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Volumn 14, Issue 4, 2003, Pages 421-426

Recent developments in pyridine nucleotide regeneration

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL DEHYDROGENASE; FORMATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) TRANSHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; NUCLEOTIDASE; ORGANIC SOLVENT; PYRIDINE NUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE DEHYDROGENASE;

EID: 0042933788     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(03)00094-6     Document Type: Review
Times cited : (341)

References (50)
  • 2
    • 0035843170 scopus 로고    scopus 로고
    • Industrial biocatalysis today and tomorrow
    • This review presents an excellent overview of the current status and the emerging frontiers in biocatalysis from an industrial perspective.
    • Schmid A., Dordick J.S., Hauer B., Kiener A., Wubbolts M., Witholt B. Industrial biocatalysis today and tomorrow. Nature. 409:2001;258-268 This review presents an excellent overview of the current status and the emerging frontiers in biocatalysis from an industrial perspective.
    • (2001) Nature , vol.409 , pp. 258-268
    • Schmid, A.1    Dordick, J.S.2    Hauer, B.3    Kiener, A.4    Wubbolts, M.5    Witholt, B.6
  • 3
    • 0035843122 scopus 로고    scopus 로고
    • Enzymes for chemical synthesis
    • Koeller K.M., Wong C.H. Enzymes for chemical synthesis. Nature. 409:2001;232-240.
    • (2001) Nature , vol.409 , pp. 232-240
    • Koeller, K.M.1    Wong, C.H.2
  • 4
    • 0036536478 scopus 로고    scopus 로고
    • Directed evolution of enzymes and pathways for industrial biocatalysis
    • Zhao H., Chockalingam K., Chen Z. Directed evolution of enzymes and pathways for industrial biocatalysis. Curr Opin Biotechnol. 13:2002;104-110.
    • (2002) Curr Opin Biotechnol , vol.13 , pp. 104-110
    • Zhao, H.1    Chockalingam, K.2    Chen, Z.3
  • 5
    • 0035313656 scopus 로고    scopus 로고
    • Dehydrogenases and transaminases in asymmetric synthesis
    • Stewart J.D. Dehydrogenases and transaminases in asymmetric synthesis. Curr Opin Chem Biol. 5:2001;120-129.
    • (2001) Curr Opin Chem Biol , vol.5 , pp. 120-129
    • Stewart, J.D.1
  • 8
    • 0035041719 scopus 로고    scopus 로고
    • Redox enzymes used in chiral syntheses coupled to coenzyme regeneration
    • Leonida M.D. Redox enzymes used in chiral syntheses coupled to coenzyme regeneration. Curr Med Chem. 8:2001;345-369.
    • (2001) Curr Med Chem , vol.8 , pp. 345-369
    • Leonida, M.D.1
  • 9
    • 0345817539 scopus 로고
    • Regeneration of nicotinamide cofactors for use in organic synthesis
    • Chenault H.K., Whitesides G.M. Regeneration of nicotinamide cofactors for use in organic synthesis. Appl Biochem Biotechnol. 14:1987;147-197.
    • (1987) Appl Biochem Biotechnol , vol.14 , pp. 147-197
    • Chenault, H.K.1    Whitesides, G.M.2
  • 10
    • 0031104963 scopus 로고    scopus 로고
    • Potential applications of NAD(P)-dependent oxidoreductases in synthesis - A survey
    • Devaux-Basséguy R., Bergel A., Comtat M. Potential applications of NAD(P)-dependent oxidoreductases in synthesis - a survey. Enzyme Microb Technol. 20:1997;248-258.
    • (1997) Enzyme Microb Technol , vol.20 , pp. 248-258
    • Devaux-Basséguy, R.1    Bergel, A.2    Comtat, M.3
  • 11
    • 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. 17:1999;487-492.
    • (1999) Trends Biotechnol , vol.17 , pp. 487-492
    • Hummel, W.1
  • 12
    • 0037084327 scopus 로고    scopus 로고
    • Highly enantioselective preparation of multifunctionalized propargylic building blocks
    • Schubert T., Hummel W., Muller M. Highly enantioselective preparation of multifunctionalized propargylic building blocks. Angew Chem Int Ed Engl. 41:2002;634-637.
