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Bornscheuer U.T., Pohl M. Improved biocatalysts by directed evolution and rational protein design. Curr Opin Chem Biol. 5:2001;137-142.
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Quantitative analyses of biochemical kinetic resolutions of enantiomers
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0034955414
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Controlling lipase enantioselectivity for organic synthesis
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An excellent review emphasizing aspects for the control of lipase enantioselectivity. Several examples in which the enantioselectivity has been altered or reversed are highlighted.
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Berglund P. Controlling lipase enantioselectivity for organic synthesis. Biomol Eng. 18:2001;13-22. An excellent review emphasizing aspects for the control of lipase enantioselectivity. Several examples in which the enantioselectivity has been altered or reversed are highlighted.
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Biomol Eng
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, pp. 13-22
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Berglund, P.1
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12
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Enzymes in organic synthesis. 42. Investigation of the effects of the isozymal composition of pig liver esterase on its stereoselectivity in preparative-scale ester hydrolyses of asymmetric synthetic value
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Lam L.K.P., Brown C.M., Jeso B.D., Lym L., Toone E.J., Jones J.B. Enzymes in organic synthesis. 42. Investigation of the effects of the isozymal composition of pig liver esterase on its stereoselectivity in preparative-scale ester hydrolyses of asymmetric synthetic value. J Am Chem Soc. 110:1988;4409-4411.
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14
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0035800909
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Cloning, functional expression and characterization of recombinant pig liver carboxyl esterase
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Lange S., Musidlowska A., Schmidt-Dannert C., Schmitt J., Bornscheuer U.T. Cloning, functional expression and characterization of recombinant pig liver carboxyl esterase. Chem Biol Chem. 2:2001;576-582.
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Chem Biol Chem
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Lange, S.1
Musidlowska, A.2
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15
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0035800379
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Via overexpression in the yeast Pichia pastoris to enhanced enantioselectivity: New aspects in the application of pig liver esterase
-
This work clearly shows the importance of using well-defined enzymes instead of crude preparations. Using the heterologously expressed γ-isoenzyme of pig liver esterase (PLE), substrates can now be resolved with high enantioselectivity, which have been not accessible in optically pure form using ill-defined commercially available PLE preparations.
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Musidlowska A., Lange S., Bornscheuer U.T. Via overexpression in the yeast Pichia pastoris to enhanced enantioselectivity: new aspects in the application of pig liver esterase. Angew Chem Int Ed Engl. 40:2001;2851-2853. This work clearly shows the importance of using well-defined enzymes instead of crude preparations. Using the heterologously expressed γ-isoenzyme of pig liver esterase (PLE), substrates can now be resolved with high enantioselectivity, which have been not accessible in optically pure form using ill-defined commercially available PLE preparations.
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(2001)
Angew Chem Int Ed Engl
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, pp. 2851-2853
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Musidlowska, A.1
Lange, S.2
Bornscheuer, U.T.3
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16
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0029060763
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Cross-linked crystals of Candida rugosa lipase: Highly efficient catalysts for the resolution of chiral esters
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Lalonde J.J., Govardhan C., Khalaf N., Martinez A.G., Visuri K., Margolin A.L. Cross-linked crystals of Candida rugosa lipase: highly efficient catalysts for the resolution of chiral esters. J Am Chem Soc. 117:1995;6845-6852.
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Visuri, K.5
Margolin, A.L.6
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17
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Enhancement of the enantioselectivity of lipase OF catalyzed hydrolysis
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Chang Y.F., Tai D.F. Enhancement of the enantioselectivity of lipase OF catalyzed hydrolysis. Tetrahedron Asymmetry. 12:2001;177-179.
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Tetrahedron Asymmetry
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Chang, Y.F.1
Tai, D.F.2
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18
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0142142207
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Enantioselective hydrolysis of d,l-menthyl benzoate to l-menthol by recombinant Candida rugosa lipases
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in press
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Vorlová S, Bornscheuer UT, Gatfield I, Hilmer JM, Bertram HJ, Schmid RD: Enantioselective hydrolysis of d,l-menthyl benzoate to l-menthol by recombinant Candida rugosa lipases. Adv Synth Catal 2002, 344:in press.
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Adv Synth Catal
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Vorlová, S.1
Bornscheuer, U.T.2
Gatfield, I.3
Hilmer, J.M.4
Bertram, H.J.5
Schmid, R.D.6
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19
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0033963834
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Molecular modeling and biocatalysis: Explanations, predictions, limitations, and opportunities
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A good overview about successful and less successful applications of molecular modeling as a tool to analyze and predict the function of certain amino acid side chains in enzymes.
