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Volumn 102, Issue 14, 2011, Pages 7023-7028

Highly efficient synthesis of chiral alcohols with a novel NADH-dependent reductase from Streptomyces coelicolor

Author keywords

Asymmetric reduction; Carbonyl reductase; Ethyl (S) 4 chloro 3 hydroxybutanoate; NADH regeneration; Streptomyces coelicolor

Indexed keywords

ASYMMETRIC REDUCTION; CARBONYL REDUCTASE; ETHYL (S)-4-CHLORO-3-HYDROXYBUTANOATE; NADH REGENERATION; STREPTOMYCES COELICOLOR;

EID: 79957851192     PISSN: 09608524     EISSN: 18732976     Source Type: Journal    
DOI: 10.1016/j.biortech.2011.04.046     Document Type: Article
Times cited : (146)

References (34)
  • 1
    • 0141483145 scopus 로고    scopus 로고
    • Cloning, sequence analysis, and heterologous expression of the gene encoding a (S)-specific alcohol dehydrogenase from Rhodococcus erythropolis DSM 43297
    • Abokitse K., Hummel W. Cloning, sequence analysis, and heterologous expression of the gene encoding a (S)-specific alcohol dehydrogenase from Rhodococcus erythropolis DSM 43297. Appl. Microbiol. Biotechnol. 2003, 62:380-386.
    • (2003) Appl. Microbiol. Biotechnol. , vol.62 , pp. 380-386
    • Abokitse, K.1    Hummel, W.2
  • 2
    • 69249220127 scopus 로고    scopus 로고
    • Biocatalytic production of (S)-4-bromo-3-hydroxybutyrate and structurally related chemicals and their applications
    • Asako H., Shimizu M., Itoh N. Biocatalytic production of (S)-4-bromo-3-hydroxybutyrate and structurally related chemicals and their applications. Appl. Microbiol. Biotechnol. 2009, 84:397-405.
    • (2009) Appl. Microbiol. Biotechnol. , vol.84 , pp. 397-405
    • Asako, H.1    Shimizu, M.2    Itoh, N.3
  • 3
    • 0032564708 scopus 로고    scopus 로고
    • Baker's yeast: production of d- and l-3-hydroxy esters
    • Dahl A.C., Madsen J.Ø. Baker's yeast: production of d- and l-3-hydroxy esters. Tetrahedron: Asymmetry 1998, 9:4395-4417.
    • (1998) Tetrahedron: Asymmetry , vol.9 , pp. 4395-4417
    • Dahl, A.C.1    Madsen, J.Ø.2
  • 4
    • 53849122329 scopus 로고    scopus 로고
    • Highly efficient chemoenzymatic synthesis of methyl (R)-o-chloromandelate, a key intermediate for clopidogrel, via asymmetric reduction with recombinant Escherichia coli
    • Ema T., Ide S., Okita N., Sakai T. Highly efficient chemoenzymatic synthesis of methyl (R)-o-chloromandelate, a key intermediate for clopidogrel, via asymmetric reduction with recombinant Escherichia coli. Adv. Synth. Catal. 2008, 350:2039-2044.
    • (2008) Adv. Synth. Catal. , vol.350 , pp. 2039-2044
    • Ema, T.1    Ide, S.2    Okita, N.3    Sakai, T.4
  • 5
    • 33748416168 scopus 로고    scopus 로고
    • Overcoming the thermodynamic limitation in asymmetric hydrogen transfer reactions catalyzed by whole cells
    • Goldberg K., Edegger K., Kroutil W., Liese A. Overcoming the thermodynamic limitation in asymmetric hydrogen transfer reactions catalyzed by whole cells. Biotechnol. Bioeng. 2006, 95:192-198.
    • (2006) Biotechnol. Bioeng. , vol.95 , pp. 192-198
    • Goldberg, K.1    Edegger, K.2    Kroutil, W.3    Liese, A.4
  • 6
    • 34547137887 scopus 로고    scopus 로고
    • Biocatalytic ketone reduction - a powerful tool for the production of chiral alcohols - part II: whole-cell reductions
    • Goldberg K., Schroer K., Lütz S., Liese A. Biocatalytic ketone reduction - a powerful tool for the production of chiral alcohols - part II: whole-cell reductions. Appl. Microbiol. Biotechnol. 2007, 76:249-255.