    • (2002) Angew Chem Int Ed Engl , vol.41 , pp. 634-637
    • Schubert, T.1    Hummel, W.2    Muller, M.3
  • 13
    • 0034677110 scopus 로고    scopus 로고
    • Cofactor-bound cross-linked enzyme crystals (CLEC) of alcohol dehydrogenase
    • This paper describes the use of CLECs to stabilize both the dehydrogenase enzyme and the cofactor in a nicotinamide cofactor regeneration system.
    • St Clair N., Wang Y.F., Margolin A.L. Cofactor-bound cross-linked enzyme crystals (CLEC) of alcohol dehydrogenase. Angew Chem Int Ed Engl. 39:2000;380-383 This paper describes the use of CLECs to stabilize both the dehydrogenase enzyme and the cofactor in a nicotinamide cofactor regeneration system.
    • (2000) Angew Chem Int Ed Engl , vol.39 , pp. 380-383
    • St Clair, N.1    Wang, Y.F.2    Margolin, A.L.3
  • 14
    • 0035689388 scopus 로고    scopus 로고
    • Two-enzyme cross-linked crystals for chiral synthesis coupled with electroenzymatic regeneration of the cofactor
    • Leonida M.D., Fry A.J., Sobolov S.B., Bartoszko-Malik A. Two-enzyme cross-linked crystals for chiral synthesis coupled with electroenzymatic regeneration of the cofactor. Intl J Biochromat. 6:2001;207-217.
    • (2001) Intl J Biochromat , vol.6 , pp. 207-217
    • Leonida, M.D.1    Fry, A.J.2    Sobolov, S.B.3    Bartoszko-Malik, A.4
  • 15
    • 84907037937 scopus 로고
    • Some new developments in reductive amination with cofactor regeneration
    • Bommarius A.S., Drauz K., Hummel W., Kula M.R., Wandrey C. Some new developments in reductive amination with cofactor regeneration. Biocatalysis. 10:1994;37-47.
    • (1994) Biocatalysis , vol.10 , pp. 37-47
    • Bommarius, A.S.1    Drauz, K.2    Hummel, W.3    Kula, M.R.4    Wandrey, C.5
  • 16
    • 0032530505 scopus 로고    scopus 로고
    • Biocatalysis to amino acid-based chiral pharmaceuticals - Examples and perspectives
    • Bommarius A.S., Schwarm M., Drauz K. Biocatalysis to amino acid-based chiral pharmaceuticals - examples and perspectives. J Mol Catal B Enzym. 5:1998;1-11.
    • (1998) J Mol Catal B Enzym , vol.5 , pp. 1-11
    • Bommarius, A.S.1    Schwarm, M.2    Drauz, K.3
  • 17
    • 0034011107 scopus 로고    scopus 로고
    • Stabilization of NAD-dependent formate dehydrogenase from Candida boidinii by site-directed mutagenesis of cysteine residues
    • Slusarczyk H., Felber S., Kula M.-R., Pohl M. Stabilization of NAD-dependent formate dehydrogenase from Candida boidinii by site-directed mutagenesis of cysteine residues. Eur J Biochem. 267:2000;1280-1289.
    • (2000) Eur J Biochem , vol.267 , pp. 1280-1289
    • Slusarczyk, H.1    Felber, S.2    Kula, M.-R.3    Pohl, M.4
  • 18
    • 0030312717 scopus 로고    scopus 로고
    • Cofactor regeneration in biocatalysis in organic media
    • Adlercreutz P. Cofactor regeneration in biocatalysis in organic media. Biocat Biotransform. 14:1996;1-30.
    • (1996) Biocat Biotransform , vol.14 , pp. 1-30
    • Adlercreutz, P.1
  • 19
    • 0037666071 scopus 로고    scopus 로고
    • Practical asymmetric enzymatic reduction through discovery of a dehydrogenase-compatible biphasic reaction media
    • Groeger H., Hummel W., Buchholz S., Drauz K., Nguyen T.V., Rollmann C., Huesken H., Abokitse K. Practical asymmetric enzymatic reduction through discovery of a dehydrogenase-compatible biphasic reaction media. Org Lett. 5:2003;173-176.