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Kazlauskas R.J. Molecular modeling and biocatalysis: explanations, predictions, limitations, and opportunities. Curr Opin Chem Biol. 4:2000;81-88. A good overview about successful and less successful applications of molecular modeling as a tool to analyze and predict the function of certain amino acid side chains in enzymes.
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Curr Opin Chem Biol
, vol.4
, pp. 81-88
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Kazlauskas, R.J.1
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20
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84962418014
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Molecular modeling of lipase-catalyzed reactions. Prediction of enantioselectivities
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Haffner F., Norin T. Molecular modeling of lipase-catalyzed reactions. Prediction of enantioselectivities. Chem Pharm Bull. 47:1999;591-600.
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Chem Pharm Bull
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, pp. 591-600
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Haffner, F.1
Norin, T.2
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23
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0035496145
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Improved enantioselectivity of a lipase by rational protein engineering
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Rotticci D., Rotticci-Mulder J.C., Denman S., Norin T., Hult K. Improved enantioselectivity of a lipase by rational protein engineering. Chem Biol Chem. 2:2001;766-770.
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Chem Biol Chem
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Rotticci, D.1
Rotticci-Mulder, J.C.2
Denman, S.3
Norin, T.4
Hult, K.5
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24
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0034794047
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Creation of an enantioselective hydrolase by engineered substrate-assisted catalysis
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Although not generally applicable, this is an impressive example that the activity of an enzyme must not be based solely on the presence of a functional catalytic machinery. Indeed, this can be achieved by supplying a functional group (here, a hydroxy residue) located in the substrate and not in the amino acid backbone of the biocatalyst.
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Magnusson A., Hult K., Holmquist M. Creation of an enantioselective hydrolase by engineered substrate-assisted catalysis. J Am Chem Soc. 123:2001;4354-4355. Although not generally applicable, this is an impressive example that the activity of an enzyme must not be based solely on the presence of a functional catalytic machinery. Indeed, this can be achieved by supplying a functional group (here, a hydroxy residue) located in the substrate and not in the amino acid backbone of the biocatalyst.
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(2001)
J Am Chem Soc
, vol.123
, pp. 4354-4355
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Magnusson, A.1
Hult, K.2
Holmquist, M.3
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25
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0033918890
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Stereoselectivity of Pseudomonas cepacia lipase toward secondary alcohols: A quantitative model
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Schulz T., Pleiss J., Schmid R.D. Stereoselectivity of Pseudomonas cepacia lipase toward secondary alcohols: a quantitative model. Protein Sci. 9:2000;1053-1062.
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Protein Sci
, vol.9
, pp. 1053-1062
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Schulz, T.1
Pleiss, J.2
Schmid, R.D.3
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26
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0034605577
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Computer-aided molecular modeling of the enantioselectivity of Pseudomonas cepacia lipase toward γ- and δ-lactones
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Hwang B.-Y., Scheib H., Pleiss J., Kim B.-G., Schmid R.D. Computer-aided molecular modeling of the enantioselectivity of Pseudomonas cepacia lipase toward γ- and δ-lactones. J Mol Catal B Enzym. 10:2000;223-231.
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J Mol Catal B Enzym
, vol.10
, pp. 223-231
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Hwang, B.-Y.1
Scheib, H.2
Pleiss, J.3
Kim, B.-G.4
Schmid, R.D.5
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27
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0034597427
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Lipase engineering database: Understanding and exploiting sequence-structure-function relationships
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Pleiss J., Fischer M., Peiker M., Thiele C., Schmid R.D. Lipase engineering database: understanding and exploiting sequence-structure-function relationships. J Mol Catal B Enzym. 10:2000;491-508.
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J Mol Catal B Enzym
, vol.10
, pp. 491-508
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Pleiss, J.1
Fischer, M.2
Peiker, M.3
Thiele, C.4
Schmid, R.D.5
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28
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0037008979
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Activity of lipases and esterases towards tertiary alcohols: New insights into structure-function relationships
-
The identification that the GGGX motif determines activity of lipases and esterases towards tertiary alcohols has a strong impact on biocatalysis because it was common belief that these enzymes are almost all inactive towards this class of compounds. Interestingly, the enzymes confirmed experimentally as active, originate from very different organisms, mammalian, bacteria and yeast, and consequently have very little sequence homology.