    • (2007) Appl. Microbiol. Biotechnol. , vol.76 , pp. 249-255
    • Goldberg, K.1    Schroer, K.2    Lütz, S.3    Liese, A.4
  • 7
    • 34547127384 scopus 로고    scopus 로고
    • Biocatalytic ketone reduction - a powerful tool for the production of chiral alcohols - part I: processes with isolated enzymes
    • Goldberg K., Schroer K., Lütz S., Liese A. Biocatalytic ketone reduction - a powerful tool for the production of chiral alcohols - part I: processes with isolated enzymes. Appl. Microbiol. Biotechnol. 2007, 76:237-248.
    • (2007) Appl. Microbiol. Biotechnol. , vol.76 , pp. 237-248
    • Goldberg, K.1    Schroer, K.2    Lütz, S.3    Liese, A.4
  • 8
    • 28944451564 scopus 로고    scopus 로고
    • Biocatalytic synthesis of ethyl (S)-4- chloro-3-hydroxy-butanoate in an aqueous-organic solvent biphasic system using Aureobasidium pullulans CGMCC 1244
    • He J.Y., Sun Z.H., Ruan W.Q., Xu Y. Biocatalytic synthesis of ethyl (S)-4- chloro-3-hydroxy-butanoate in an aqueous-organic solvent biphasic system using Aureobasidium pullulans CGMCC 1244. Process Biochem. 2006, 41:244-249.
    • (2006) Process Biochem. , vol.41 , pp. 244-249
    • He, J.Y.1    Sun, Z.H.2    Ruan, W.Q.3    Xu, Y.4
  • 9
    • 55049135570 scopus 로고    scopus 로고
    • Identification, cloning, characterization of a novel ketoreductase from the cyanobacterium Synechococcus sp. strain PCC 7942
    • Hölsch K., Havel J., Haslbeck M., Weuster-Botz D. Identification, cloning, characterization of a novel ketoreductase from the cyanobacterium Synechococcus sp. strain PCC 7942. Appl. Environ. Microbiol. 2008, 74:6697-6702.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 6697-6702
    • Hölsch, K.1    Havel, J.2    Haslbeck, M.3    Weuster-Botz, D.4
  • 10
    • 77955982670 scopus 로고    scopus 로고
    • New oxidoreductases from cyanobacteria: exploring nature's diversity
    • Hölsch K., Weuster-Botz D. New oxidoreductases from cyanobacteria: exploring nature's diversity. Enzyme Microb. Technol. 2010, 47:228-235.
    • (2010) Enzyme Microb. Technol. , vol.47 , pp. 228-235
    • Hölsch, K.1    Weuster-Botz, D.2
  • 11
    • 0025115797 scopus 로고
    • Reduction of acetophenone to R(+)-phenylethanol by a new alcohol dehydrogenase from Lactobacillus kefir
    • Hummel W. Reduction of acetophenone to R(+)-phenylethanol by a new alcohol dehydrogenase from Lactobacillus kefir. Appl. Microbiol. Biotechnol. 1990, 34:15-19.
    • (1990) Appl. Microbiol. Biotechnol. , vol.34 , pp. 15-19
    • Hummel, W.1
  • 12
    • 0030632239 scopus 로고    scopus 로고
    • New alcohol dehydrogenases for the synthesis of chiral compounds
    • Hummel W. New alcohol dehydrogenases for the synthesis of chiral compounds. Adv. Biochem. Eng. Biotechnol. 1997, 58:145-184.
    • (1997) Adv. Biochem. Eng. Biotechnol. , vol.58 , pp. 145-184
    • Hummel, W.1
  • 13
    • 0033485581 scopus 로고    scopus 로고
    • Large-scale applications of NAD(P)-dependent oxidoreductases: recent developments
    • Hummel W. Large-scale applications of NAD(P)-dependent oxidoreductases: recent developments. Trends Biotechnol. 1999, 17:482-487.
