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Volumn 20, Issue 4, 1997, Pages 248-258

Potential applications of NAD(P)-dependent oxidoreductases in synthesis: A survey

Author keywords

Cofactor; Electrochemistry; Electroenzymatic synthesis; NAD(P); Oxidoreductase; Synthesis

Indexed keywords

ELECTROCHEMISTRY; ORGANIC COMPOUNDS; SYNTHESIS (CHEMICAL);

EID: 0031104963     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(96)00120-2     Document Type: Article
Times cited : (108)

References (100)
  • 1
    • 0026569956 scopus 로고
    • Biocatalysis in the 1990s: A perspective
    • May, S. W. Biocatalysis in the 1990s: a perspective. Enzyme Microb. Technol. 1992, 14, 80-84
    • (1992) Enzyme Microb. Technol. , vol.14 , pp. 80-84
    • May, S.W.1
  • 2
    • 0005062733 scopus 로고
    • Continuous cofactor regeneration. Utilization of polymer bound NAD(H) for the production of optically active acids
    • Wandrey, C. and Bossow, B. Continuous cofactor regeneration. Utilization of polymer bound NAD(H) for the production of optically active acids. Int. Conf. Chem. Biotechnol. Biol. Act. Proc. 3rd 1987, 1, 195-214
    • (1987) Int. Conf. Chem. Biotechnol. Biol. Act. Proc. 3rd , vol.1 , pp. 195-214
    • Wandrey, C.1    Bossow, B.2
  • 3
    • 0342296500 scopus 로고
    • Tentatives de régénération du coenzyme NADH par réduction électrochimique et hydrogénation catalytique
    • Bergel, A., Durliat, H., and Comtat, M. Tentatives de régénération du coenzyme NADH par réduction électrochimique et hydrogénation catalytique. J. Chim. Phys. 1987, 84, 593-598
    • (1987) J. Chim. Phys. , vol.84 , pp. 593-598
    • Bergel, A.1    Durliat, H.2    Comtat, M.3
  • 4
    • 0012025444 scopus 로고
    • Thin-layer spectroelectrochemical study of the reversible reaction between nicotinamide adenine dinucleotide and flavin adenine dinucleotide
    • Bergel, A. and Comtat, M. Thin-layer spectroelectrochemical study of the reversible reaction between nicotinamide adenine dinucleotide and flavin adenine dinucleotide. J. Electroanal. Chem. 1991, 302, 219-231
    • (1991) J. Electroanal. Chem. , vol.302 , pp. 219-231
    • Bergel, A.1    Comtat, M.2
  • 6
    • 0000129259 scopus 로고
    • Efficient indirect electrochemical in situ regeneration of NADH: Electrochemically driven enzymatic reduction of pyruvate catalyzed by D-LDH
    • Ruppert, R., Herrmann, S., and Steckhan, E. Efficient indirect electrochemical in situ regeneration of NADH: Electrochemically driven enzymatic reduction of pyruvate catalyzed by D-LDH. Tetrahedron Lett. 1987, 28, 6583-6586
    • (1987) Tetrahedron Lett. , vol.28 , pp. 6583-6586
    • Ruppert, R.1    Herrmann, S.2    Steckhan, E.3
  • 8
    • 0025874120 scopus 로고
    • Direct electron transfer from modified glassy carbon electrodes carrying covalently immobilised mediators to a dissolved viologen accepting pyridine nucleotide oxidoreductase and dihydrolipoamide dehydrogenase
    • Paxinos, A. S., Günther, H., Schmedding, D. J. M., and Simon, H. Direct electron transfer from modified glassy carbon electrodes carrying covalently immobilised mediators to a dissolved viologen accepting pyridine nucleotide oxidoreductase and dihydrolipoamide dehydrogenase. Bioelectrochem. Bioenerg. 1991, 25, 425-436
    • (1991) Bioelectrochem. Bioenerg. , vol.25 , pp. 425-436
    • Paxinos, A.S.1    Günther, H.2    Schmedding, D.J.M.3    Simon, H.4
  • 9
    • 0027544151 scopus 로고
    • Electrochemical regeneration of nicotinamide cofactor using a polypyrrole rhodium bis-terpyridine modified electrode
    • Beley, M. and Collin, J.-P. Electrochemical regeneration of nicotinamide cofactor using a polypyrrole rhodium bis-terpyridine modified electrode. J. Mol. Catal. 1993, 79, 133-140
    • (1993) J. Mol. Catal. , vol.79 , pp. 133-140
    • Beley, M.1    Collin, J.-P.2
  • 11
    • 0000697019 scopus 로고
    • Enzyme-catalyzed organic synthesis: A comparison of strategies for in situ regeneration of NAD from NADH
    • Lee, L. G. and Whitesides, G. M. Enzyme-catalyzed organic synthesis: A comparison of strategies for in situ regeneration of NAD from NADH. J. Am. Chem. Soc. 1985, 107, 6999-7008
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 6999-7008
    • Lee, L.G.1    Whitesides, G.M.2
  • 13
    • 0027682561 scopus 로고
    • Chiral engineering breaks through the looking glass
    • Samdani, G. and Ondrey, G. Chiral engineering breaks through the looking glass. Chem. Eng. 1993, 100, (10), 35-39
    • (1993) Chem. Eng. , vol.100 , Issue.10 , pp. 35-39
    • Samdani, G.1    Ondrey, G.2
  • 15
    • 33845555834 scopus 로고
    • Asymmetric synthesis of γ-lactones. A facile synthesis of the sex pheronome of the Japanese beetle
    • Midland, M. and Nguyen, N. H. Asymmetric synthesis of γ-lactones. A facile synthesis of the sex pheronome of the Japanese beetle. J. Org. Chem. 1981, 46, 4107-4108
