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Volumn 74, Issue 1, 2007, Pages 99-106

Cloning, sequencing, and expression of a novel epoxide hydrolase gene from Rhodococcus opacus in Escherichia coli and characterization of enzyme

Author keywords

Characterization; Cloning; Epoxide hydrolase; Prokaryotic expression; Rhodococcus opacus ML 0004

Indexed keywords

EPOXIDE HYDROLASE; PROKARYOTIC EXPRESSION; RHODOCOCCUS OPACUS ML-0004;

EID: 33846580455     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-006-0635-8     Document Type: Article
Times cited : (42)

References (34)
  • 1
    • 0033570996 scopus 로고    scopus 로고
    • Cloning and molecular characterization of a soluble epoxide hydrolase from Aspergillus niger that is related to mammalian microsomal epoxide hydrolase
    • Arand M, Hemmer H, Durk H, Baratti J, Archelas A, Furstoss R, Oesch F (1999) Cloning and molecular characterization of a soluble epoxide hydrolase from Aspergillus niger that is related to mammalian microsomal epoxide hydrolase. Biochem J 344:273-280
    • (1999) Biochem J , vol.344 , pp. 273-280
    • Arand, M.1    Hemmer, H.2    Durk, H.3    Baratti, J.4    Archelas, A.5    Furstoss, R.6    Oesch, F.7
  • 2
    • 0035313421 scopus 로고    scopus 로고
    • Synthetic applications of epoxide hydrolases
    • Archelas A, Furstoss R (2001) Synthetic applications of epoxide hydrolases. Curr Opin Chem Biol 5:112-119
    • (2001) Curr Opin Chem Biol , vol.5 , pp. 112-119
    • Archelas, A.1    Furstoss, R.2
  • 3
    • 0029040624 scopus 로고
    • Stereocontrolled hydrolysis of the linoleic acid monoepoxide regioisomers catalyzed by soybean epoxide hydrolase
    • Blée E, Schuber F (1995) Stereocontrolled hydrolysis of the linoleic acid monoepoxide regioisomers catalyzed by soybean epoxide hydrolase. Eur J Biochem 230:229-234
    • (1995) Eur J Biochem , vol.230 , pp. 229-234
    • Blée, E.1    Schuber, F.2
  • 4
    • 0032768820 scopus 로고    scopus 로고
    • Affinity purification and characterization of a yeast epoxide hydrolase
    • Botes AL (1999) Affinity purification and characterization of a yeast epoxide hydrolase. Biotechnol Lett 21:511-517
    • (1999) Biotechnol Lett , vol.21 , pp. 511-517
    • Botes, A.L.1
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0001341659 scopus 로고
    • Identification of organic acids on paper chromatograms
    • Buch ML, Montgomery R, Porter WL (1952) Identification of organic acids on paper chromatograms. Anal Chem 24:489-491
    • (1952) Anal Chem , vol.24 , pp. 489-491
    • Buch, M.L.1    Montgomery, R.2    Porter, W.L.3
  • 7
    • 9944263454 scopus 로고    scopus 로고
    • Immobilization of a whole-cell epoxide-hydrolyzing biocatalyst in sodium alginate-cellulose sulfate-poly(methylene-co-guanidine) capsules using a controlled encapsulation process
    • Bučko M, Vikartovska A, Lacik I, Kollarikova G, Gemeiner P, Patoprsty V, Brygin M (2005) Immobilization of a whole-cell epoxide-hydrolyzing biocatalyst in sodium alginate-cellulose sulfate-poly(methylene-co-guanidine) capsules using a controlled encapsulation process. Enzyme Microb Technol 36:118-126
    • (2005) Enzyme Microb Technol , vol.36 , pp. 118-126
    • Bučko, M.1    Vikartovska, A.2    Lacik, I.3    Kollarikova, G.4    Gemeiner, P.5    Patoprsty, V.6    Brygin, M.7
  • 8
    • 0024558335 scopus 로고
    • One-step preparation of competent Escherichia coli: Transformation and storage of bacterial cells in the same solution
    • Chung CT, Niemela SL, Miller RH (1989) One-step preparation of competent Escherichia coli: transformation and storage of bacterial cells in the same solution. Proc Natl Acad Sci USA 86:2172-2175
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 2172-2175
    • Chung, C.T.1    Niemela, S.L.2    Miller, R.H.3
  • 11