-
Henke E., Pleiss J., Bornscheuer U.T. Activity of lipases and esterases towards tertiary alcohols: new insights into structure-function relationships. Angew Chem Int Ed Engl. 41:2002;3211-3213. The identification that the GGGX motif determines activity of lipases and esterases towards tertiary alcohols has a strong impact on biocatalysis because it was common belief that these enzymes are almost all inactive towards this class of compounds. Interestingly, the enzymes confirmed experimentally as active, originate from very different organisms, mammalian, bacteria and yeast, and consequently have very little sequence homology.
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(2002)
Angew Chem Int Ed Engl
, vol.41
, pp. 3211-3213
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Henke, E.1
Pleiss, J.2
Bornscheuer, U.T.3
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29
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0035313078
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Novel methods for biocatalyst screening
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Wahler D., Reymond J.L. Novel methods for biocatalyst screening. Curr Opin Chem Biol. 5:2001;152-158.
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(2001)
Curr Opin Chem Biol
, vol.5
, pp. 152-158
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Wahler, D.1
Reymond, J.L.2
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30
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0034921134
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Directed evolution of enzymes for biocatalytic applications
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Bornscheuer U.T. Directed evolution of enzymes for biocatalytic applications. Biocat Biotransf. 19:2001;84-96.
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(2001)
Biocat Biotransf
, vol.19
, pp. 84-96
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Bornscheuer, U.T.1
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33
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0033834791
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Directed evolution of an enantioselective lipase
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Liebeton K., Zonta A., Schimossek K., Nardini M., Lang D., Dijkstra B.W., Reetz M.T., Jaeger K.E. Directed evolution of an enantioselective lipase. Chem Biol. 7:2000;709-718.
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(2000)
Chem Biol
, vol.7
, pp. 709-718
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Liebeton, K.1
Zonta, A.2
Schimossek, K.3
Nardini, M.4
Lang, D.5
Dijkstra, B.W.6
Reetz, M.T.7
Jaeger, K.E.8
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34
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0035477024
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Directed evolution of an enantioselective enzyme through combinatorial multiple-cassette mutagenesis
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Reetz M.T., Wilensek S., Zha D., Jaeger K.-E. Directed evolution of an enantioselective enzyme through combinatorial multiple-cassette mutagenesis. Angew Chemie Int Ed Engl. 40:2001;3589-3591.
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(2001)
Angew Chemie Int Ed Engl
, vol.40
, pp. 3589-3591
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Reetz, M.T.1
Wilensek, S.2
Zha, D.3
Jaeger, K.-E.4
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35
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0026476140
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Drastic solvent effect on lipase-catalyzed enantioselective hydrolysis of prochiral 1,4-dihydropyridines
-
Hirose Y., Kariya K., Sasaki I., Kurono Y., Ebiike H., Achiwa K. Drastic solvent effect on lipase-catalyzed enantioselective hydrolysis of prochiral 1,4-dihydropyridines. Tetrahedron Lett. 33:1992;7157-7160.
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Tetrahedron Lett
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Hirose, Y.1
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Sasaki, I.3
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Ebiike, H.5
Achiwa, K.6
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36
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0034743027
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Dimethyl sulfoxide as a co-solvent dramatically enhances the enantioselectivity in lipase-catalysed resolutions of 2-phenoxypropionic acyl derivatives
-
The effect of the addition of a co-solvent on enzyme performance cannot be predicted and is still a trial and error approach. However, this work shows that it is always worth a try, as E-values could be substantially increased turning a rather useless resolution into a practical one.
-
Watanabe K., Ueji S.-I. Dimethyl sulfoxide as a co-solvent dramatically enhances the enantioselectivity in lipase-catalysed resolutions of 2-phenoxypropionic acyl derivatives. J Chem Soc Perkin Trans. 1:2001;1386-1390. The effect of the addition of a co-solvent on enzyme performance cannot be predicted and is still a trial and error approach. However, this work shows that it is always worth a try, as E-values could be substantially increased turning a rather useless resolution into a practical one.
-
(2001)
J Chem Soc Perkin Trans
, vol.1
, pp. 1386-1390
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Watanabe, K.1
Ueji, S.-I.2
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37
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0035648023
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A dramatic improvement of enantioselectivity of lipase in organic solvents by addition of aqueous SDS: A close correlation between enantioselectivity and conformational flexibility of lipase
-
Ueji S.-I., Nishimura M., Kudo R., Matsumi R., Watanabe K., Ebara Y. A dramatic improvement of enantioselectivity of lipase in organic solvents by addition of aqueous SDS: a close correlation between enantioselectivity and conformational flexibility of lipase. Chem Lett. 1:2001;912-913.