    • (1981) J. Org. Chem. , vol.46 , pp. 4107-4108
    • Midland, M.1    Nguyen, N.H.2
  • 16
    • 84944484180 scopus 로고
    • Atropine and the hyoscyamines - A study of the action of optical isomers
    • Cushny, A. R. Atropine and the hyoscyamines - a study of the action of optical isomers. J. Physiol. 1904, 30, 176-194
    • (1904) J. Physiol. , vol.30 , pp. 176-194
    • Cushny, A.R.1
  • 17
    • 85005697480 scopus 로고
    • Dehydrogenases for the synthesis of chiral compounds
    • Hummel, W. and Kula, M.-R. Dehydrogenases for the synthesis of chiral compounds. Eur. J. Biochem. 1989, 184, 1-13
    • (1989) Eur. J. Biochem. , vol.184 , pp. 1-13
    • Hummel, W.1    Kula, M.-R.2
  • 18
    • 0020292388 scopus 로고
    • Multienzyme systems in membrane reactors
    • Wandrey, C., Wichmann, R., and Jandel, A.-S. Multienzyme systems in membrane reactors. Enzyme Eng. 1982, 6, 61-67
    • (1982) Enzyme Eng. , vol.6 , pp. 61-67
    • Wandrey, C.1    Wichmann, R.2    Jandel, A.-S.3
  • 19
    • 0023620670 scopus 로고
    • Continuous enzymatic transformation in an enzyme-membrane reactor with simultaneous NADH regeneration
    • Kula, M.-R. and Wandrey, C. Continuous enzymatic transformation in an enzyme-membrane reactor with simultaneous NADH regeneration. Methods Enzymol. 1987, 136, 9-21
    • (1987) Methods Enzymol. , vol.136 , pp. 9-21
    • Kula, M.-R.1    Wandrey, C.2
  • 20
    • 84941889613 scopus 로고
    • Continuous enzymatic transformation in an enzyme membrane reactor with simultaneous NAD(H) regeneration
    • Wichmann, R., Wandrey, C., Bückmann, A. F., and Kula, M.-R. Continuous enzymatic transformation in an enzyme membrane reactor with simultaneous NAD(H) regeneration. Biotechnol. Bioeng. 1981, 23, 2789-2802
    • (1981) Biotechnol. Bioeng. , vol.23 , pp. 2789-2802
    • Wichmann, R.1    Wandrey, C.2    Bückmann, A.F.3    Kula, M.-R.4
  • 21
    • 0022151621 scopus 로고
    • Enzymatic production of L-amino acid with continuous coenzyme regeneration by liquid membrane technique
    • Makryaleas, K., Scheper, T., Schügerl, K., and Kula, M.-R. Enzymatic production of L-amino acid with continuous coenzyme regeneration by liquid membrane technique. Ger. Chem. Eng. 1985, 8, 345-350
    • (1985) Ger. Chem. Eng. , vol.8 , pp. 345-350
    • Makryaleas, K.1    Scheper, T.2    Schügerl, K.3    Kula, M.-R.4
  • 24
    • 0021647332 scopus 로고
    • L-amino acids from a racemic mixture of α-hydroxy acids
    • Wandrey, C., Fiolitakis, E., and Wichmann, U. L-amino acids from a racemic mixture of α-hydroxy acids. Ann. N.Y. Acad. Sci. 1984, 443, 91-94
    • (1984) Ann. N.Y. Acad. Sci. , vol.443 , pp. 91-94
    • Wandrey, C.1    Fiolitakis, E.2    Wichmann, U.3
  • 25
    • 0026417562 scopus 로고
    • Modelling of hollow-fiber capillary reactor for the production of L-alanine with coenzyme regeneration
    • Fujii, T., Miyawaki, O., and Yano, T. Modelling of hollow-fiber capillary reactor for the production of L-alanine with coenzyme regeneration. Biotechnol. Bioeng. 1991, 38, 1166-1172
    • (1991) Biotechnol. Bioeng. , vol.38 , pp. 1166-1172
    • Fujii, T.1    Miyawaki, O.2    Yano, T.3
  • 27
    • 84989446779 scopus 로고
    • Enzyme production of L-alanine from malic acid with malic enzyme and alanine dehydrogenase with coenzyme regeneration
    • Suye, S.-I., Kawagoe, M., and Inuta, S. Enzyme production of L-alanine from malic acid with malic enzyme and alanine dehydrogenase with coenzyme regeneration. Can. J. Chem. Eng. 1992, 70, 306-312
    • (1992) Can. J. Chem. Eng. , vol.70 , pp. 306-312
    • Suye, S.-I.1    Kawagoe, M.2    Inuta, S.3
  • 28
    • 0016327276 scopus 로고
    • + in an enzyme electrode and in model enzyme reactors
    • + in an enzyme electrode and in model enzyme reactors. Biochim. Biophys. Acta 1974, 370, 329-338
    • (1974) Biochim. Biophys. Acta , vol.370 , pp. 329-338
    • Davies, P.1    Mosbach, K.2
  • 29
    • 0020457004 scopus 로고
    • Regeneration of NADH with immobilized systems of alanine dehydrogenase and hydrogen-denydrogenase
    • Danielsson, B., Winqvist, F., Malpote, J. Y., and Mosbach, K. Regeneration of NADH with immobilized systems of alanine dehydrogenase and hydrogen-denydrogenase. Biotechnol. Lett. 1982, 4, 673-678
    • (1982) Biotechnol. Lett. , vol.4 , pp. 673-678
    • Danielsson, B.1    Winqvist, F.2    Malpote, J.Y.3    Mosbach, K.4
  • 30
  • 31
    • 0022884631 scopus 로고
    • L-phenylalanine dehydrogenase from Brevibacterium sp. for production of L-phenylalanine by reductive amination of phenylpyruvate
    • Hummel, W., Schmidt, E., Wandrey, C., and Kula, M.-R. L-phenylalanine dehydrogenase from Brevibacterium sp. for production of L-phenylalanine by reductive amination of phenylpyruvate. Appl. Microbiol. Biotechnol. 1986, 25, 175-185