    • (2003) Org Lett , vol.5 , pp. 173-176
    • Groeger, H.1    Hummel, W.2    Buchholz, S.3    Drauz, K.4    Nguyen, T.V.5    Rollmann, C.6    Huesken, H.7    Abokitse, K.8
  • 20
    • 0035931416 scopus 로고    scopus 로고
    • Preparative regio- and chemoselective functionalization of hydrocarbons catalyzed by cell-free preparations of 2-hydroxybiphenyl 3-monooxygenase
    • Schmid A., Vereyken I., Held M., Witholt B. Preparative regio- and chemoselective functionalization of hydrocarbons catalyzed by cell-free preparations of 2-hydroxybiphenyl 3-monooxygenase. J Mol Catal B Enzym. 11:2001;455-462.
    • (2001) J Mol Catal B Enzym , vol.11 , pp. 455-462
    • Schmid, A.1    Vereyken, I.2    Held, M.3    Witholt, B.4
  • 21
    • 0034827207 scopus 로고    scopus 로고
    • Phosphite dehydrogenase: An unusual phosphoryl transfer reaction
    • Vrtis J.M., White A., Metcalf W.W., van der Donk W.A. Phosphite dehydrogenase: an unusual phosphoryl transfer reaction. J Am Chem Soc. 123:2001;2672-2673.
    • (2001) J Am Chem Soc , vol.123 , pp. 2672-2673
    • Vrtis, J.M.1    White, A.2    Metcalf, W.W.3    Van der Donk, W.A.4
  • 22
    • 0035907326 scopus 로고    scopus 로고
    • Purification and characterization of a novel phosphorus-oxidizing enzyme from Pseudomonas stutzeri WM88
    • Costas A.M., White A.K., Metcalf W.W. Purification and characterization of a novel phosphorus-oxidizing enzyme from Pseudomonas stutzeri WM88. J Biol Chem. 276:2001;17429-17436.
    • (2001) J Biol Chem , vol.276 , pp. 17429-17436
    • Costas, A.M.1    White, A.K.2    Metcalf, W.W.3
  • 23
    • 0037008984 scopus 로고    scopus 로고
    • Phosphite dehydrogenase, a new versatile cofactor regeneration enzyme
    • This study presents a new method for regenerating reduced nicotinamide cofactors based on a recently discovered enzyme, phosphite dehydrogenase. Because of the intrinsic large thermodynamic driving force, the innocuous nature of phosphite and phosphate to the enzymes, and the low cost of phosphite, this phosphite-phosphite dehydrogenase system may prove complementary to the most widely used formate-formate dehydrogenase system.
    • Vrtis J.M., White A., Metcalf W.W., van der Donk W.A. Phosphite dehydrogenase, a new versatile cofactor regeneration enzyme. Angew Chem Int Ed Engl. 41:2002;3257-3259 This study presents a new method for regenerating reduced nicotinamide cofactors based on a recently discovered enzyme, phosphite dehydrogenase. Because of the intrinsic large thermodynamic driving force, the innocuous nature of phosphite and phosphate to the enzymes, and the low cost of phosphite, this phosphite-phosphite dehydrogenase system may prove complementary to the most widely used formate-formate dehydrogenase system.
    • (2002) Angew Chem Int Ed Engl , vol.41 , pp. 3257-3259
    • Vrtis, J.M.1    White, A.2    Metcalf, W.W.3    Van der Donk, W.A.4
  • 25
    • 0034466694 scopus 로고    scopus 로고
    • Cofactor regeneration by a soluble pyridine nucleotide transhydrogenase for biological production of hydromorphone
    • This article describes the use of an STH from Pseudomonas fluorescens for the regeneration of the nicotinamide cofactors NAD and NADP in the synthesis of hydromorphone in both cell-free and whole-cell systems. STH can transfer reducing equivalents between NAD(H) and NADP(H).
    • Boonstra B., Rathbone D.A., French C.E., Walker E.H., Bruce N.C. Cofactor regeneration by a soluble pyridine nucleotide transhydrogenase for biological production of hydromorphone. Appl Environ Microbiol. 66:2000;5161-5166 This article describes the use of an STH from Pseudomonas fluorescens for the regeneration of the nicotinamide cofactors NAD and NADP in the synthesis of hydromorphone in both cell-free and whole-cell systems. STH can transfer reducing equivalents between NAD(H) and NADP(H).
    • (2000) Appl Environ Microbiol , vol.66 , pp. 5161-5166
    • Boonstra, B.1    Rathbone, D.A.2    French, C.E.3    Walker, E.H.4    Bruce, N.C.5
  • 26
    • 85005697480 scopus 로고
    • Dehydrogenases for the synthesis of chiral compounds
    • Hummel W., Kula M.R. Dehydrogenases for the synthesis of chiral compounds. Eur J Biochem. 184:1989;1-13.
