메뉴 건너뛰기




Volumn 21, Issue 8, 1997, Pages 559-571

The enantiomeric ratio: Origin, determination and prediction

Author keywords

Chirality; Enantioselectivity; Intrinsic enantiomeric ratio; Kinetic resolution; Molecular modeling

Indexed keywords

CATALYSIS; CATALYST SELECTIVITY; COMPUTER SIMULATION; GIBBS FREE ENERGY; MOLECULAR DYNAMICS; MOLECULAR STRUCTURE;

EID: 0031455616     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(97)00066-5     Document Type: Article
Times cited : (214)

References (87)
  • 3
    • 33749942544 scopus 로고
    • Chiral drugs
    • September 19
    • Stinson, S. C. Chiral drugs. Chem. Eng. News 1994, September 19, 38-72
    • (1994) Chem. Eng. News , pp. 38-72
    • Stinson, S.C.1
  • 5
    • 84988074926 scopus 로고
    • Symbolism and terminology in enzyme kinetics
    • NC-IUB. Symbolism and terminology in enzyme kinetics. Eur. J. Biochem. 1982, 128, 281-291
    • (1982) Eur. J. Biochem. , vol.128 , pp. 281-291
  • 6
    • 85088081160 scopus 로고
    • Specificity constants for two-substrate reactions
    • Barnsley, E. A. Specificity constants for two-substrate reactions. Biochem. J. 1993, 291, 323
    • (1993) Biochem. J. , vol.291 , pp. 323
    • Barnsley, E.A.1
  • 8
    • 0002382567 scopus 로고
    • Asymmetric syntheses and resolutions
    • Jones, J. B., Sih, C. J., and Perlman, D., Eds. John Wiley & Sons, New York
    • Jones, J. B. and Beck, J. F. Asymmetric syntheses and resolutions. In: Applications of Biochemical Systems in Organic Chemistry Part I (Jones, J. B., Sih, C. J., and Perlman, D., Eds.). John Wiley & Sons, New York, 1976, 107-401
    • (1976) Applications of Biochemical Systems in Organic Chemistry Part I , pp. 107-401
    • Jones, J.B.1    Beck, J.F.2
  • 9
    • 33947480286 scopus 로고
    • Steric course and specificity of α-chymotrypsin-catalysed reactions
    • Hein, G. E. and Niemann, C. Steric course and specificity of α-chymotrypsin-catalysed reactions. J. Am. Chem. Soc. 1962, 90, 4487-4494
    • (1962) J. Am. Chem. Soc. , vol.90 , pp. 4487-4494
    • Hein, G.E.1    Niemann, C.2
  • 10
    • 20644469267 scopus 로고
    • Quantitative analysis of biochemical kinetic resolutions of enantiomers
    • Chen, C.-S., Fujimoto, Y., Girdaukas, G., and Sih, C. J. Quantitative analysis of biochemical kinetic resolutions of enantiomers. J. Am. Chem. Soc. 1982, 104, 7294-7299
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 7294-7299
    • Chen, C.-S.1    Fujimoto, Y.2    Girdaukas, G.3    Sih, C.J.4
  • 11
    • 8044227965 scopus 로고
    • Preparation of chiral compounds with high optical purity by irradiation of circularly polarized light, a model reaction for the prebiotic generation of optical activity
    • Balavoine, G., Moradpour, A., and Kagan, H. B. Preparation of chiral compounds with high optical purity by irradiation of circularly polarized light, a model reaction for the prebiotic generation of optical activity J. Am. Chem. Soc. 1974, 96, 5152-5158
    • (1974) J. Am. Chem. Soc. , vol.96 , pp. 5152-5158
    • Balavoine, G.1    Moradpour, A.2    Kagan, H.B.3
  • 13
    • 33845557915 scopus 로고
    • Kinetic resolution of racemic allylic alcohols by enantioselective epoxidation. A route to substances of absolute enantiomeric purity
    • Martin, V. S., Woodard, S. S., Katsuki, T., Yamada, Y., Ikeda, M., and Sharpless, K. B. Kinetic resolution of racemic allylic alcohols by enantioselective epoxidation. A route to substances of absolute enantiomeric purity. J. Am. Chem. Soc. 1981, 103, 6237-6240
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 6237-6240
    • Martin, V.S.1    Woodard, S.S.2    Katsuki, T.3    Yamada, Y.4    Ikeda, M.5    Sharpless, K.B.6
  • 14
    • 85050327741 scopus 로고
    • Resolution of enantiomers via biocatalysis
    • Sih, C. J. and Wu, S.-H. Resolution of enantiomers via biocatalysis. Top. Stereochem. 1989, 19, 63-125
    • (1989) Top. Stereochem. , vol.19 , pp. 63-125
    • Sih, C.J.1    Wu, S.-H.2
  • 15
    • 84954578972 scopus 로고
    • Extending the applicability of esterases of low enantioselectivity in asymmetric synthesis
    • Porter, R., and Clark, S., Eds. Pitman, London