    • (1986) Appl. Microbiol. Biotechnol. , vol.25 , pp. 175-185
    • Hummel, W.1    Schmidt, E.2    Wandrey, C.3    Kula, M.-R.4
  • 32
    • 0000798607 scopus 로고
    • Isolation of L-phenylalanine dehydrogenase from Rhodococcus sp, M4 and its application for the production of L-phenylalanine
    • Hummel, W., Schütte, H., Schmidt, E., Wandrey, C., and Kula, M.-R. Isolation of L-phenylalanine dehydrogenase from Rhodococcus sp, M4 and its application for the production of L-phenylalanine. Appl. Microbiol. Biotechnol. 1987, 26, 409-416
    • (1987) Appl. Microbiol. Biotechnol. , vol.26 , pp. 409-416
    • Hummel, W.1    Schütte, H.2    Schmidt, E.3    Wandrey, C.4    Kula, M.-R.5
  • 33
    • 0343166044 scopus 로고
    • Multiple steady states in a coupled enzyme system represented by enzymatically catalysed production of L-phenylalanine
    • Schmidt, E., Fiolitakis, E., and Wandrey, C. Multiple steady states in a coupled enzyme system represented by enzymatically catalysed production of L-phenylalanine. Ann. N. Y. Acad. Sci. 1987, 501, 434-437
    • (1987) Ann. N. Y. Acad. Sci. , vol.501 , pp. 434-437
    • Schmidt, E.1    Fiolitakis, E.2    Wandrey, C.3
  • 34
    • 0023268854 scopus 로고
    • Enzymatic production of L-phenylalanine from the racemic mixture of D, L-phenyllactate. Modelling of the reactor
    • Schmidt, E., Vasic-Racki, D., and Wandrey, C. Enzymatic production of L-phenylalanine from the racemic mixture of D, L-phenyllactate. Modelling of the reactor. Appl. Microbiol. Technol. 1987, 26, 42-48
    • (1987) Appl. Microbiol. Technol. , vol.26 , pp. 42-48
    • Schmidt, E.1    Vasic-Racki, D.2    Wandrey, C.3
  • 35
    • 0013619882 scopus 로고
    • Isolation and characterization of acetamidocinnamate acylase, a new enzyme suitable for production of L-phenylalanine
    • Hummel, W., Schütte, H., Schmidt, E. and Kula, M.-R. Isolation and characterization of acetamidocinnamate acylase, a new enzyme suitable for production of L-phenylalanine. Appl. Microbiol. Biotechnol. 1987, 27, 283-291
    • (1987) Appl. Microbiol. Biotechnol. , vol.27 , pp. 283-291
    • Hummel, W.1    Schütte, H.2    Schmidt, E.3    Kula, M.-R.4
  • 37
    • 0000755745 scopus 로고
    • L-Lactate dehydrogenase: Substrate specificity and use as a catalyst in the synthesis of homochiral 2-hydroxy acids
    • Kim, M.-J. and Whitesides, G. M. L-Lactate dehydrogenase: Substrate specificity and use as a catalyst in the synthesis of homochiral 2-hydroxy acids. J. Am. Chem. Soc. 1988, 110, 2959-2964
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 2959-2964
    • Kim, M.-J.1    Whitesides, G.M.2
  • 38
    • 0023834373 scopus 로고
    • Enzymatic synthesis of (S)-(-)-3-(3,4-Dihydroxy-phenyl) lactic acid
    • Rao, N. N. and Roth, H. J. Enzymatic synthesis of (S)-(-)-3-(3,4-Dihydroxy-phenyl) lactic acid. Arch. Pharm. (Weinheim) 1988, 321, 179-180
    • (1988) Arch. Pharm. (Weinheim) , vol.321 , pp. 179-180
    • Rao, N.N.1    Roth, H.J.2
  • 39
    • 0026515583 scopus 로고
    • Potential of R-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei for stereospecific reductions
    • Kallwass, H. K. W. Potential of R-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei for stereospecific reductions. Enzyme Microb. Technol. 1992, 14, 28-35
    • (1992) Enzyme Microb. Technol. , vol.14 , pp. 28-35
    • Kallwass, H.K.W.1
  • 40
    • 0000935831 scopus 로고
    • Laboratory-scale enzymatic/chemical synthesis of D-and L-β-chlorolactic acid and D-and L-potassium glycidate
    • Hirschbein, B. L. and Whitesides, G. M. Laboratory-scale enzymatic/chemical synthesis of D-and L-β-chlorolactic acid and D-and L-potassium glycidate. J. Am. Chem. Soc. 1982, 104, 4458-4460
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4458-4460
    • Hirschbein, B.L.1    Whitesides, G.M.2
  • 41
    • 0000800444 scopus 로고
    • Enantioselective oxidation of 1,2-diols to L-α-hydroxy acids using coimmobilized alcohol and aldehyde dehydrogenases as catalysts
    • Wong, C.-H. and Matos, J. R. Enantioselective oxidation of 1,2-diols to L-α-hydroxy acids using coimmobilized alcohol and aldehyde dehydrogenases as catalysts. J. Org. Chem. 1985, 50, 1992-1994
    • (1985) J. Org. Chem. , vol.50 , pp. 1992-1994
    • Wong, C.-H.1    Matos, J.R.2
  • 42
    • 33847087242 scopus 로고
    • Enzyme-catalysed organic synthesis: NADH regeneration by using formate dehydrogenase
    • Shaked, Z. and Whitesides, G. M. Enzyme-catalysed organic synthesis: NADH regeneration by using formate dehydrogenase. J. Am. Chem. Soc. 1980, 102, 7104-7105
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 7104-7105
    • Shaked, Z.1    Whitesides, G.M.2
  • 43
    • 0000999905 scopus 로고
