Rationally engineered double substituted variants of Yarrowia lipolytica lipase with enhanced activity coupled with highly inverted enantioselectivity towards 2-bromo phenyl acetic acid esters
Inverting enzyme enantioselectivity by protein engineering is still a great challenge. Lip2p lipase from Yarrowia lipolytica, which demonstrates a low S-enantioselectivity (E-value = 5) during the hydrolytic kinetic resolution of 2-bromo-phenyl acetic acid octyl esters (an important class of chemica...
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| Published in | Biotechnology and bioengineering Vol. 106; no. 6; pp. 852 - 859 |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
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Hoboken
Wiley Subscription Services, Inc., A Wiley Company
15.08.2010
Wiley Subscription Services, Inc Wiley |
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| Abstract | Inverting enzyme enantioselectivity by protein engineering is still a great challenge. Lip2p lipase from Yarrowia lipolytica, which demonstrates a low S-enantioselectivity (E-value = 5) during the hydrolytic kinetic resolution of 2-bromo-phenyl acetic acid octyl esters (an important class of chemical intermediates in the pharmaceutical industry), was converted, by a rational engineering approach, into a totally R-selective enzyme (E-value > 200). This tremendous change in selectivity is the result of only two amino acid changes. The starting point of our strategy was the prior identification of two key positions, 97 and 232, for enantiomer discrimination. Four single substitution variants were recently identified as exhibiting a low inversion of selectivity coupled to a low-hydrolytic activity. On the basis of these results, six double substituted variants, combining relevant mutations at both 97 and 232 positions, were constructed by site-directed mutagenesis. This work led to the isolation of one double substituted variant (D97A-V232F), which displays a total preference for the R-enantiomer. The highly reversed enantioselectivity of this variant is accompanied by a 4.5-fold enhancement of its activity toward the preferred enantiomer. The molecular docking of the R- and S-enantiomers in the wild-type enzyme and the D97A-V232F variant suggests that V232F mutation provides a more favorable stacking interaction for the phenyl group of the R-enantiomer, that could explain both the enhanced activity and the reversal of enantioselectivity. These results demonstrate the potential of rationally engineered mutations to further enhance enzyme activity and to modulate selectivity. Biotechnol. Bioeng. 2010;106: 852-859. |
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| AbstractList | Inverting enzyme enantioselectivity by protein engineering is still a great challenge. Lip2p lipase from Yarrowia lipolytica, which demonstrates a low S‐enantioselectivity (E‐value = 5) during the hydrolytic kinetic resolution of 2‐bromo‐phenyl acetic acid octyl esters (an important class of chemical intermediates in the pharmaceutical industry), was converted, by a rational engineering approach, into a totally R‐selective enzyme (E‐value > 200). This tremendous change in selectivity is the result of only two amino acid changes. The starting point of our strategy was the prior identification of two key positions, 97 and 232, for enantiomer discrimination. Four single substitution variants were recently identified as exhibiting a low inversion of selectivity coupled to a low‐hydrolytic activity. On the basis of these results, six double substituted variants, combining relevant mutations at both 97 and 232 positions, were constructed by site‐directed mutagenesis. This work led to the isolation of one double substituted variant (D97A‐V232F), which displays a total preference for the R‐enantiomer. The highly reversed enantioselectivity of this variant is accompanied by a 4.5‐fold enhancement of its activity toward the preferred enantiomer. The molecular docking of the R‐ and S‐enantiomers in the wild‐type enzyme and the D97A‐V232F variant suggests that V232F mutation provides a more favorable stacking interaction for the phenyl group of the R‐enantiomer, that could explain both the enhanced activity and the reversal of enantioselectivity. These results demonstrate the potential of rationally engineered mutations to further enhance enzyme activity and to modulate selectivity. Biotechnol. Bioeng. 2010;106: 852–859. © 2010 Wiley Periodicals, Inc. Inverting enzyme enantioselectivity by protein engineering is still a great challenge. Lip2p lipase from Yarrowia lipolytica , which demonstrates a low S ‐enantioselectivity ( E ‐value = 5) during the hydrolytic kinetic resolution of 2‐bromo‐phenyl acetic acid octyl esters (an important class of chemical intermediates in the pharmaceutical industry), was converted, by a rational engineering approach, into a totally R ‐selective enzyme ( E ‐value > 200). This tremendous change in selectivity is the result of only two amino acid changes. The starting point of our strategy was the prior identification of two key positions, 97 and 232, for enantiomer discrimination. Four single substitution variants were recently identified as exhibiting a low inversion of selectivity coupled to a low‐hydrolytic activity. On the basis of these results, six double substituted variants, combining relevant mutations at both 97 and 232 positions, were constructed by site‐directed mutagenesis. This work led to the isolation of one double substituted variant (D97A‐V232F), which displays a total preference for the R ‐enantiomer. The highly reversed enantioselectivity of this variant is accompanied by a 4.5‐fold enhancement of its activity toward the preferred enantiomer. The molecular docking of the R ‐ and S ‐enantiomers in the wild‐type enzyme and the D97A‐V232F variant suggests that V232F mutation provides a more favorable stacking interaction for the phenyl group of the R ‐enantiomer, that could explain both the enhanced activity and the reversal of enantioselectivity. These results demonstrate the potential of rationally engineered mutations to further enhance enzyme activity and to modulate selectivity. Biotechnol. Bioeng. 