    • Wang, Y.-F., Chen, C.-S., Girdaukas, G., and Sih, C. J. Extending the applicability of esterases of low enantioselectivity in asymmetric synthesis. In: Enzymes in Organic Synthesis (Porter, R., and Clark, S., Eds.). Pitman, London, 1985, 128-145
    • (1985) Enzymes in Organic Synthesis , pp. 128-145
    • Wang, Y.-F.1    Chen, C.-S.2    Girdaukas, G.3    Sih, C.J.4
  • 16
    • 0027469773 scopus 로고
    • Application of the term "relative enantioselectivity" as useful measure for comparison of chiral catalysts, demonstrated on asymmetric hydrogenation of amino acid precursors
    • Selke, R., Facklam, C., Foken, H., and Heller, D. Application of the term "relative enantioselectivity" as useful measure for comparison of chiral catalysts, demonstrated on asymmetric hydrogenation of amino acid precursors. Tetrahedron Asym. 1993, 4, 369-382
    • (1993) Tetrahedron Asym. , vol.4 , pp. 369-382
    • Selke, R.1    Facklam, C.2    Foken, H.3    Heller, D.4
  • 17
    • 0003031978 scopus 로고
    • Stereochemical control of yeast reductions. 2: Quantitative treatment of the kinetics of competing enzyme systems for a single substrate
    • Chen, C.-S., Zhou, B.-N., Girdaukas, G., Shieh, W.-R., VanMiddlesworth, F., Gopalan, A. S., and Sih, C. J. Stereochemical control of yeast reductions. 2. Quantitative treatment of the kinetics of competing enzyme systems for a single substrate. Bioorg. Chem. 1984, 12, 98-117
    • (1984) Bioorg. Chem. , vol.12 , pp. 98-117
    • Chen, C.-S.1    Zhou, B.-N.2    Girdaukas, G.3    Shieh, W.-R.4    VanMiddlesworth, F.5    Gopalan, A.S.6    Sih, C.J.7
  • 18
    • 0027138526 scopus 로고
    • Selectivity enhancement of hydrolase reactions
    • Faber, K., Ottolina, G., and Riva, S. Selectivity enhancement of hydrolase reactions. Biocatalysis 1993, 8, 91-132
    • (1993) Biocatalysis , vol.8 , pp. 91-132
    • Faber, K.1    Ottolina, G.2    Riva, S.3
  • 19
    • 0344734017 scopus 로고
    • Process strategies in enzymatic racemate resolution
    • Galindo, E., and Ramirez, O. T., Eds. Kluwer Academic Publishers, The Netherlands
    • Rakels, J. L. L., Straathof, A. J. J., and Heijnen, J. J. Process strategies in enzymatic racemate resolution. In: Advances in Bio-process Engineering (Galindo, E., and Ramirez, O. T., Eds.). Kluwer Academic Publishers, The Netherlands. 1994, 473-480
    • (1994) Advances in Bio-process Engineering , pp. 473-480
    • Rakels, J.L.L.1    Straathof, A.J.J.2    Heijnen, J.J.3
  • 20
    • 0001448059 scopus 로고
    • Is there a preferred expression for the composition of a mixture of enantiomers?
    • Kagan, H. B. Is there a preferred expression for the composition of a mixture of enantiomers? Recl. Trav. Chim. Pays-Bas 1995, 114, 203-205
    • (1995) Recl. Trav. Chim. Pays-bas , vol.114 , pp. 203-205
    • Kagan, H.B.1
  • 22
    • 0027897680 scopus 로고
    • A simple method to determine the enantiomeric ratio in enantioselective biocatalysis
    • Rakels, J. L. L., Straathof, A. J. J., and Heijnen, J. J. A simple method to determine the enantiomeric ratio in enantioselective biocatalysis. Enzyme Microb. Technol. 1993, 15, 1051-1056
    • (1993) Enzyme Microb. Technol. , vol.15 , pp. 1051-1056
    • Rakels, J.L.L.1    Straathof, A.J.J.2    Heijnen, J.J.3
  • 23
    • 0028008538 scopus 로고
    • Kinetic resolutions concentrate the minor enantiomer and aid measurements of high enantiomeric purity
    • Caron, G., Tseng, W.-M., and Kazlauskas, R. J. Kinetic resolutions concentrate the minor enantiomer and aid measurements of high enantiomeric purity. Tetrahedron Asym. 1994, 5, 83-92
    • (1994) Tetrahedron Asym. , vol.5 , pp. 83-92
    • Caron, G.1    Tseng, W.-M.2    Kazlauskas, R.J.3
  • 25
    • 0028809211 scopus 로고
    • Mass balancing in kinetic resolution: Calculating yield and enantiomeric excess using chiral balance
    • Straathof, A. J. J., Rakels, J. L. L., and Heijnen, J. J. Mass balancing in kinetic resolution: Calculating yield and enantiomeric excess using chiral balance. Biotechnol. Bioeng. 1995, 45, 536-538
    • (1995) Biotechnol. Bioeng. , vol.45 , pp. 536-538
    • Straathof, A.J.J.1    Rakels, J.L.L.2    Heijnen, J.J.3
  • 26
    • 0000626186 scopus 로고
    • How can the solvent affect enantioselectivity?