    • 0030222084 scopus 로고    scopus 로고
    • Novel aliphatic epoxide hydrolase activities from dematiaceous fungi
    • Grogan G, Roberts SM, Willetts AJ (1996) Novel aliphatic epoxide hydrolase activities from dematiaceous fungi. FEMS Microbiol Lett 141:239-243
    • (1996) FEMS Microbiol Lett , vol.141 , pp. 239-243
    • Grogan, G.1    Roberts, S.M.2    Willetts, A.J.3
  • 14
    • 33846608477 scopus 로고    scopus 로고
    • Kamatani Y, Ogino K (1977) Production of L, tartaric acid. US Patent 4,011,135
    • Kamatani Y, Ogino K (1977) Production of L(+)-tartaric acid. US Patent 4,011,135
  • 15
    • 4444276636 scopus 로고
    • For an alternative approach to the synthesis of optically active 1,2-diols
    • Kolb HC, Van Nieuwenhze MS, Sharpless KB (1994) For an alternative approach to the synthesis of optically active 1,2-diols. Chem Rev 94:2483-2547
    • (1994) Chem Rev , vol.94 , pp. 2483-2547
    • Kolb, H.C.1    Van Nieuwenhze, M.S.2    Sharpless, K.B.3
  • 16
    • 0032522192 scopus 로고    scopus 로고
    • Purification and characterization of a highly selective epoxide hydrolase from Nocardia sp. EH1
    • Kroutil W, Genzel Y, Pietzsch M, Syldatk C, Faber K (1998) Purification and characterization of a highly selective epoxide hydrolase from Nocardia sp. EH1. J Biotechnol 61:143-150
    • (1998) J Biotechnol , vol.61 , pp. 143-150
    • Kroutil, W.1    Genzel, Y.2    Pietzsch, M.3    Syldatk, C.4    Faber, K.5
  • 17
    • 0034093824 scopus 로고    scopus 로고
    • Kurillová L', Gemeiner P, Vikartovská A, Miková H, Rosenberg M, Ilavský M (2000) Calcium pectate gel beads for cell entrapment. 6. Morphology of stabilized and hardened calcium pectate gel beads with cells for immobilized biotechnology. J Microencapsul 17:279-296
    • Kurillová L', Gemeiner P, Vikartovská A, Miková H, Rosenberg M, Ilavský M (2000) Calcium pectate gel beads for cell entrapment. 6. Morphology of stabilized and hardened calcium pectate gel beads with cells for immobilized biotechnology. J Microencapsul 17:279-296
  • 18
    • 3142660254 scopus 로고    scopus 로고
    • Cloning and sequencing of an epoxide hydrolase gene from Rhodosporidium paludigenum
    • Labuschagne M, Botes AL, Albertyn J (2004) Cloning and sequencing of an epoxide hydrolase gene from Rhodosporidium paludigenum. DNA Seq 15:202-205
    • (2004) DNA Seq , vol.15 , pp. 202-205
    • Labuschagne, M.1    Botes, A.L.2    Albertyn, J.3
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of bacteriphoge T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of bacteriphoge T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 33846644266 scopus 로고
    • Microbiological process for preparing L-tartaric acid in presence of surfactants
    • US Patent 4,017,362
    • Miura Y, Yutani K, Takesue H, Fujii K (1977) Microbiological process for preparing L-tartaric acid in presence of surfactants. US Patent 4,017,362
    • (1977)
    • Miura, Y.1    Yutani, K.2    Takesue, H.3    Fujii, K.4
  • 23
    • 0033565356 scopus 로고    scopus 로고
    • Purification and characterization of a highly enantioselective epoxide hydrolase from Aspergillus niger
    • Morisseau C, Archelas A, Guitton C, Faucher D, Furstoss P, Baratti JC (1999) Purification and characterization of a highly enantioselective epoxide hydrolase from Aspergillus niger. Eur J Biochem 263:386-395
    • (1999) Eur J Biochem , vol.263 , pp. 386-395
    • Morisseau, C.1    Archelas, A.2    Guitton, C.3    Faucher, D.4    Furstoss, P.5    Baratti, J.C.6
  • 24
    • 0031016293 scopus 로고    scopus 로고
    • Biocatalytic resolution of 2-methyl-2-(aryl)alkyloxiranes using novel bacterial epoxide hydrolases
    • Osprian I, Kroutil W, Mischitz M, Faber K (1997) Biocatalytic resolution of 2-methyl-2-(aryl)alkyloxiranes using novel bacterial epoxide hydrolases. Tetrahedron: Asymmetry 8:65-71