    • (1999) Trends Biotechnol. , vol.17 , pp. 482-487
    • Hummel, W.1
  • 14
    • 23644444887 scopus 로고    scopus 로고
    • Production of (R)-chiral alcohols by a hydrogen-transfer bioreduction with NADH-dependent Leifsonia alcohol dehydrogenase (LSADH)
    • Inoue K., Makino Y., Itoh N. Production of (R)-chiral alcohols by a hydrogen-transfer bioreduction with NADH-dependent Leifsonia alcohol dehydrogenase (LSADH). Tetrahedron: Asymmetry 2005, 16:2539-2549.
    • (2005) Tetrahedron: Asymmetry , vol.16 , pp. 2539-2549
    • Inoue, K.1    Makino, Y.2    Itoh, N.3
  • 15
    • 22144495063 scopus 로고    scopus 로고
    • Purification and characterization of a novel alcohol dehydrogenase from Leifsonia sp. strain S749: a promising biocatalyst for an asymmetric hydrogen transfer bioreduction
    • Inoue K., Makino K., Itoh N. Purification and characterization of a novel alcohol dehydrogenase from Leifsonia sp. strain S749: a promising biocatalyst for an asymmetric hydrogen transfer bioreduction. Appl. Environ. Microbiol. 2005, 71:3633-3641.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 3633-3641
    • Inoue, K.1    Makino, K.2    Itoh, N.3
  • 16
    • 33344463227 scopus 로고    scopus 로고
    • Gene cloning and expression of Leifsonia alcohol dehydrogenase (LSADH) involved in asymmetric hydrogen-transfer bioreduction to product (R)-form chiral alcohols
    • Inoue K., Makino Y., Dairi T., Itoh N. Gene cloning and expression of Leifsonia alcohol dehydrogenase (LSADH) involved in asymmetric hydrogen-transfer bioreduction to product (R)-form chiral alcohols. Biosci. Biotechnol. Biochem. 2006, 70:418-426.
    • (2006) Biosci. Biotechnol. Biochem. , vol.70 , pp. 418-426
    • Inoue, K.1    Makino, Y.2    Dairi, T.3    Itoh, N.4
  • 18
    • 0035024562 scopus 로고    scopus 로고
    • Synthesis of optically pure ethyl (S)-4-chloro-3-hydroxybutanoate by Escherichia coli transformant cells coexpressing the carbonyl reductase and glucose dehydrogenase genes
    • Kizaki N., Yasohara Y., Hasegawa J., Wada M., Kataoka M., Shimizu S. Synthesis of optically pure ethyl (S)-4-chloro-3-hydroxybutanoate by Escherichia coli transformant cells coexpressing the carbonyl reductase and glucose dehydrogenase genes. Appl. Microbiol. Biotechnol. 2001, 55:590-595.
    • (2001) Appl. Microbiol. Biotechnol. , vol.55 , pp. 590-595
    • Kizaki, N.1    Yasohara, Y.2    Hasegawa, J.3    Wada, M.4    Kataoka, M.5    Shimizu, S.6
  • 19
    • 1842583994 scopus 로고    scopus 로고
    • Recent advances in the biocatalytic reduction of ketones and oxidation of sec-alcohols
    • Kroutil W., Mang H., Edegger K., Faber K. Recent advances in the biocatalytic reduction of ketones and oxidation of sec-alcohols. Curr. Opin. Chem. Biol. 2004, 8:120-126.
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 120-126
    • Kroutil, W.1    Mang, H.2    Edegger, K.3    Faber, K.4
  • 20
    • 0023385987 scopus 로고
    • Rules for the optimization of biocatalysis in organic solvents
    • Laane C., Boeren S., Vox K., Weeger C. Rules for the optimization of biocatalysis in organic solvents. Biotechnol. Bioeng. 1987, 30:81-87.
    • (1987) Biotechnol. Bioeng. , vol.30 , pp. 81-87
    • Laane, C.1    Boeren, S.2    Vox, K.3    Weeger, C.4
  • 21
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver H., Burk D. The determination of enzyme dissociation constants. J. Am. Chem. Soc. 1934, 56:658-666.