    • Fitzpatrick, P. A. and Klibanov, A. M. How can the solvent affect enantioselectivity? J. Am. Chem. Soc. 1991, 113, 3166-3171
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 3166-3171
    • Fitzpatrick, P.A.1    Klibanov, A.M.2
  • 27
    • 84987187753 scopus 로고
    • Enantioselective enzymatic catalysis: I. A novel method to determine the enantiomeric ratio
    • Jongejan, J. A., Van Tol, J. B. A., Geerlof, A., and Duine, J. A. Enantioselective enzymatic catalysis: I. A novel method to determine the enantiomeric ratio. Recl. Trav. Chim. Pays-Bas 1991, 110, 247-254
    • (1991) Recl. Trav. Chim. Pays-bas , vol.110 , pp. 247-254
    • Jongejan, J.A.1    Van Tol, J.B.A.2    Geerlof, A.3    Duine, J.A.4
  • 28
    • 0028764977 scopus 로고
    • Kinetic analysis of enzymatic chiral resolution by progress curve evaluation
    • Rakels, J. L. L., Romein, B., Straathof, A. J. J., and Heijnen, J. J. Kinetic analysis of enzymatic chiral resolution by progress curve evaluation. Biotechnol. Bioeng. 1994, 43, 411-422
    • (1994) Biotechnol. Bioeng. , vol.43 , pp. 411-422
    • Rakels, J.L.L.1    Romein, B.2    Straathof, A.J.J.3    Heijnen, J.J.4
  • 29
    • 0002725872 scopus 로고
    • Mathematical modelling of lipase catalysed resolution of O-acetyl and O-formyl derivatives of secondary alcohols
    • Bevinakatti, H. S., Banerji, A. A., Newadkar, R. V., and Mukesh, D. Mathematical modelling of lipase catalysed resolution of O-acetyl and O-formyl derivatives of secondary alcohols. Biocatalysis 1991, 5, 99-108
    • (1991) Biocatalysis , vol.5 , pp. 99-108
    • Bevinakatti, H.S.1    Banerji, A.A.2    Newadkar, R.V.3    Mukesh, D.4
  • 30
    • 0029013153 scopus 로고
    • A convenient method for evaluation of the enantiomeric ratio of kinetic resolution
    • Lu, Y., Zhao, X., and Chen, Z.-N. A convenient method for evaluation of the enantiomeric ratio of kinetic resolution. Tetrahedron Asym. 1995, 6, 1093-1096
    • (1995) Tetrahedron Asym. , vol.6 , pp. 1093-1096
    • Lu, Y.1    Zhao, X.2    Chen, Z.-N.3
  • 31
    • 0025284519 scopus 로고
    • Enhancing the enantioselectivity of Candida lipase catalyzed ester hydrolysis via noncovalent enzyme modification
    • Wu, S.-H., Guo, Z.-H., and Sih, C. J. Enhancing the enantioselectivity of Candida lipase catalyzed ester hydrolysis via noncovalent enzyme modification. J. Am. Chem. Soc. 1990, 112, 1990-1995
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 1990-1995
    • Wu, S.-H.1    Guo, Z.-H.2    Sih, C.J.3
  • 32
    • 0027954884 scopus 로고
    • Enzymatic resolution of racemates contaminated by racemic product
    • Wolff, A., Straathof, A. J. J., and Heijnen, J. J. Enzymatic resolution of racemates contaminated by racemic product. Biocatalysis 1994, 11, 249-261
    • (1994) Biocatalysis , vol.11 , pp. 249-261
    • Wolff, A.1    Straathof, A.J.J.2    Heijnen, J.J.3
  • 33
    • 0342905501 scopus 로고
    • Novel plots of data from combined multistep enzymatic resolutions of enantiomers
    • Guo, Z.-W. Novel plots of data from combined multistep enzymatic resolutions of enantiomers. J. Org. Chem. 1993, 58 5748-5752
    • (1993) J. Org. Chem. , vol.58 , pp. 5748-5752
    • Guo, Z.-W.1
  • 35
    • 0342905496 scopus 로고
    • Strategies in the preparation of homochiral compounds using combined enantioselective enzymes
    • Straathof. A. J. J., Rakels, J. L. L., and Heijnen, J. J. Strategies in the preparation of homochiral compounds using combined enantioselective enzymes. Biocatalysis 1990. 4, 89-104
    • (1990) Biocatalysis , vol.4 , pp. 89-104
    • Straathof, A.J.J.1    Rakels, J.L.L.2    Heijnen, J.J.3
  • 36
    • 0345164264 scopus 로고    scopus 로고
    • A computer program for the optimization of kinetic resolutions with spontaneous hydrolysis: 'Selectivity-KReSH'
    • Roberts, S. M., ed. John Wiley & Sons, New York, Update 8, 0:0.79-0:0.84
    • Faber, K., Mischitz M., and Kleewein, A. A computer program for the optimization of kinetic resolutions with spontaneous hydrolysis: 'Selectivity-KReSH'. In: Preparative Biotransformations. (Roberts, S. M., ed.). John Wiley & Sons, New York, 1996, Update 8, 0:0.79-0:0.84