    • (1989) Eur J Biochem , vol.184 , pp. 1-13
    • Hummel, W.1    Kula, M.R.2
  • 28
    • 0037415359 scopus 로고    scopus 로고
    • NADH oxidase from Lactobacillus brevis: A new catalyst for the regeneration of NAD
    • + from NADH in which the NADH oxidase was coupled with an NAD-dependent ADH to produce enantiomerically pure alcohol from a racemic mixture.
    • + from NADH in which the NADH oxidase was coupled with an NAD-dependent ADH to produce enantiomerically pure alcohol from a racemic mixture.
    • (2003) Enzyme Microb Technol , vol.32 , pp. 205-211
    • Geueke, B.1    Riebel, B.2    Hummel, W.3
  • 29
    • 0034792157 scopus 로고    scopus 로고
    • Structural, redox, and mechanistic parameters for cysteine-sulfenic acid function in catalysis and regulation
    • Claiborne A., Mallett T.C., Yeh J.I., Luba J., Parsonage D. Structural, redox, and mechanistic parameters for cysteine-sulfenic acid function in catalysis and regulation. Adv Protein Chem. 58:2001;215-276.
    • (2001) Adv Protein Chem , vol.58 , pp. 215-276
    • Claiborne, A.1    Mallett, T.C.2    Yeh, J.I.3    Luba, J.4    Parsonage, D.5
  • 30
    • 0035471221 scopus 로고    scopus 로고
    • Surface-modified electrodes for NADH oxidation in oxidoreductase-catalysed synthesis
    • Délécouls-Servat K., Bergel A., Basséguy R. Surface-modified electrodes for NADH oxidation in oxidoreductase-catalysed synthesis. J Appl Electrochem. 31:2001;1095-1101.
    • (2001) J Appl Electrochem , vol.31 , pp. 1095-1101
    • Délécouls-Servat, K.1    Bergel, A.2    Basséguy, R.3
  • 33
    • 0346668121 scopus 로고    scopus 로고
    • Membrane electrochemical reactor (MER): Application to NADH regeneration for ADH-catalysed synthesis
    • Délécouls-Servat K., Basséguy R., Bergel A. Membrane electrochemical reactor (MER): application to NADH regeneration for ADH-catalysed synthesis. Chem Engin Sci. 57:2002;4633-4642.
    • (2002) Chem Engin Sci , vol.57 , pp. 4633-4642
    • Délécouls-Servat, K.1    Basséguy, R.2    Bergel, A.3
  • 34
    • 33748225950 scopus 로고
    • Formate-driven, nonenzymic NAD(P)H regeneration in the alcohol dehydrogenase-catalyzed stereoselective reduction of 4-phenyl-2-butanone
    • Westerhausen D., Herrmann S., Hummel W., Steckhan E. Formate-driven, nonenzymic NAD(P)H regeneration in the alcohol dehydrogenase-catalyzed stereoselective reduction of 4-phenyl-2-butanone. Angew Chem Int Ed Engl. 31:1992;1529-1531.
    • (1992) Angew Chem Int Ed Engl , vol.31 , pp. 1529-1531
    • Westerhausen, D.1    Herrmann, S.2    Hummel, W.3    Steckhan, E.4
  • 35
    • 0035825143 scopus 로고    scopus 로고
    • The first synthetic application of a monooxygenase employing indirect electrochemical NADH regeneration
    • 2+ for cofactor regeneration with monooxygenases. This Rh complex exhibits high stability and activity over a broad range of pH and temperature. Moreover, both cheap electrical power and chemicals such as formate or alcohols can be used as the source of reducing equivalents. Compared with other in vitro enzymatic cofactor regeneration systems, the turnover numbers of this method are somewhat lower.
    • 2+ for cofactor regeneration with monooxygenases. This Rh complex exhibits high stability and activity over a broad range of pH and temperature. Moreover, both cheap electrical power and chemicals such as formate or alcohols can be used as the source of reducing equivalents. Compared with other in vitro enzymatic cofactor regeneration systems, the turnover numbers of this method are somewhat lower.