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(2001)
Chem Lett
, vol.1
, pp. 912-913
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Ueji, S.-I.1
Nishimura, M.2
Kudo, R.3
Matsumi, R.4
Watanabe, K.5
Ebara, Y.6
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38
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0035653245
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Effects of chemical modification of lipase on its enantioselectivity in organic solvents
-
Ueji S.-I., Tanaka H., Hanaoka T., Ueda A., Watanabe K., Kaihatsu K., Ebara Y. Effects of chemical modification of lipase on its enantioselectivity in organic solvents. Chem Lett. 1:2001;1066-1067.
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(2001)
Chem Lett
, vol.1
, pp. 1066-1067
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Ueji, S.-I.1
Tanaka, H.2
Hanaoka, T.3
Ueda, A.4
Watanabe, K.5
Kaihatsu, K.6
Ebara, Y.7
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39
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0000034575
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Ionic liquids - new solutions for transition metal catalysis
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Wasserscheid P., Keim W. Ionic liquids - new solutions for transition metal catalysis. Angew Chem Int Ed Engl. 39:2000;3772-3789.
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(2000)
Angew Chem Int Ed Engl
, vol.39
, pp. 3772-3789
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Wasserscheid, P.1
Keim, W.2
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41
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0035819970
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Enzyme catalysis in ionic liquids: Lipase catalysed kinetic resolution of 1-phenylethanol with improved enantioselectivity
-
Although the molecular reason for higher enantioselectivity of a lipase in ionic liquids (ILs) is still unclear, this paper demonstrates that ILs can have a more pronounced effect on enantioselectivity than conventional organic solvents.
-
Schöfer S.H., Kaftzik N., Wasserscheid P., Kragl U. Enzyme catalysis in ionic liquids: lipase catalysed kinetic resolution of 1-phenylethanol with improved enantioselectivity. Chem Commun. 1:2001;425-426. Although the molecular reason for higher enantioselectivity of a lipase in ionic liquids (ILs) is still unclear, this paper demonstrates that ILs can have a more pronounced effect on enantioselectivity than conventional organic solvents.
-
(2001)
Chem Commun
, vol.1
, pp. 425-426
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-
Schöfer, S.H.1
Kaftzik, N.2
Wasserscheid, P.3
Kragl, U.4
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42
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0035902269
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Biocatalysis in ionic liquids: Markedly enhanced enantioselectivity of lipase
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Kim K.-W., Song B., Choi M.-Y., Kim M.-J. Biocatalysis in ionic liquids: markedly enhanced enantioselectivity of lipase. Org Lett. 3:2001;1507-1509.
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(2001)
Org Lett
, vol.3
, pp. 1507-1509
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-
Kim, K.-W.1
Song, B.2
Choi, M.-Y.3
Kim, M.-J.4
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43
-
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0035861716
-
Improved preparation and use of room-temperature ionic liquids in lipase-catalyzed enantio- and regioselective acylations
-
Kazlauskas and co-workers demonstrate that a variety of substrates and ionic liquids (ILs) represent a very promising alternative to conventional solvent systems. Moreover, it is the first very detailed and thorough study of ILs. One of the major findings is that the purity of ILs can have a strong impact on enzyme performance and should be carefully checked.
-
Park S., Kazlauskas R.J. Improved preparation and use of room-temperature ionic liquids in lipase-catalyzed enantio- and regioselective acylations. J Org Chem. 66:2002;8395-8401. Kazlauskas and co-workers demonstrate that a variety of substrates and ionic liquids (ILs) represent a very promising alternative to conventional solvent systems. Moreover, it is the first very detailed and thorough study of ILs. One of the major findings is that the purity of ILs can have a strong impact on enzyme performance and should be carefully checked.
-
(2002)
J Org Chem
, vol.66
, pp. 8395-8401
-
-
Park, S.1
Kazlauskas, R.J.2
-
44
-
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0036267045
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Enhanced enantioselectivity of lipase from Pseudomonas sp. at high temperatures and fixed water activity in the ionic liquid, 1-butyl-3-methylimidazolium bis[(trifluoromethyl)sulfonyl]amide
-
Eckstein M., Wasserscheid P., Kragl U. Enhanced enantioselectivity of lipase from Pseudomonas sp. at high temperatures and fixed water activity in the ionic liquid, 1-butyl-3-methylimidazolium bis[(trifluoromethyl)sulfonyl]amide. Biotechnol Lett. 24:2002;763-767.