    • (1996) Preparative Biotransformations
    • Faber, K.1    Mischitz, M.2    Kleewein, A.3
  • 37
    • 0029060763 scopus 로고
    • Cross-linked crystals of Candida rugosa lipase: Highly efficient catalysts for the resolution of chiral esters
    • Lalonde, J. J., Govardhan, C., Khalaf. N., Martinez, A. G., Visurim, K., and Margolin, A. L. Cross-linked crystals of Candida rugosa lipase: Highly efficient catalysts for the resolution of chiral esters. J. Am. Chem. Soc. 1995, 117, 6845-6852
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 6845-6852
    • Lalonde, J.J.1    Govardhan, C.2    Khalaf, N.3    Martinez, A.G.4    Visurim, K.5    Margolin, A.L.6
  • 38
    • 0344301799 scopus 로고
    • The kinetic resolution of enantiomers by means of enzymatic reactions
    • Otto, P. P. H. L. The kinetic resolution of enantiomers by means of enzymatic reactions. Chem. Biochem. Eng. Q. 1990, 4, 137-149
    • (1990) Chem. Biochem. Eng. Q. , vol.4 , pp. 137-149
    • Otto, P.P.H.L.1
  • 39
    • 0000298944 scopus 로고
    • Enzymatic second-order asymmetric hydrolysis of ketorolac esters: In situ racemization
    • Fülling, G. and Sih, C. J. Enzymatic second-order asymmetric hydrolysis of ketorolac esters: In situ racemization. J. Am. Chem. Soc. 1987, 109, 2845-2846
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 2845-2846
    • Fülling, G.1    Sih, C.J.2
  • 40
    • 0027400239 scopus 로고
    • Mathematical treatment of kinetic resolution of chirally labile substrates
    • Kitamura, M., Tokunaga, M., and Noyori, R. Mathematical treatment of kinetic resolution of chirally labile substrates. Tetrahedron 1993, 49, 1853-1860
    • (1993) Tetrahedron , vol.49 , pp. 1853-1860
    • Kitamura, M.1    Tokunaga, M.2    Noyori, R.3
  • 41
    • 0006091928 scopus 로고
    • Sequential kinetic resolution by two enantioselective enzymes
    • Rakels, J. L. L., Wolff, A., Straathof, A. J. J., and Heijnen. J. J. Sequential kinetic resolution by two enantioselective enzymes. Biocatalysis 1994, 9, 31-47
    • (1994) Biocatalysis , vol.9 , pp. 31-47
    • Rakels, J.L.L.1    Wolff, A.2    Straathof, A.J.J.3    Heijnen, J.J.4
  • 42
    • 33845282987 scopus 로고
    • Quantitative analyses of biochemical kinetic resolutions of enantiomers. 2: Enzyme-catalyzed esterifications in water-organic solvent biphasic systems
    • Chen, C.-S., Wu. S.-H., Girdaukas, G., and Sih, C. J. Quantitative analyses of biochemical kinetic resolutions of enantiomers. 2. Enzyme-catalyzed esterifications in water-organic solvent biphasic systems. J. Am. Chem. Soc. 1987, 109, 2812-2817
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 2812-2817
    • Chen, C.-S.1    Wu, S.-H.2    Girdaukas, G.3    Sih, C.J.4
  • 43
    • 0002456045 scopus 로고
    • Kinetics of the enzymatic resolution of racemic compounds in bi-bi reactions
    • Straathof, A. J. J., Rakels, J. L. L., and Heijnen, J. J. Kinetics of the enzymatic resolution of racemic compounds in bi-bi reactions. Biocatalysis 1992, 7, 13-27
    • (1992) Biocatalysis , vol.7 , pp. 13-27
    • Straathof, A.J.J.1    Rakels, J.L.L.2    Heijnen, J.J.3
  • 44
    • 0024716125 scopus 로고
    • Enantioselective inhibition: A strategy for improving the enantioselectivity of biocatalytic systems
    • Guo, Z.-W. and Sih, C. J. Enantioselective inhibition: A strategy for improving the enantioselectivity of biocatalytic systems. J. Am. Chem. Soc. 1989, 111, 6836-6841
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 6836-6841
    • Guo, Z.-W.1    Sih, C.J.2
  • 45
    • 0029109785 scopus 로고
    • Description of hydrolase-enantioselectivity must be based on the actual kinetic mechanism: Analysis of the kinetic resolution of glycidyl (2,3-epoxy-1-propyl) butyrate by pig pancreas lipase
    • Van Tol, J. B. A., Jongejan, J. A., and Duine, J. A. Description of hydrolase-enantioselectivity must be based on the actual kinetic mechanism: Analysis of the kinetic resolution of glycidyl (2,3-epoxy-1-propyl) butyrate by pig pancreas lipase. Biocatal. Biotransform. 1995, 12, 99-117
    • (1995) Biocatal. Biotransform. , vol.12 , pp. 99-117
    • Van Tol, J.B.A.1    Jongejan, J.A.2    Duine, J.A.3