    • (1997) Tetrahedron: Asymmetry , vol.8 , pp. 65-71
    • Osprian, I.1    Kroutil, W.2    Mischitz, M.3    Faber, K.4
  • 25
    • 0032813366 scopus 로고    scopus 로고
    • Production of L-tartaric acid by immobilized bacterial cells Nocardia tartaricans
    • Rosenberg M, Miková H, Krištofíkova L' (1999) Production of L-tartaric acid by immobilized bacterial cells Nocardia tartaricans. Biotechnol Lett 21:491-495
    • (1999) Biotechnol Lett , vol.21 , pp. 491-495
    • Rosenberg, M.1    Miková, H.2    L', K.3
  • 26
    • 22144457118 scopus 로고    scopus 로고
    • Protein engineering of epoxide hydrolase from Agrobacterium radiobacter AD1 for enhanced activity and enantioselective production of (R)-1-phenylethane-1,2-diol
    • Rui LY, Cao L, Chen W, Reardon KF, Wood TK (2005) Protein engineering of epoxide hydrolase from Agrobacterium radiobacter AD1 for enhanced activity and enantioselective production of (R)-1-phenylethane-1,2-diol. Appl Environ Microb 71:3995-4003
    • (2005) Appl Environ Microb , vol.71 , pp. 3995-4003
    • Rui, L.Y.1    Cao, L.2    Chen, W.3    Reardon, K.F.4    Wood, T.K.5
  • 28
    • 0035710814 scopus 로고    scopus 로고
    • Microbial epoxide hydroxylases for preparative biotransformations
    • Steinreiber A, Faber K (2001) Microbial epoxide hydroxylases for preparative biotransformations. Curr Opin Biotechnol 12:552-558
    • (2001) Curr Opin Biotechnol , vol.12 , pp. 552-558
    • Steinreiber, A.1    Faber, K.2
  • 29
    • 3342911436 scopus 로고    scopus 로고
    • Directed evolution of epoxide hydrolase from A-radiobacter toward higher enantioselectivity by error-prone PCR and DNA shuffling
    • van Loo B, Spelberg JHL, Kingma J, Sonke T, Wubbolts MG, Janssen DB (2004) Directed evolution of epoxide hydrolase from A-radiobacter toward higher enantioselectivity by error-prone PCR and DNA shuffling. Chem Biol 11:981-990
    • (2004) Chem Biol , vol.11 , pp. 981-990
    • van Loo, B.1    Spelberg, J.H.L.2    Kingma, J.3    Sonke, T.4    Wubbolts, M.G.5    Janssen, D.B.6
  • 30
    • 0032708907 scopus 로고    scopus 로고
    • Isolation and characterization of the epoxide hydrolase-encoding gene from Xanthophyllomyces dendrorhous
    • Visser H, De Bont JAM, Verdoes JC (1999) Isolation and characterization of the epoxide hydrolase-encoding gene from Xanthophyllomyces dendrorhous. Appl Microbiol Biotechnol 65:5459-5463
    • (1999) Appl Microbiol Biotechnol , vol.65 , pp. 5459-5463
    • Visser, H.1    De Bont, J.A.M.2    Verdoes, J.C.3
  • 31
    • 0034011922 scopus 로고    scopus 로고
    • Cloning and characterization of an epoxide hydrolase-encoding gene from Rhodotorula glutinis
    • Visser H, Vreugdenhil S, de Bont JAM, Verdoes JC (2000) Cloning and characterization of an epoxide hydrolase-encoding gene from Rhodotorula glutinis. Appl Microbiol Biotechnol 53:415-419
    • (2000) Appl Microbiol Biotechnol , vol.53 , pp. 415-419
    • Visser, H.1    Vreugdenhil, S.2    de Bont, J.A.M.3    Verdoes, J.C.4
  • 32
    • 0033545515 scopus 로고    scopus 로고
    • Epoxide hydrolases from yeasts and other sources: Versatile tools in biocatalysis
    • Weijers CAGM, de Bont JAM (1999) Epoxide hydrolases from yeasts and other sources: versatile tools in biocatalysis. J Mol Catal B 6:199-214
    • (1999) J Mol Catal B , vol.6 , pp. 199-214
    • Weijers, C.A.G.M.1    de Bont, J.A.M.2
  • 33
    • 0034154094 scopus 로고    scopus 로고
    • Production of L(+)-tartaric acid by immobilized Corynebacterium sp. JZ-1
    • Zhang JG, Qian YJ (2000) Production of L(+)-tartaric acid by immobilized Corynebacterium sp. JZ-1. Chin J Biotechnol 16:188-192
    • (2000) Chin J Biotechnol , vol.16 , pp. 188-192
    • Zhang, J.G.1    Qian, Y.J.2


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