    • (1934) J. Am. Chem. Soc. , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 23
    • 79952537762 scopus 로고    scopus 로고
    • Biocatalytic properties of a recombinant aldo-keto reductase with broad substrate spectrum and excellent stereoselectivity
    • Ni Y., Li C.X., Ma H.M., Zhang J., Xu J.H. Biocatalytic properties of a recombinant aldo-keto reductase with broad substrate spectrum and excellent stereoselectivity. Appl. Microbiol. Biotechnol. 2010, 89:1111-1118.
    • (2010) Appl. Microbiol. Biotechnol. , vol.89 , pp. 1111-1118
    • Ni, Y.1    Li, C.X.2    Ma, H.M.3    Zhang, J.4    Xu, J.H.5
  • 24
    • 84913063444 scopus 로고
    • Specification of the stereospecificity of some oxido-reductases by diamond lattice sections
    • Prelog V. Specification of the stereospecificity of some oxido-reductases by diamond lattice sections. Pure Appl. Chem. 1964, 9:119-130.
    • (1964) Pure Appl. Chem. , vol.9 , pp. 119-130
    • Prelog, V.1
  • 25
    • 72449130896 scopus 로고    scopus 로고
    • A continuously operated bimembrane reactor process for the biocatalytic production of (2R, 5R)-hexanediol
    • Schroer K., Lütz S. A continuously operated bimembrane reactor process for the biocatalytic production of (2R, 5R)-hexanediol. Org. Process Res. Dev. 2009, 13:1202-1205.
    • (2009) Org. Process Res. Dev. , vol.13 , pp. 1202-1205
    • Schroer, K.1    Lütz, S.2
  • 26
    • 0025281564 scopus 로고
    • Stereoselective reduction of ethyl 4-chloro-3-oxobutanoate by a microbial aldehyde reductase in an organic solvent-water diphasic system
    • Shimizu S., Kataoka M., Katoh M., Morikawa T., Miyoshi T., Yamada H. Stereoselective reduction of ethyl 4-chloro-3-oxobutanoate by a microbial aldehyde reductase in an organic solvent-water diphasic system. Appl. Environ. Microbiol. 1990, 56:2374-2377.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 2374-2377
    • Shimizu, S.1    Kataoka, M.2    Katoh, M.3    Morikawa, T.4    Miyoshi, T.5    Yamada, H.6
  • 27
    • 71149095075 scopus 로고    scopus 로고
    • Isolation of a Bacillus strain producing ketone reductase with high substrate tolerance
    • Xie Y., Xu J.H., Xu Y. Isolation of a Bacillus strain producing ketone reductase with high substrate tolerance. Bioresour. Technol. 2010, 101:1054-1059.
    • (2010) Bioresour. Technol. , vol.101 , pp. 1054-1059
    • Xie, Y.1    Xu, J.H.2    Xu, Y.3
  • 28
    • 0037393493 scopus 로고    scopus 로고
    • Synthesis of ethyl (S)-4-chloro-3-hydroxybutanoate using fabG-homologues
    • Yamamoto H., Matsuyama A., Kobayashi Y. Synthesis of ethyl (S)-4-chloro-3-hydroxybutanoate using fabG-homologues. Appl. Microbiol. Biotechnol. 2003, 61:133-139.
    • (2003) Appl. Microbiol. Biotechnol. , vol.61 , pp. 133-139
    • Yamamoto, H.1    Matsuyama, A.2    Kobayashi, Y.3
  • 29
    • 0034223670 scopus 로고    scopus 로고
    • Molecular cloning and overexpression of the gene encoding an NADPH-dependent carbonyl reductase from Candida magnoliae, involved in stereoselective reduction of ethyl 4-chloro-3-oxobutanoate
    • Yasohara Y., Kizaki N., Hasegawa J., Wada M., Kataokac M., Shimizu S. Molecular cloning and overexpression of the gene encoding an NADPH-dependent carbonyl reductase from Candida magnoliae, involved in stereoselective reduction of ethyl 4-chloro-3-oxobutanoate. Biosci. Biotechnol. Biochem. 2000, 64:1430-1436.