  • 47
    • 0027054921 scopus 로고
    • Evaluation of process options for enzymatic kinetic resolution
    • Straathof, A. J. J., Rakels, J. L. L., and Heijnen, J. J. Evaluation of process options for enzymatic kinetic resolution. Ann. N. Y. Acad. Sci. 1992, 672, 497-501
    • (1992) Ann. N. Y. Acad. Sci. , vol.672 , pp. 497-501
    • Straathof, A.J.J.1    Rakels, J.L.L.2    Heijnen, J.J.3
  • 48
    • 0019879061 scopus 로고
    • Enzymatic synthesis in biphasic aqueous-organic systems. I: Chemical equilibrium shift
    • Martinek, K., Semenov, A. N., and Berezin, I. V. Enzymatic synthesis in biphasic aqueous-organic systems. I. Chemical equilibrium shift. Biochim. Biophys. Acta 1981, 658, 90-101
    • (1981) Biochim. Biophys. Acta , vol.658 , pp. 90-101
    • Martinek, K.1    Semenov, A.N.2    Berezin, I.V.3
  • 49
    • 0000176509 scopus 로고
    • Multiphase membrane reactors for enzymatic resolution: Diffusional effects on stereoselectivity
    • Sikdar, S. K., Bier, M., and Todd, P., Eds. CRC Press, Boca Raton, FL
    • Matson, S. L. and Lopez, J. L. Multiphase membrane reactors for enzymatic resolution: Diffusional effects on stereoselectivity. In: Frontiers in bioprocessing (Sikdar, S. K., Bier, M., and Todd, P., Eds.). CRC Press, Boca Raton, FL, 1990, 391-403
    • (1990) Frontiers in Bioprocessing , pp. 391-403
    • Matson, S.L.1    Lopez, J.L.2
  • 50
    • 0025476235 scopus 로고
    • Enzymatic resolution with a multiphase membrane bioreactor: A theoretical analysis
    • Wu, D., Belfort, G., and Cramer, S. Enzymatic resolution with a multiphase membrane bioreactor: A theoretical analysis. Ind. Eng. Chem. Res. 1990, 29, 1612-1621
    • (1990) Ind. Eng. Chem. Res. , vol.29 , pp. 1612-1621
    • Wu, D.1    Belfort, G.2    Cramer, S.3
  • 52
    • 0000272271 scopus 로고
    • Kinetic analysis and simulation studies for lipase-catalysed resolution of racemic 2-methyl-l-pentanol
    • Indlekofer, M., Reuss, M., Barth, S., and Effenberger, F. Kinetic analysis and simulation studies for lipase-catalysed resolution of racemic 2-methyl-l-pentanol. Biocatalysis 1993, 7, 249-266
    • (1993) Biocatalysis , vol.7 , pp. 249-266
    • Indlekofer, M.1    Reuss, M.2    Barth, S.3    Effenberger, F.4
  • 53
    • 0028815168 scopus 로고
    • Continuous enantioselective transesterification in organic solvents. Use of suspended lipase preparations in a microfiltration membrane reactor
    • Indlekofer, M., Funke, M., Claassen, W., and Reuss, M. Continuous enantioselective transesterification in organic solvents. Use of suspended lipase preparations in a microfiltration membrane reactor. Biotechnol. Progr. 1995, 11, 436-442
    • (1995) Biotechnol. Progr. , vol.11 , pp. 436-442
    • Indlekofer, M.1    Funke, M.2    Claassen, W.3    Reuss, M.4
  • 54
    • 84987172619 scopus 로고
    • Enantioselective enzymatic catalysis. 2: Applicability of methods for enantiomeric ratio determination
    • Van Tol, J. B. A., Jongejan, J. A., Geerlof, A., and Duine, J. A. Enantioselective enzymatic catalysis. 2. Applicability of methods for enantiomeric ratio determination. Recl. Trav. Chim. Pays-Bas 1991, 110, 255-262
    • (1991) Recl. Trav. Chim. Pays-bas , vol.110 , pp. 255-262
    • Van Tol, J.B.A.1    Jongejan, J.A.2    Geerlof, A.3    Duine, J.A.4
  • 55
    • 0027982637 scopus 로고
    • Activity and selectivity of some hydrolases in enantiomeric solvents
    • Ottolina, G., Bovara, R., Riva, S., and Carrea, G. Activity and selectivity of some hydrolases in enantiomeric solvents. Biotechnol. Lett. 1994, 16, 923-928
    • (1994) Biotechnol. Lett. , vol.16 , pp. 923-928
    • Ottolina, G.1    Bovara, R.2    Riva, S.3    Carrea, G.4
  • 56
    • 0028037029 scopus 로고
    • Kinetic mechanism and enantioselectivity of the oxidation of alcohols and aldehydes by quinohaemoprotein ethanol dehydrogenase from Comamonas testosteroni LMD 26.36
    • Geerlof, A., Rakels, J. L. L., Straathof, A. J. J., Heijnen, J. J., Jongejan, J. A., and Duine, J. A. Kinetic mechanism and enantioselectivity of the oxidation of alcohols and aldehydes by quinohaemoprotein ethanol dehydrogenase from Comamonas testosteroni LMD 26.36. Eur. J. Biochem. 1994, 226, 537-546