    • (2001) Angew Chem Int Ed Engl , vol.40 , pp. 169-171
    • Hollmann, F.1    Schmid, A.2    Steckhan, E.3
  • 36
    • 0037010696 scopus 로고    scopus 로고
    • Preparative application of 2-hydroxybiphenyl 3-monooxygenase with enzymatic cofactor regeneration in organic-aqueous reaction media
    • Lutz J., Mozhaev V.V., Khmelnitsky Y.L., Witholt B., Schmid A. Preparative application of 2-hydroxybiphenyl 3-monooxygenase with enzymatic cofactor regeneration in organic-aqueous reaction media. J Mol Catal B Enzym. 19:2002;177-187.
    • (2002) J Mol Catal B Enzym , vol.19 , pp. 177-187
    • Lutz, J.1    Mozhaev, V.V.2    Khmelnitsky, Y.L.3    Witholt, B.4    Schmid, A.5
  • 37
    • 0035904986 scopus 로고    scopus 로고
    • +: Structure-activity relationships, kinetics, and mechanistic aspects in the formation of the 1,4-NADH derivatives
    • +: structure-activity relationships, kinetics, and mechanistic aspects in the formation of the 1,4-NADH derivatives. Inorg Chem. 40:2001;6705-6716.
    • (2001) Inorg Chem , vol.40 , pp. 6705-6716
    • Lo, H.C.1    Leiva, C.2    Buriez, O.3    Kerr, J.B.4    Olmstead, M.M.5    Fish, R.H.6
  • 38
    • 10044271107 scopus 로고    scopus 로고
    • 2+: A versatile tool for efficient and non-enzymatic regeneration of nicotinamide and flavin coenzymes
    • 2+: a versatile tool for efficient and non-enzymatic regeneration of nicotinamide and flavin coenzymes. J Mol Catal B Enzym. 19:2002;167-176.
    • (2002) J Mol Catal B Enzym , vol.19 , pp. 167-176
    • Hollmann, F.1    Witholt, B.2    Schmid, A.3
  • 40
    • 0030738089 scopus 로고    scopus 로고
    • Synthesis of chiral ε-lactones in a two-enzyme system of cyclohexanone mono-oxygenase and formate dehydrogenase with integrated bubble-free aeration
    • Rissom S., Schwarz-Linek U., Vogel M., Tishkov V.I., Kragl U. Synthesis of chiral ε-lactones in a two-enzyme system of cyclohexanone mono-oxygenase and formate dehydrogenase with integrated bubble-free aeration. Tetrahedron Asymmetry. 8:1997;2523-2526.
    • (1997) Tetrahedron Asymmetry , vol.8 , pp. 2523-2526
    • Rissom, S.1    Schwarz-Linek, U.2    Vogel, M.3    Tishkov, V.I.4    Kragl, U.5
  • 41
  • 42
    • 0035923612 scopus 로고    scopus 로고
    • Taxol biosynthesis: Taxane 13 α-hydroxylase is a cytochrome P450-dependent monooxygenase
    • Jennewein S., Rithner C.D., Williams R.M., Croteau R.B. Taxol biosynthesis: Taxane 13 α-hydroxylase is a cytochrome P450-dependent monooxygenase. Proc Natl Acad Sci USA. 98:2001;13595-13600.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 13595-13600
    • Jennewein, S.1    Rithner, C.D.2    Williams, R.M.3    Croteau, R.B.4
  • 43
    • 0037023928 scopus 로고    scopus 로고
    • Use of isolated cyclohexanone monooxygenase from recombinant Escherichia coli as a biocatalyst for Baeyer-Villiger and sulfide oxidations
    • Zambianchi F., Pasta P., Carrea G., Colonna S., Gaggero N., Woodley J.M. Use of isolated cyclohexanone monooxygenase from recombinant Escherichia coli as a biocatalyst for Baeyer-Villiger and sulfide oxidations. Biotechnol Bioeng. 78:2002;489-496.
    • (2002) Biotechnol Bioeng , vol.78 , pp. 489-496
    • Zambianchi, F.1    Pasta, P.2    Carrea, G.3    Colonna, S.4    Gaggero, N.5    Woodley, J.M.6
  • 44
    • 0037454977 scopus 로고    scopus 로고
    • Oxidation of amines catalyzed by cyclohexanone monooxygenase
    • Colonna S., Pironti V., Pasta P., Zambianchi F. Oxidation of amines catalyzed by cyclohexanone monooxygenase. Tetrahedron Lett. 44:2003;869-871.