    • Enzyme-catalyzed organic synthesis: NAD(P)H cofactor regeneration by using glucose-6-phosphate and glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides
    • Wong, C.-H. and Whitesides, G. M. Enzyme-catalyzed organic synthesis: NAD(P)H cofactor regeneration by using glucose-6-phosphate and glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides. J. Am. Chem. Soc. 1981, 103, 4890-4899
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 4890-4899
    • Wong, C.-H.1    Whitesides, G.M.2
  • 44
    • 0001389862 scopus 로고
    • Enzyme-catalysed organic synthesis: NAD(P)H regeneration using dihydrogen and the dehydrogenase from Methanobacterium thermoautotrophicum
    • Wong, C.-H., Daniels, L., Orme-Johnson, W. H., and Whitesides, G. M. Enzyme-catalysed organic synthesis: NAD(P)H regeneration using dihydrogen and the dehydrogenase from Methanobacterium thermoautotrophicum. J Am. Chem. Soc. 1981, 103, 6227-6228
    • (1981) J Am. Chem. Soc. , vol.103 , pp. 6227-6228
    • Wong, C.-H.1    Daniels, L.2    Orme-Johnson, W.H.3    Whitesides, G.M.4
  • 45
    • 0022076889 scopus 로고
    • Enzymatic vs. Fermentative synthesis: Thermostable glucose dehydrogenase catalysed regeneration of NAD(P)H for use in enzymatic synthesis
    • Wong, C.-H., Drueckhammer, D. G., and Sweers, H. M. Enzymatic vs. fermentative synthesis: Thermostable glucose dehydrogenase catalysed regeneration of NAD(P)H for use in enzymatic synthesis. J. Am. Chem. Soc. 1985, 107, 4028-4031
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 4028-4031
    • Wong, C.-H.1    Drueckhammer, D.G.2    Sweers, H.M.3
  • 47
    • 0000708089 scopus 로고
    • Complete conversion of L-lactate and D-lactate. A generic approach involving enzymatic catalysis, electrochemical oxidation of NADH, and electrochemical reduction of pyruvate
    • Biade, A.-E. Bourdillon, C., Laval J.-M., Mairesse, G., and Moiroux, J. Complete conversion of L-lactate and D-lactate. A generic approach involving enzymatic catalysis, electrochemical oxidation of NADH, and electrochemical reduction of pyruvate. J. Am. Chem. Soc. 1992, 114, 893-897
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 893-897
    • Biade, A.-E.1    Bourdillon, C.2    Laval, J.-M.3    Mairesse, G.4    Moiroux, J.5
  • 48
    • 0001132548 scopus 로고
    • Membrane-enclosed electroenzymatic catalysis with a low molecular weight electron-transfer mediator
    • Grimes, M. T. and Drueckhammer, D. G. Membrane-enclosed electroenzymatic catalysis with a low molecular weight electron-transfer mediator. J. Org. Chem. 1993, 58, 6148-6150
    • (1993) J. Org. Chem. , vol.58 , pp. 6148-6150
    • Grimes, M.T.1    Drueckhammer, D.G.2
  • 49
    • 0342296491 scopus 로고
    • Synthèse réductive de la L-carnitine par voie enzymatique avec regeneration du NADH utilise
    • Vandecasteele, J.-P. and Lemal, J. Synthèse réductive de la L-carnitine par voie enzymatique avec regeneration du NADH utilise. Bull. Soc. Chim. Fr 1980, 1-2, II-101-103
    • (1980) Bull. Soc. Chim. Fr , vol.1-2
    • Vandecasteele, J.-P.1    Lemal, J.2
  • 50
    • 0026857665 scopus 로고
    • NADPH regeneration by glucose dehydrogenase from Gluconobacter scleroides for L-leucovorin synthesis
    • Eguchi, T., Kuge, Y., Inoue, K., Yoshikawa, N., Mochida, K., and Uwajima, T. NADPH regeneration by glucose dehydrogenase from Gluconobacter scleroides for L-leucovorin synthesis. Biosci. Biotechnol. Biochem. 1992, 56, 701-703
    • (1992) Biosci. Biotechnol. Biochem. , vol.56 , pp. 701-703
    • Eguchi, T.1    Kuge, Y.2    Inoue, K.3    Yoshikawa, N.4    Mochida, K.5    Uwajima, T.6
  • 51
    • 0020790310 scopus 로고
    • Enzyme-catalysed organic synthesis: Regeneration of deuterated nicotinamide cofactors for use in large-scale enzymatic synthesis of deuterated substances
    • Wong, C.-H. and Whitesides, G. M. Enzyme-catalysed organic synthesis: Regeneration of deuterated nicotinamide cofactors for use in large-scale enzymatic synthesis of deuterated substances. J. Am. Chem. Soc. 1983, 105, 5012-5014
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 5012-5014
    • Wong, C.-H.1    Whitesides, G.M.2
  • 52
    • 0342296490 scopus 로고    scopus 로고
    • The development of membrane reactors for enzyme processes-processing laboratory results to a commercial scale
    • Manchester
    • Bommarius, A. S., Schwarm, M., and Drauz, K. The development of membrane reactors for enzyme processes-processing laboratory results to a commercial scale. In: Industrial Biocatalysis: Making It Happen. Proc. InBio'96. Manchester, 1996
    • (1996) Industrial Biocatalysis: Making It Happen. Proc. InBio'96
    • Bommarius, A.S.1    Schwarm, M.2    Drauz, K.3
  • 53
    • 0000561789 scopus 로고
    • Enzymes in organic synthesis. 25. Heterocyclic ketones as substrates of horse liver alcohol dehydrogenase. Highly stereoselective reductions of 2-substituted tetrahydropyran-4-ones