    • (1994) Eur. J. Biochem. , vol.226 , pp. 537-546
    • Geerlof, A.1    Rakels, J.L.L.2    Straathof, A.J.J.3    Heijnen, J.J.4    Jongejan, J.A.5    Duine, J.A.6
  • 57
    • 69249097642 scopus 로고
    • Temperature effects in enzyme kinetics
    • Punch, D. L., Ed. Academic Press, New York
    • Laidler, K. J. and Peterman, B. F. Temperature effects in enzyme kinetics. In: Contemporary Enzyme Kinetics and Mechanism (Punch, D. L., Ed.). Academic Press, New York, 1983, 149-171
    • (1983) Contemporary Enzyme Kinetics and Mechanism , pp. 149-171
    • Laidler, K.J.1    Peterman, B.F.2
  • 59
    • 84989484683 scopus 로고
    • Enzyme kinetics in monophasic and biphasic aqueous-organic systems
    • Tramper, J., Vermuë, M. H., Beeftink, H. H., and von Stockar, U., Eds. Elsevier, Amsterdam
    • Straathof, A. J. J., Rakels, J. L. L., and Heijnen, J. J. Enzyme kinetics in monophasic and biphasic aqueous-organic systems. Biocatalysis in Non-Conventional Media. (Tramper, J., Vermuë, M. H., Beeftink, H. H., and von Stockar, U., Eds.). Elsevier, Amsterdam, 1992, 137-144
    • (1992) Biocatalysis in Non-conventional Media , pp. 137-144
    • Straathof, A.J.J.1    Rakels, J.L.L.2    Heijnen, J.J.3
  • 60
    • 6844245547 scopus 로고
    • Relation of enzymatic reaction rate and hydrophobicity of the solvent
    • Tramper, J., Vermuë, M. H., Beeftink, H. H., and von Stockar, U., Eds. Elsevier, Amsterdam
    • Van Tol, J. B. A., Odenthal, J. B., Jongejan, J. A., and Duine, J. A. Relation of enzymatic reaction rate and hydrophobicity of the solvent. Biocatalysis in Non-Conventional Media, (Tramper, J., Vermuë, M. H., Beeftink, H. H., and von Stockar, U., Eds.). Elsevier, Amsterdam, 1992, 229-235
    • (1992) Biocatalysis in Non-conventional Media , pp. 229-235
    • Van Tol, J.B.A.1    Odenthal, J.B.2    Jongejan, J.A.3    Duine, J.A.4
  • 61
    • 0004401220 scopus 로고
    • Ground state and transition state effects in the acylation of α-chymotrypsin in organic solvent-water mixtures
    • Bell, R. P., Critchlow, J. E., and Page, M. Ground state and transition state effects in the acylation of α-chymotrypsin in organic solvent-water mixtures. J. Chem. Soc., Chem. Commun. 1974, 2, 66-70
    • (1974) J. Chem. Soc., Chem. Commun. , vol.2 , pp. 66-70
    • Bell, R.P.1    Critchlow, J.E.2    Page, M.3
  • 62
    • 0030066698 scopus 로고    scopus 로고
    • Temperature modulation of the stereochemistry of enzymatic catalysis: Prospects for exploitation
    • Phillips, R. S. Temperature modulation of the stereochemistry of enzymatic catalysis: Prospects for exploitation. TIBTECH 1996, 14, 13-16
    • (1996) TIBTECH , vol.14 , pp. 13-16
    • Phillips, R.S.1
  • 63
    • 0001699388 scopus 로고
    • Control of enzyme enantioselectivity with pressure changes in supercritical fluoroform
    • Kamat, S. V., Beckman, E. J., and Russell, A. J. Control of enzyme enantioselectivity with pressure changes in supercritical fluoroform. J. Am. Chem. Soc. 1993, 115, 8845-8846
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 8845-8846
    • Kamat, S.V.1    Beckman, E.J.2    Russell, A.J.3
  • 65
    • 0642367795 scopus 로고
    • Asymmetric transformations catalyzed by enzymes in organic solvents
    • Klibanov, A. M. Asymmetric transformations catalyzed by enzymes in organic solvents. Acc. Chem. Res. 1990, 23, 114-120
    • (1990) Acc. Chem. Res. , vol.23 , pp. 114-120
    • Klibanov, A.M.1
  • 66
    • 0026892825 scopus 로고
    • Designing enzymes for use in organic solvents
    • Dordick, J. S. Designing enzymes for use in organic solvents. Biotechnol. Prog. 1992, 8, 259-266
    • (1992) Biotechnol. Prog. , vol.8 , pp. 259-266
    • Dordick, J.S.1
  • 67
    • 0028302684 scopus 로고
    • The solvent dependence of enzyme specificity
    • Wescott, C. R. and Klibanov, A. M. The solvent dependence of enzyme specificity. Biochem. Biophys. Acta 1994, 1206, 1-9
    • (1994) Biochem. Biophys. Acta , vol.1206 , pp. 1-9
    • Wescott, C.R.1    Klibanov, A.M.2
  • 68
    • 21844481352 scopus 로고
    • Enzymes in organic media: New solutions for industrial enzymatic catalysis?