    • (2003) Tetrahedron Lett , vol.44 , pp. 869-871
    • Colonna, S.1    Pironti, V.2    Pasta, P.3    Zambianchi, F.4
  • 45
    • 0041404265 scopus 로고    scopus 로고
    • Microbial conversion with cofactor regeneration using genetically engineered bacteria
    • Endo T., Koizumi S. Microbial conversion with cofactor regeneration using genetically engineered bacteria. Adv Synth Cat. 343:2001;521-526.
    • (2001) Adv Synth Cat , vol.343 , pp. 521-526
    • Endo, T.1    Koizumi, S.2
  • 46
    • 0035424201 scopus 로고    scopus 로고
    • Using proteins in their natural environment: Potential and limitations of microbial whole-cell hydroxylations in applied biocatalysis
    • This review gives an excellent overview of the field of whole-cell catalysis for hydroxylation reactions.
    • Duetz W.A., van Beilen J.B., Witholt B. Using proteins in their natural environment: potential and limitations of microbial whole-cell hydroxylations in applied biocatalysis. Curr Opin Biotechnol. 12:2001;419-425 This review gives an excellent overview of the field of whole-cell catalysis for hydroxylation reactions.
    • (2001) Curr Opin Biotechnol , vol.12 , pp. 419-425
    • Duetz, W.A.1    Van Beilen, J.B.2    Witholt, B.3
  • 47
    • 0032951737 scopus 로고    scopus 로고
    • Stereoselective reduction of ethyl 4-chloro-3-oxobutanoate by Escherichia coli transformant cells coexpressing the aldehyde reductase and glucose dehydrogenase genes
    • Kataoka M., Yamamoto K., Kawabata H., Wada M., Kita K., Yanase H., Shimizu S. Stereoselective reduction of ethyl 4-chloro-3-oxobutanoate by Escherichia coli transformant cells coexpressing the aldehyde reductase and glucose dehydrogenase genes. Appl Microbiol Biotechnol. 51:1999;486-490.
    • (1999) Appl Microbiol Biotechnol , vol.51 , pp. 486-490
    • Kataoka, M.1    Yamamoto, K.2    Kawabata, H.3    Wada, M.4    Kita, K.5    Yanase, H.6    Shimizu, S.7
  • 48
    • 0037087669 scopus 로고    scopus 로고
    • Biocatalytic asymmetric hydrogen transfer
    • This paper reports the first-time use of lyophilized whole cells of Rhodococcus ruber DSM 44541 to produce secondary alcohols using acetone as a cosubstrate.
    • Stampfer W., Kosjek B., Moitzi C., Kroutil W., Faber K. Biocatalytic asymmetric hydrogen transfer. Angew Chem Int Ed Engl. 41:2002;1014-1017 This paper reports the first-time use of lyophilized whole cells of Rhodococcus ruber DSM 44541 to produce secondary alcohols using acetone as a cosubstrate.
    • (2002) Angew Chem Int Ed Engl , vol.41 , pp. 1014-1017
    • Stampfer, W.1    Kosjek, B.2    Moitzi, C.3    Kroutil, W.4    Faber, K.5
  • 49
    • 0037473197 scopus 로고    scopus 로고
    • On the organic solvent and thermostability of the biocatalytic redox system of Rhodococcus ruber DSM 44541
    • Stampfer W., Kosjek B., Kroutil W., Faber K. On the organic solvent and thermostability of the biocatalytic redox system of Rhodococcus ruber DSM 44541. Biotechnol Bioeng. 81:2003;865-869.
    • (2003) Biotechnol Bioeng , vol.81 , pp. 865-869
    • Stampfer, W.1    Kosjek, B.2    Kroutil, W.3    Faber, K.4
  • 50
    • 0036093463 scopus 로고    scopus 로고
    • Chiral alcohol production by NADH-dependent phenylacetaldehyde reductase coupled with in situ regeneration of NADH
    • Itoh N., Matsuda M., Mabuchi M., Dairi T., Wang J. Chiral alcohol production by NADH-dependent phenylacetaldehyde reductase coupled with in situ regeneration of NADH. Eur J Biochem. 269:2002;2394-2402.
    • (2002) Eur J Biochem , vol.269 , pp. 2394-2402
    • Itoh, N.1    Matsuda, M.2    Mabuchi, M.3    Dairi, T.4    Wang, J.5


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