    • Haslegrave, J. A. and Jones, J. B. Enzymes in organic synthesis. 25. Heterocyclic ketones as substrates of horse liver alcohol dehydrogenase. Highly stereoselective reductions of 2-substituted tetrahydropyran-4-ones. J. Am. Chem. Soc. 1982, 104, 4666-4671
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4666-4671
    • Haslegrave, J.A.1    Jones, J.B.2
  • 54
    • 84989152381 scopus 로고
    • Synthetic applications of alcohol dehydrogenase from Thermoanaerobium brockii
    • Keinan, E., Seth, K. K., and Lamed, R. Synthetic applications of alcohol dehydrogenase from Thermoanaerobium brockii. Ann. N. Y. Acad. Sci. 1987, 501, 130-149
    • (1987) Ann. N. Y. Acad. Sci. , vol.501 , pp. 130-149
    • Keinan, E.1    Seth, K.K.2    Lamed, R.3
  • 55
    • 0025037430 scopus 로고
    • Continuous coenzyme dependent stereoselective synthesis of sulcatol by alcohol dehydrogenase
    • Röthig, T. R., Kulbe, K. D., Bückmann, F., and Carrea, G. Continuous coenzyme dependent stereoselective synthesis of sulcatol by alcohol dehydrogenase. Biotechnol. Lett. 1990, 12, 353-356
    • (1990) Biotechnol. Lett. , vol.12 , pp. 353-356
    • Röthig, T.R.1    Kulbe, K.D.2    Bückmann, F.3    Carrea, G.4
  • 56
    • 0025636482 scopus 로고
    • Rejection and continuous regeneration of the native coenzyme NAD(P)H in a charged membrane enzyme reactor
    • Kulbe, K. D., Howaldt, M. W., Schmidt, K., Röthig, T. R., and Chmiel, H. Rejection and continuous regeneration of the native coenzyme NAD(P)H in a charged membrane enzyme reactor. Ann. N. Y. Acad. Sci. 1990, 613, 820-826
    • (1990) Ann. N. Y. Acad. Sci. , vol.613 , pp. 820-826
    • Kulbe, K.D.1    Howaldt, M.W.2    Schmidt, K.3    Röthig, T.R.4    Chmiel, H.5
  • 57
    • 0023473067 scopus 로고
    • Regeneration of NADPH and hydrogenation of ketones to alcohols with the combination of hydrogenase, ferredoxin-NADP reductase, and alcohol dehydrogenase
    • Okura, I., Kurabayashi, K., and Aono, S. Regeneration of NADPH and hydrogenation of ketones to alcohols with the combination of hydrogenase, ferredoxin-NADP reductase, and alcohol dehydrogenase. Bull. Chem. Soc. Jpn. 1987, 60, 3663-3666
    • (1987) Bull. Chem. Soc. Jpn. , vol.60 , pp. 3663-3666
    • Okura, I.1    Kurabayashi, K.2    Aono, S.3
  • 58
    • 18244423206 scopus 로고
    • Regeneration of NADH and ketone hydrogenation by hydrogen with the combination of hydrogenase and alcohol dehydrogenase
    • Okura, I., Otsuka, K., Nakada, N., and Hasumi, F. Regeneration of NADH and ketone hydrogenation by hydrogen with the combination of hydrogenase and alcohol dehydrogenase. Appl. Biochem. Biotechnol. 1990, 24/25, 425-430
    • (1990) Appl. Biochem. Biotechnol. , vol.24-25 , pp. 425-430
    • Okura, I.1    Otsuka, K.2    Nakada, N.3    Hasumi, F.4
  • 59
    • 0024639573 scopus 로고
    • Regeneration of NADH and ketone hydrogenation by hydrogen with the combination of hydrogenase and alcohol dehydrogenase
    • Otsuka, K., Aono, S., Okura, I., and Hasumi, F. Regeneration of NADH and ketone hydrogenation by hydrogen with the combination of hydrogenase and alcohol dehydrogenase. J. Mol. Catal. 1989, 51, 35-39
    • (1989) J. Mol. Catal. , vol.51 , pp. 35-39
    • Otsuka, K.1    Aono, S.2    Okura, I.3    Hasumi, F.4
  • 60
    • 0342296489 scopus 로고
    • Formate-driven non-enzymatic NAD(P)H regeneration for the ADH-catalysed stereoselective reduction of 4-phenyl-2-butanone
    • VCH Verlagsgesellschaft
    • Westerhausen, D. and Steckhan, E. Formate-driven non-enzymatic NAD(P)H regeneration for the ADH-catalysed stereoselective reduction of 4-phenyl-2-butanone. DECHEMA Biotechnol. Conf. 5, VCH Verlagsgesellschaft, 1992, 105-108
    • (1992) DECHEMA Biotechnol. Conf. 5 , pp. 105-108
    • Westerhausen, D.1    Steckhan, E.2
  • 61
    • 0025059329 scopus 로고
    • Enzyme-catalyzed synthesis of optically pure R(+)-phenylethanol
    • Hummel, W. Enzyme-catalyzed synthesis of optically pure R(+)-phenylethanol. Biotechnol. Lett. 1990, 12, 403-408
    • (1990) Biotechnol. Lett. , vol.12 , pp. 403-408
    • Hummel, W.1
  • 62
    • 0001275962 scopus 로고
    • Preparation of optically active 1,2-diols and α-hydroxy ketones using glycerol dehydrogenase as catalyst: Limits to enzyme-catalysed synthesis due to noncompetitive and mixed inhibition by product
    • Lee, L. G. and Whitesides, G. M. Preparation of optically active 1,2-diols and α-hydroxy ketones using glycerol dehydrogenase as catalyst: Limits to enzyme-catalysed synthesis due to noncompetitive and mixed inhibition by product. J. Org. Chem. 1986, 51, 25-36
    • (1986) J. Org. Chem. , vol.51 , pp. 25-36
    • Lee, L.G.1    Whitesides, G.M.2
  • 63
    • 0025435214 scopus 로고
    • Two-phase system membrane reactor with cofactor recycling