    • Jongejan, J. A., van Tol, J. B. A., and Duine, J. A. Enzymes in organic media: New solutions for industrial enzymatic catalysis? Chimicaoggi 1994, July/August, 15-24
    • (1994) Chimicaoggi , vol.JULY-AUGUST , pp. 15-24
    • Jongejan, J.A.1    Van Tol, J.B.A.2    Duine, J.A.3
  • 69
    • 0028855057 scopus 로고
    • Role of solvents in the control of enzyme selectivity in organic media
    • Carrea, G., Ottolina, G., and Riva, S. Role of solvents in the control of enzyme selectivity in organic media. TIBTECH 1995, 13, 63-70
    • (1995) TIBTECH , vol.13 , pp. 63-70
    • Carrea, G.1    Ottolina, G.2    Riva, S.3
  • 70
    • 0025777167 scopus 로고
    • Reversible enantioselectivity of enzymatic reactions by media
    • Wu, S.-H., Chu, F. Y., and Wang, K. T. Reversible enantioselectivity of enzymatic reactions by media. Bioorg. Med. Chem. Lett. 1991, 1, 339-342
    • (1991) Bioorg. Med. Chem. Lett. , vol.1 , pp. 339-342
    • Wu, S.-H.1    Chu, F.Y.2    Wang, K.T.3
  • 71
    • 0026592262 scopus 로고
    • Effects of medium conditions on the enantioselectivity of lipases in organic solvents and possible rationales
    • Secundo, F., Riva, S., and Carrea, G. Effects of medium conditions on the enantioselectivity of lipases in organic solvents and possible rationales. Tetrahedron Asym. 1992, 3, 267-280
    • (1992) Tetrahedron Asym. , vol.3 , pp. 267-280
    • Secundo, F.1    Riva, S.2    Carrea, G.3
  • 72
    • 0029168644 scopus 로고
    • The catalytic performance of pig pancreas lipase in enantioselective transesterification in organic solvents
    • Van Tol, J. B. A., Kraayveld, D. E., Jongejan, J. A., and Duine, J. A. The catalytic performance of pig pancreas lipase in enantioselective transesterification in organic solvents. Biocatal. Biotransform. 1995, 12, 119-136
    • (1995) Biocatal. Biotransform. , vol.12 , pp. 119-136
    • Van Tol, J.B.A.1    Kraayveld, D.E.2    Jongejan, J.A.3    Duine, J.A.4
  • 74
    • 0028396938 scopus 로고
    • Thermodynamic predictions for biocatalysis in nonconventional media: Theory, tests, and recommendations for experimental design and analysis
    • Halling, P. J. Thermodynamic predictions for biocatalysis in nonconventional media: Theory, tests, and recommendations for experimental design and analysis. Enzyme Microb. Technol. 1993, 16, 178-200
    • (1993) Enzyme Microb. Technol. , vol.16 , pp. 178-200
    • Halling, P.J.1
  • 75
    • 0001319374 scopus 로고    scopus 로고
    • Crown ethers as regulators of enzymatic reactions: Enhanced reaction rate and enantioselectivity in lipase-catalyzed hydrolysis of 2-cyano-l-methylethyl acetate
    • Itoh, T., Takagi, Y., Murakami, T., Hiyama, Y., and Tsukube, H. Crown ethers as regulators of enzymatic reactions: Enhanced reaction rate and enantioselectivity in lipase-catalyzed hydrolysis of 2-cyano-l-methylethyl acetate. J. Org. Chem. 1996, 61, 2158-2163
    • (1996) J. Org. Chem. , vol.61 , pp. 2158-2163
    • Itoh, T.1    Takagi, Y.2    Murakami, T.3    Hiyama, Y.4    Tsukube, H.5
  • 76
    • 0027475881 scopus 로고
    • Controlling lipase stereo-selectivity via the surface pressure
    • Rogalska, E., Ransac, S., and Verger, R. Controlling lipase stereo-selectivity via the surface pressure. J. Biol. Chem. 1993, 268, 792-794
    • (1993) J. Biol. Chem. , vol.268 , pp. 792-794
    • Rogalska, E.1    Ransac, S.2    Verger, R.3
  • 77
    • 0028567450 scopus 로고
    • Effect of support material and enzyme pretreatment on enantioselectivity of immobilized subtilisin in organic solvents
    • Orsat, B., Drtina, G. J., Williams, M. G., and Klibanov, A. M. Effect of support material and enzyme pretreatment on enantioselectivity of immobilized subtilisin in organic solvents. Biotechnol. Bioeng. 1994, 44, 1265-1269