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(2002)
Biotechnol Lett
, vol.24
, pp. 763-767
-
-
Eckstein, M.1
Wasserscheid, P.2
Kragl, U.3
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45
-
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0036899228
-
Enzyme-catalysis in ionic liquids
-
in press
-
Kragl U: Enzyme-catalysis in ionic liquids. Curr Opin Biotechnol 2002, in press. A very comprehensive and informative review summarizing all aspects of ionic liquids in biocatalysis.
-
(2002)
Curr Opin Biotechnol
-
-
Kragl, U.1
-
46
-
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0035796741
-
Enantiomer separation by extraction after lipase-catalyzed, enantiomer-selective fluoroacylation
-
Substrate and fluorinated product could be efficiently separated by repetitive extraction in methanol/n-perfluorohexane. In addition, a small increase in enantioselectivity was found.
-
Hungerhoff B., Sonnenschein H., Theil F. Enantiomer separation by extraction after lipase-catalyzed, enantiomer-selective fluoroacylation. Angew Chemie Int Ed Engl. 40:2001;2492-2494. Substrate and fluorinated product could be efficiently separated by repetitive extraction in methanol/n-perfluorohexane. In addition, a small increase in enantioselectivity was found.
-
(2001)
Angew Chemie Int Ed Engl
, vol.40
, pp. 2492-2494
-
-
Hungerhoff, B.1
Sonnenschein, H.2
Theil, F.3
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47
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0001267533
-
Resolution of 1-(2-naphthyl)ethanol by a combination of an enzyme-catalyzed kinetic resolution with a fluorous triphasic separative reaction
-
Luo Z., Swaleh S.M., Theil F., Curran D.P. Resolution of 1-(2-naphthyl)ethanol by a combination of an enzyme-catalyzed kinetic resolution with a fluorous triphasic separative reaction. Org Lett. 4:2002;2585-2587.
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(2002)
Org Lett
, vol.4
, pp. 2585-2587
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Luo, Z.1
Swaleh, S.M.2
Theil, F.3
Curran, D.P.4
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48
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0034401067
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Highly enantioselective lipase-catalyzed resolution of ibuprofen
-
Henke E., Schuster S., Yang H., Bornscheuer U.T. Highly enantioselective lipase-catalyzed resolution of ibuprofen. Chem Month. 131:2000;633-638.
-
(2000)
Chem Month
, vol.131
, pp. 633-638
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-
Henke, E.1
Schuster, S.2
Yang, H.3
Bornscheuer, U.T.4
-
49
-
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0035931510
-
Influence of acyl chain length on the enantioselectivity of Candida antarctica lipase B and its thermodynamic components in kinetic resolution of sec-alcohols
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Ottosson J., Hult K. Influence of acyl chain length on the enantioselectivity of Candida antarctica lipase B and its thermodynamic components in kinetic resolution of sec-alcohols. J Mol Catal B Enzym. 11:2001;1025-1028.
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J Mol Catal B Enzym
, vol.11
, pp. 1025-1028
-
-
Ottosson, J.1
Hult, K.2
-
50
-
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0035804942
-
Molecular basis for enantioselectivity of lipase from Chromobacterium viscosum toward the diesters of 2,3-dihydro-3-(4′-hydroxyphenyl)-1,1,3-trimethyl-1H-inden-5-ol
-
Computer modeling indicates that a remote ester group (five bonds distance to the chiral center) in a bisphenol derivative controls the enantioselectivity of a lipase from Chromobacterium viscosum.
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Gascoyne D.G., Finkbeiner H.L., Chan K.P., Gordon J.L., Stewart K.R., Kazlauskas R.J. Molecular basis for enantioselectivity of lipase from Chromobacterium viscosum toward the diesters of 2,3-dihydro-3-(4′-hydroxyphenyl)-1,1,3-trimethyl-1H-inden-5-ol. J Org Chem. 66:2001;3041-3048. Computer modeling indicates that a remote ester group (five bonds distance to the chiral center) in a bisphenol derivative controls the enantioselectivity of a lipase from Chromobacterium viscosum.
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(2001)
J Org Chem
, vol.66
, pp. 3041-3048
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Gascoyne, D.G.1
Finkbeiner, H.L.2
Chan, K.P.3
Gordon, J.L.4
Stewart, K.R.5
Kazlauskas, R.J.6
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