    • Kise, S. and Hayashida, M. Two-phase system membrane reactor with cofactor recycling. J. Biotechnol. 1990, 14, 221-228
    • (1990) J. Biotechnol. , vol.14 , pp. 221-228
    • Kise, S.1    Hayashida, M.2
  • 64
    • 0001239248 scopus 로고
    • Regeneration of NAD(P)H using glucose 6-sulfate and glucose 6-phosphate dehydrogenase
    • Wong, C.-H., Gordon, J., Cooney, C. L., and Whitesides, G. M. Regeneration of NAD(P)H using glucose 6-sulfate and glucose 6-phosphate dehydrogenase. J. Org. Chem. 1981, 46, 4676-4679
    • (1981) J. Org. Chem. , vol.46 , pp. 4676-4679
    • Wong, C.-H.1    Gordon, J.2    Cooney, C.L.3    Whitesides, G.M.4
  • 65
    • 33845374385 scopus 로고
    • Asymmetric oxidoreductions catalyzed by alcohol dehydrogenase in organic solvents
    • Grunwald, J., Wirz, B., Scollar, M. P., and Klibanov, A. M. Asymmetric oxidoreductions catalyzed by alcohol dehydrogenase in organic solvents. J. Am. Chem. Soc. 1986, 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
  • 66
    • 0021969313 scopus 로고
    • Regeneration and retention of NADP(H) for xylitol production in an ionized membrane reactor
    • Kitpreechavanich, V., Nishio, N., Hayashi, M., and Nagai, S. Regeneration and retention of NADP(H) for xylitol production in an ionized membrane reactor. Biorechnol. Lett. 1985, 7, 657-662
    • (1985) Biorechnol. Lett. , vol.7 , pp. 657-662
    • Kitpreechavanich, V.1    Nishio, N.2    Hayashi, M.3    Nagai, S.4
  • 67
    • 0025442982 scopus 로고
    • Sorbitol production in charged membrane bioreactor with coenzyme regeneration system: I. Selective retainment of NADP(H) in a continuous reaction
    • Ikemi, M., Koizumi, N., and Ishimatsu, Y. Sorbitol production in charged membrane bioreactor with coenzyme regeneration system: I. Selective retainment of NADP(H) in a continuous reaction, Biotechnol. Bioeng. 1990, 36, 149-154
    • (1990) Biotechnol. Bioeng. , vol.36 , pp. 149-154
    • Ikemi, M.1    Koizumi, N.2    Ishimatsu, Y.3
  • 68
    • 0016722076 scopus 로고
    • Kinetics of a hallow fiber dehydrogenase reactor
    • Fink, D. J. and Rodwell, V. W. Kinetics of a hallow fiber dehydrogenase reactor. Biotechnol. Bioeng. 1975, 17, 1029-1050
    • (1975) Biotechnol. Bioeng. , vol.17 , pp. 1029-1050
    • Fink, D.J.1    Rodwell, V.W.2
  • 69
    • 0026417364 scopus 로고
    • The effects of electrochemical regeneration upon the enzymatic catalysts of a thermodynamically unfavorable reaction
    • Laval, J. M., Moiroux, J., and Bourdillon, C. The effects of electrochemical regeneration upon the enzymatic catalysts of a thermodynamically unfavorable reaction. Biotechnol. Bioeng. 1991, 38, 788-796
    • (1991) Biotechnol. Bioeng. , vol.38 , pp. 788-796
    • Laval, J.M.1    Moiroux, J.2    Bourdillon, C.3
  • 70
    • 0026565382 scopus 로고
    • Displacement of equilibrium in electroenzymatic reactor for acetaldehyde production using yeast alcohol dehydrogenase
    • Lortie, R., Fassouane, A., Laval, J.-M., and Bourdillon, C. Displacement of equilibrium in electroenzymatic reactor for acetaldehyde production using yeast alcohol dehydrogenase. Biotechnol. Bioeng. 1990, 39, 157-163
    • (1990) Biotechnol. Bioeng. , vol.39 , pp. 157-163
    • Lortie, R.1    Fassouane, A.2    Laval, J.-M.3    Bourdillon, C.4
  • 71
    • 84988112879 scopus 로고
    • Enzymatic production of long-chain aldehydes in a fixed bed reactor using organic solvents and cofactor regeneration
    • Lortie, R., Villaume, I., Legoy, M. D., and Thomas, D. Enzymatic production of long-chain aldehydes in a fixed bed reactor using organic solvents and cofactor regeneration. Biotechnol. Bioeng. 1989, 33, 229-232
    • (1989) Biotechnol. Bioeng. , vol.33 , pp. 229-232
    • Lortie, R.1    Villaume, I.2    Legoy, M.D.3    Thomas, D.4
  • 72
    • 0017778716 scopus 로고
    • Asymmetric synthesis via enantiotopically selective horse liver alcohol dehydrogenase catalysed oxidations of diols containing a prochiral center
    • Irwin, A. J. and Jones, J. B. Asymmetric synthesis via enantiotopically selective horse liver alcohol dehydrogenase catalysed oxidations of diols containing a prochiral center. J. Am. Chem. Soc. 1977, 99, 556-561
    • (1977) J. Am. Chem. Soc. , vol.99 , pp. 556-561
    • Irwin, A.J.1    Jones, J.B.2
  • 73
    • 0000561788 scopus 로고
    • Enzymes in organic synthesis. 24. Preparations of enantiomerically pure chiral lactones via stereo-specific horse liver alcohol dehydrogenase catalysed oxidations of monocyclic meso diols
    • Jakovac, I. J., Goodbrand, H. B., Lok, K. P., and Jones, J. B. Enzymes in organic synthesis. 24. Preparations of enantiomerically pure chiral lactones via stereo-specific horse liver alcohol dehydrogenase catalysed oxidations of monocyclic meso diols. J. Am. Chem. Soc. 1982, 104, 4659-4665