    • (1994) Biotechnol. Bioeng. , vol.44 , pp. 1265-1269
    • Orsat, B.1    Drtina, G.J.2    Williams, M.G.3    Klibanov, A.M.4
  • 78
    • 0027982637 scopus 로고
    • Activity and selectivity of some hydrolases in enantiomeric solvents
    • Ottolina, G., Bovara, R., Riva, S., and Carrea, G. Activity and selectivity of some hydrolases in enantiomeric solvents. Biotechnol. Lett. 1994, 16, 923-928
    • (1994) Biotechnol. Lett. , vol.16 , pp. 923-928
    • Ottolina, G.1    Bovara, R.2    Riva, S.3    Carrea, G.4
  • 79
    • 4243794106 scopus 로고
    • The biocatalytic approach to the preparation of enantiomerically pure chiral building blocks
    • Santaniello, E., Ferraboschi, P., Grisenti, P., and Manzocchi, A. The biocatalytic approach to the preparation of enantiomerically pure chiral building blocks. Chem. Rev. 1992, 92, 1071-1140
    • (1992) Chem. Rev. , vol.92 , pp. 1071-1140
    • Santaniello, E.1    Ferraboschi, P.2    Grisenti, P.3    Manzocchi, A.4
  • 80
    • 0026000874 scopus 로고
    • Cofactor engineering
    • Duine, J. A. Cofactor engineering. TIBTECH 1991, 9, 343-346
    • (1991) TIBTECH , vol.9 , pp. 343-346
    • Duine, J.A.1
  • 82
    • 0001373684 scopus 로고
    • Improving the enantioselectivity of the Candida cylindracea lipase in chemical modification
    • Gu, Q.-M. and Sih. C. J. Improving the enantioselectivity of the Candida cylindracea lipase in chemical modification. Biocatalysis 1992, 6, 115-126
    • (1992) Biocatalysis , vol.6 , pp. 115-126
    • Gu, Q.-M.1    Sih, C.J.2
  • 83
    • 0001416337 scopus 로고
    • Esterases in organic synthesis: Present and future
    • Jones, J. B. Esterases in organic synthesis: Present and future. Pure Appl. Chem. 1990, 62, 1445-1448
    • (1990) Pure Appl. Chem. , vol.62 , pp. 1445-1448
    • Jones, J.B.1
  • 84
    • 33751499686 scopus 로고
    • A rule to predict which enantiomer of a secondary alcohol reacts faster in reactions catalysed by cholesterol esterase, lipase from Pseudomonas cepacia, and lipase from Candida rugosa
    • Kazlauskas, R. J., Weissfloch, A. N. E., Rappaport, A. T., and Cuccia, L. A. A rule to predict which enantiomer of a secondary alcohol reacts faster in reactions catalysed by cholesterol esterase, lipase from Pseudomonas cepacia, and lipase from Candida rugosa. J. Org. Chem. 1991, 56, 2656-2665
    • (1991) J. Org. Chem. , vol.56 , pp. 2656-2665
    • Kazlauskas, R.J.1    Weissfloch, A.N.E.2    Rappaport, A.T.3    Cuccia, L.A.4
  • 85
    • 84907036514 scopus 로고
    • Molecular modeling of chymotrypsin-substrate interactions: Calculation of enantioselectivity
    • Norin, M., Mattson, A., Hult, K., and Norin, T. Molecular modeling of chymotrypsin-substrate interactions: Calculation of enantioselectivity. Biocatalysis 1993, 7, 131-147
    • (1993) Biocatalysis , vol.7 , pp. 131-147
    • Norin, M.1    Mattson, A.2    Hult, K.3    Norin, T.4
  • 86
    • 0028146056 scopus 로고
    • Molecular dynamics simulation of an enzyme surrounded by vacuum, water or a hydrophobic solvent
    • Norin, M., Haeffner, F., Hult, K., and Edholm, O. Molecular dynamics simulation of an enzyme surrounded by vacuum, water or a hydrophobic solvent. Biophys. J. 1994, 67, 548-559
    • (1994) Biophys. J. , vol.67 , pp. 548-559
    • Norin, M.1    Haeffner, F.2    Hult, K.3    Edholm, O.4
  • 87
    • 0026928586 scopus 로고
    • Computer-assisted modeling of subtilisin enantioselectivity in organic solvents
    • Fitzpatrick, P. A., Ringe, D., and Klibanov, A. M. Computer-assisted modeling of subtilisin enantioselectivity in organic solvents. Biotechnol. Bioeng. 1992, 40, 735-742
    • (1992) Biotechnol. Bioeng. , vol.40 , pp. 735-742
    • Fitzpatrick, P.A.1    Ringe, D.2    Klibanov, A.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.