K (2013) Overcoming co-product inhibition in the nicotinamide independent asymmetric bioreduction of activated C=C-bonds using flavin-dependent ene-reductases. Biotechnol Bioeng 110: 3085-3092.
    • (2013) Biotechnol Bioeng , vol.110 , pp. 3085-3092
    • Winkler, C.K.1    Clay, D.2    van Heerden, E.3    Faber, K.4
  • 28
    • 79956148088 scopus 로고    scopus 로고
    • Asymmetric bioreduction of alkenes using ene-reductases YersER and KYE1 and effects of organic solvents
    • Yanto Y, Winkler CK, Lohr S, Hall M, Faber K, Bommarius AS (2011) Asymmetric bioreduction of alkenes using ene-reductases YersER and KYE1 and effects of organic solvents. Org Lett 13: 2540-2543.
    • (2011) Org Lett , vol.13 , pp. 2540-2543
    • Yanto, Y.1    Winkler, C.K.2    Lohr, S.3    Hall, M.4    Faber, K.5    Bommarius, A.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.