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4659-4665
    • Jakovac, I.J.1    Goodbrand, H.B.2    Lok, K.P.3    Jones, J.B.4
  • 74
    • 0001734660 scopus 로고
    • FMN reductase catalysed regeneration of NAD(P) for use in enzymatic synthesis
    • Drueckhammer, D. G., Riddle, V. W., and Wong, C.-H. FMN reductase catalysed regeneration of NAD(P) for use in enzymatic synthesis. J. Org. Chem. 1985, 50, 5387-5389
    • (1985) J. Org. Chem. , vol.50 , pp. 5387-5389
    • Drueckhammer, D.G.1    Riddle, V.W.2    Wong, C.-H.3
  • 75
    • 0005104386 scopus 로고
    • Biphasic one-pot synthesis of two useful and separable compounds using cofactor-requiring enzymatic reactions: Glutamate dehydrogenase catalysed synthesis of L-α-aminoadipate coupled with alcohol dehydrogenase catalysed synthesis of a chiral lactone
    • Matos, J. R. and Wong, C.-H. J. Biphasic one-pot synthesis of two useful and separable compounds using cofactor-requiring enzymatic reactions: Glutamate dehydrogenase catalysed synthesis of L-α-aminoadipate coupled with alcohol dehydrogenase catalysed synthesis of a chiral lactone. J. Org. Chem. 1986, 51, 2388-2389
    • (1986) J. Org. Chem. , vol.51 , pp. 2388-2389
    • Matos, J.R.1    Wong, C.-H.J.2
  • 79
    • 0021423717 scopus 로고
    • Enzymatic preparation of 12-ketochenodeoxycholic acid with NADP regeneration
    • Carrea, G., Bovara, R., Cremonesi, P., and Lordi, R. Enzymatic preparation of 12-ketochenodeoxycholic acid with NADP regeneration. Biotechnol. Bioeng. 1984, 26, 560-563
    • (1984) Biotechnol. Bioeng. , vol.26 , pp. 560-563
    • Carrea, G.1    Bovara, R.2    Cremonesi, P.3    Lordi, R.4
  • 81
    • 10044253384 scopus 로고
    • Charged membrane enzyme reactors for continuous regeneration of native coenzymes. II. Synthesis of hydrophobic compounds with NADP(H) dependent dehydrogenase
    • VCH Verlagsgesellschaft
    • Röthig, T. R., Schmidt, K., Chmiel, H., Hasenfratz, H., and Kulbe, K. D. Charged membrane enzyme reactors for continuous regeneration of native coenzymes. II. Synthesis of hydrophobic compounds with NADP(H) dependent dehydrogenase. DECHEMA Biotechnol. Conf. 3 VCH Verlagsgesellschaft, 1989, 643-647
    • (1989) DECHEMA Biotechnol. Conf. 3 , pp. 643-647
    • Röthig, T.R.1    Schmidt, K.2    Chmiel, H.3    Hasenfratz, H.4    Kulbe, K.D.5
  • 82
    • 37049086140 scopus 로고
    • Efficient preparative-scale enzymatic synthesis of specifically deuteriated bile acids
    • Riva, S., Ottolina, G., and Carrea, G. Efficient preparative-scale enzymatic synthesis of specifically deuteriated bile acids. J. Chem. Soc. Perkin Trans. 1989, 1, 2073-2074
    • (1989) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 2073-2074
    • Riva, S.1    Ottolina, G.2    Carrea, G.3
  • 83
    • 4243408774 scopus 로고
    • Utilisation des hydroxysteroïdes déshydrogénases en milieu non aqueux. Recyclage du cofacteur pyridinique
    • Legoy, M. D. and Thomas, D. Utilisation des hydroxysteroïdes déshydrogénases en milieu non aqueux. Recyclage du cofacteur pyridinique. Bull. Soc. Chim. Fr. 1980, 1-2, II-98-100
    • (1980) Bull. Soc. Chim. Fr. , vol.1-2
    • Legoy, M.D.1    Thomas, D.2
  • 84
    • 85047689907 scopus 로고
    • Steroid modifications with immobilized biocatalysts-use of immobilized enzyme-requiring cofactor regeneration and of immobilized mycelium
    • Ergan, F., Atrai, P., Dhulster, P., Gellf, G., Kim, M. N. Legoy, M. D., and Thomas, D. Steroid modifications with immobilized biocatalysts-use of immobilized enzyme-requiring cofactor regeneration and of immobilized mycelium. Z. Allg. Mikrobiol. 1982, 22, 607-615
    • (1982) Z. Allg. Mikrobiol. , vol.22 , pp. 607-615
    • Ergan, F.1    Atrai, P.2    Dhulster, P.3    Gellf, G.4    Kim, M.N.5    Legoy, M.D.6    Thomas, D.7
  • 85
    • 0021647367 scopus 로고
    • Selection and micro-encapsulation of "NADH-oxidying" bacterium and its use for NAD regeneration
    • Ergan, F., Thomas, D., and Chang, T. M. S. Selection and micro-encapsulation of "NADH-oxidying" bacterium and its use for NAD regeneration. Appl. Biochem. Biotechnol. 1984, 10, 61-71
    • (1984) Appl. Biochem. Biotechnol. , vol.10 , pp. 61-71
    • Ergan, F.1    Thomas, D.2    Chang, T.M.S.3
  • 87
    • 0024035118 scopus 로고
    • Enzymatic oxido-reduction of steroids in two-phase systems: Effects of organic solvents on enzyme kinetics and evaluation of the performance of different reactors
    • Carrea, G., Riva, S., Bovara, R., and Pasta, P. Enzymatic oxido-reduction of steroids in two-phase systems: Effects of organic solvents on enzyme kinetics and evaluation of the performance of different reactors. Enzyme Microb. Technol. 1988, 10, 333-340
    • (1988) Enzyme Microb. Technol. , vol.10 , pp. 333-340
    • Carrea, G.1    Riva, S.2    Bovara, R.3    Pasta, P.4