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 1430-1436
    • Yasohara, Y.1    Kizaki, N.2    Hasegawa, J.3    Wada, M.4    Kataokac, M.5    Shimizu, S.6
  • 30
    • 0035898137 scopus 로고    scopus 로고
    • Stereoselective reduction of alkyl 3-oxobutanoate by carbonyl reductase from Candida magnoliae
    • Yasohara Y., Kizaki N., Hasegawa J., Wada M., Kataokac M., Shimizu S. Stereoselective reduction of alkyl 3-oxobutanoate by carbonyl reductase from Candida magnoliae. Tetrahedron: Asymmetry 2001, 12:1713-1718.
    • (2001) Tetrahedron: Asymmetry , vol.12 , pp. 1713-1718
    • Yasohara, Y.1    Kizaki, N.2    Hasegawa, J.3    Wada, M.4    Kataokac, M.5    Shimizu, S.6
  • 31
    • 68649096334 scopus 로고    scopus 로고
    • A new member of the short-chain dehydrogenases/reductases superfamily: purification, characterization and substrate specificity of a recombinant carbonyl reductase from Pichia stipitis
    • Ye Q., Yan M., Yao Z., Xu L., Cao H., Li Z.J., Chen Y., Li S.Y., Bai J.X., Xiong J., Ying H.J., Ouyang P.K. A new member of the short-chain dehydrogenases/reductases superfamily: purification, characterization and substrate specificity of a recombinant carbonyl reductase from Pichia stipitis. Bioresour. Technol. 2009, 100:6022-6027.
    • (2009) Bioresour. Technol. , vol.100 , pp. 6022-6027
    • Ye, Q.1    Yan, M.2    Yao, Z.3    Xu, L.4    Cao, H.5    Li, Z.J.6    Chen, Y.7    Li, S.Y.8    Bai, J.X.9    Xiong, J.10    Ying, H.J.11    Ouyang, P.K.12
  • 32
    • 77955176128 scopus 로고    scopus 로고
    • Construction and co-expression of a polycistronic plasmid encoding carbonyl reductase and glucose dehydrogenase for production of ethyl (S)-4-chloro-3-hydroxybutanoate
    • Ye Q., Cao H., Yan M., Cao F., Zhang Y.Y., Li X.M., Xu L., Chen Y., Xiong J., Ouyang P.K., Ying H.J. Construction and co-expression of a polycistronic plasmid encoding carbonyl reductase and glucose dehydrogenase for production of ethyl (S)-4-chloro-3-hydroxybutanoate. Bioresour. Technol. 2010, 101:6761-6767.
    • (2010) Bioresour. Technol. , vol.101 , pp. 6761-6767
    • Ye, Q.1    Cao, H.2    Yan, M.3    Cao, F.4    Zhang, Y.Y.5    Li, X.M.6    Xu, L.7    Chen, Y.8    Xiong, J.9    Ouyang, P.K.10    Ying, H.J.11
  • 33
    • 26444620937 scopus 로고    scopus 로고
    • 'Green' synthesis of important pharmaceutical building blocks: enzymatic access to enantiomerically pure α-chloroalcohols
    • Zhu D., Chandrani M., Hua L. 'Green' synthesis of important pharmaceutical building blocks: enzymatic access to enantiomerically pure α-chloroalcohols. Tetrahedron: Asymmetry 2005, 16:3275-3278.
    • (2005) Tetrahedron: Asymmetry , vol.16 , pp. 3275-3278
    • Zhu, D.1    Chandrani, M.2    Hua, L.3
  • 34
    • 33646930611 scopus 로고    scopus 로고
    • Stereoselective enzymatic synthesis of chiral alcohols with the use of a carbonyl reductase from Candida magnoliae with anti-Prelog enantioselectivity
    • Zhu D., Yang Y., Hua L. Stereoselective enzymatic synthesis of chiral alcohols with the use of a carbonyl reductase from Candida magnoliae with anti-Prelog enantioselectivity. J. Org. Chem. 2006, 71:4202-4205.
    • (2006) J. Org. Chem. , vol.71 , pp. 4202-4205
    • Zhu, D.1    Yang, Y.2    Hua, L.3


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