  • 88
    • 0001604360 scopus 로고
    • Enzyme-catalysed steroid transformations in water-organic solvent two-phase systems
    • Carrea, G. and Cremonesi, P. Enzyme-catalysed steroid transformations in water-organic solvent two-phase systems. Methods Enzymol. 1987, 136, 150-157
    • (1987) Methods Enzymol. , vol.136 , pp. 150-157
    • Carrea, G.1    Cremonesi, P.2
  • 89
    • 0028447421 scopus 로고
    • Electrochemical conversion of carbon dioxide to methanol with the assistance of formate dehydrogenase and methanol dehydrogenase as biocatalysts
    • Kuwabata, S., Tsuda, R., and Yoneyama, H. Electrochemical conversion of carbon dioxide to methanol with the assistance of formate dehydrogenase and methanol dehydrogenase as biocatalysts. J. Am. Chem. Soc. 1994, 116, 5437-5443
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 5437-5443
    • Kuwabata, S.1    Tsuda, R.2    Yoneyama, H.3
  • 90
    • 0028448548 scopus 로고
    • Photochemical reduction of carbon dioxide to methanol using ZnS microcrystallite as photocatalyst in the presence of methanol dehydrogenase
    • Kuwabata, S., Nishida, K., Tsuda, R., Inoue, H., and Yoneyama, H. Photochemical reduction of carbon dioxide to methanol using ZnS microcrystallite as photocatalyst in the presence of methanol dehydrogenase. J. Electrochem. Soc. 1994, 141, 1498-1503
    • (1994) J. Electrochem. Soc. , vol.141 , pp. 1498-1503
    • Kuwabata, S.1    Nishida, K.2    Tsuda, R.3    Inoue, H.4    Yoneyama, H.5
  • 91
    • 0006523896 scopus 로고
    • Electrochemical fixation of carbon dioxide in oxoglutaric acid using an enzyme as an electrobiocatalyst
    • Suigimura, K., Kuwabata, S., and Yoneyama, H. Electrochemical fixation of carbon dioxide in oxoglutaric acid using an enzyme as an electrobiocatalyst. J. Am. Chem. Soc. 1989, 111, 2361-2362
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 2361-2362
    • Suigimura, K.1    Kuwabata, S.2    Yoneyama, H.3
  • 92
    • 0342731484 scopus 로고
    • 2 in acetyl-coenzyme A to yield pyruvic acid using pyruvate dehydrogenase complexes as an electrobiocatalyst
    • 2 in acetyl-coenzyme A to yield pyruvic acid using pyruvate dehydrogenase complexes as an electrobiocatalyst. Chem Lett. 1990, 1151-1154
    • (1990) Chem Lett. , pp. 1151-1154
    • Kuwabata, S.1    Morishita, N.2    Yoneyama, H.3
  • 93
    • 0342731477 scopus 로고
    • Electrochemical fixation of carbon dioxide in pyruvic acid to yield malic acid using malic enzyme as an electrobiocatalyst
    • Sugimura, K., Kuwabata, S., and Yoneyama, H. Electrochemical fixation of carbon dioxide in pyruvic acid to yield malic acid using malic enzyme as an electrobiocatalyst. Bioelectrochem. Bioenerg. 1990, 24, 241-247
    • (1990) Bioelectrochem. Bioenerg. , vol.24 , pp. 241-247
    • Sugimura, K.1    Kuwabata, S.2    Yoneyama, H.3
  • 94
    • 0026816759 scopus 로고
    • Reduction of nitrate and nitrite in water by immobilized enzymes
    • Mellor, R. B., Ronnenberg, J., Campbell, W. H., and Diekmann, S. Reduction of nitrate and nitrite in water by immobilized enzymes. Nature 1992, 355, 717-719
    • (1992) Nature , vol.355 , pp. 717-719
    • Mellor, R.B.1    Ronnenberg, J.2    Campbell, W.H.3    Diekmann, S.4
  • 95
    • 0043138644 scopus 로고
    • Metal-dependent conversion of inorganic nitrogen and sulfur compounds
    • Kroneck, P. M. H., Beuerle, J., and Schumacher, W. Metal-dependent conversion of inorganic nitrogen and sulfur compounds. Met. Ions Biol. Syst. 1992, 28, 455-505
    • (1992) Met. Ions Biol. Syst. , vol.28 , pp. 455-505
    • Kroneck, P.M.H.1    Beuerle, J.2    Schumacher, W.3
  • 98
    • 0028040633 scopus 로고
    • Influence of redox potential on the anaerobic biotransformation of nitrogen-heterocyclic compounds in anoxic fresh-water sediments
    • Liu, S. M., Jones, W. J., and Rogers, J. E. Influence of redox potential on the anaerobic biotransformation of nitrogen-heterocyclic compounds in anoxic fresh-water sediments. Appl. Microbiol. Biotecnnol. 1994, 41, 717-724
    • (1994) Appl. Microbiol. Biotecnnol. , vol.41 , pp. 717-724
    • Liu, S.M.1    Jones, W.J.2    Rogers, J.E.3
  • 99
    • 4244212316 scopus 로고
    • Biology boots waste treatment
    • Fouhy, K. and Grinthal, W. Biology boots waste treatment. Chem. Eng. 1994, 101-2, 30-31
    • (1994) Chem. Eng. , vol.2-101 , pp. 30-31
    • Fouhy, K.1    Grinthal, W.2
  • 100
    • 0025305410 scopus 로고
    • Sulfur removal from coal through multiphase media containing biocatalysts
    • Lee, K. I. and Yen, T. F. Sulfur removal from coal through multiphase media containing biocatalysts. J. Chem. Technol. Biotechnol. 1990, 48, 71-79
    • (1990) J. Chem. Technol. Biotechnol. , vol.48 , pp. 71-79
    • Lee, K.I.1    Yen, T.F.2


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