2010;106: 852–859. © 2010 Wiley Periodicals, Inc. Inverting enzyme enantioselectivity by protein engineering is still a great challenge. Lip2p lipase from Yarrowia lipolytica, which demonstrates a low S-enantioselectivity (E-value...=...5) during the hydrolytic kinetic resolution of 2-bromo-phenyl acetic acid octyl esters (an important class of chemical intermediates in the pharmaceutical industry), was converted, by a rational engineering approach, into a totally R-selective enzyme (E-value...>...200). This tremendous change in selectivity is the result of only two amino acid changes. The starting point of our strategy was the prior identification of two key positions, 97 and 232, for enantiomer discrimination. Four single substitution variants were recently identified as exhibiting a low inversion of selectivity coupled to a low-hydrolytic activity. On the basis of these results, six double substituted variants, combining relevant mutations at both 97 and 232 positions, were constructed by site-directed mutagenesis. This work led to the isolation of one double substituted variant (D97A-V232F), which displays a total preference for the R-enantiomer. The highly reversed enantioselectivity of this variant is accompanied by a 4.5-fold enhancement of its activity toward the preferred enantiomer. The molecular docking of the R- and S-enantiomers in the wild-type enzyme and the D97A-V232F variant suggests that V232F mutation provides a more favorable stacking interaction for the phenyl group of the R-enantiomer, that could explain both the enhanced activity and the reversal of enantioselectivity. These results demonstrate the potential of rationally engineered mutations to further enhance enzyme activity and to modulate selectivity. (ProQuest: ... denotes formulae/symbols omitted.) Inverting enzyme enantioselectivity by protein engineering is still a great challenge. Lip2p lipase from Yarrowia lipolytica, which demonstrates a low S-enantioselectivity (E-value = 5) during the hydrolytic kinetic resolution of 2-bromo-phenyl acetic acid octyl esters (an important class of chemical intermediates in the pharmaceutical industry), was converted, by a rational engineering approach, into a totally R-selective enzyme (E-value > 200). This tremendous change in selectivity is the result of only two amino acid changes. The starting point of our strategy was the prior identification of two key positions, 97 and 232, for enantiomer discrimination. Four single substitution variants were recently identified as exhibiting a low inversion of selectivity coupled to a low-hydrolytic activity. On the basis of these results, six double substituted variants, combining relevant mutations at both 97 and 232 positions, were constructed by site-directed mutagenesis. This work led to the isolation of one double substituted variant (D97A-V232F), which displays a total preference for the R-enantiomer. The highly reversed enantioselectivity of this variant is accompanied by a 4.5-fold enhancement of its activity toward the preferred enantiomer. The molecular docking of the R- and S-enantiomers in the wild-type enzyme and the D97A-V232F variant suggests that V232F mutation provides a more favorable stacking interaction for the phenyl group of the R-enantiomer, that could explain both the enhanced activity and the reversal of enantioselectivity. These results demonstrate the potential of rationally engineered mutations to further enhance enzyme activity and to modulate selectivity. Inverting enzyme enantioselectivity by protein engineering is still a great challenge. Lip2p lipase from Yarrowia lipolytica, which demonstrates a low S-enantioselectivity (E-value=5) during the hydrolytic kinetic resolution of 2-bromo-phenyl acetic acid octyl esters (an important class of chemical intermediates in the pharmaceutical industry), was converted, by a rational engineering approach, into a totally R-selective enzyme (E-value>200). This tremendous change in selectivity is the result of only two amino acid changes. The starting point of our strategy was the prior identification of two key positions, 97 and 232, for enantiomer discrimination. Four single substitution variants were recently identified as exhibiting a low inversion of selectivity coupled to a low-hydrolytic activity. On the basis of these results, six double substituted variants, combining relevant mutations at both 97 and 232 positions, were constructed by site-directed mutagenesis. This work led to the isolation of one double substituted variant (D97A-V232F), which displays a total preference for the R-enantiomer. The highly reversed enantioselectivity of this variant is accompanied by a 4.5-fold enhancement of its activity toward the preferred enantiomer. The molecular docking of the R- and S-enantiomers in the wild-type enzyme and the D97A-V232F variant suggests that V232F mutation provides a more favorable stacking interaction for the phenyl group of the R-enantiomer, that could explain both the enhanced activity and the reversal of enantioselectivity. These results demonstrate the potential of rationally engineered mutations to further enhance enzyme activity and to modulate selectivity. Biotechnol. Bioeng. 2010; 106: 852-859. [copy 2010 Wiley Periodicals, Inc. Inverting enzyme enantioselectivity by protein engineering is still a great challenge. Lip2p lipase from Yarrowia lipolytica, which demonstrates a low S-enantioselectivity (E-value = 5) during the hydrolytic kinetic resolution of 2-bromo-phenyl acetic acid octyl esters (an important class of chemical intermediates in the pharmaceutical industry), was converted, by a rational engineering approach, into a totally R-selective enzyme (E-value > 200). This tremendous change in selectivity is the result of only two amino acid changes. The starting point of our strategy was the prior identification of two key positions, 97 and 232, for enantiomer discrimination. Four single substitution variants were recently identified as exhibiting a low inversion of selectivity coupled to a low-hydrolytic activity. On the basis of these results, six double substituted variants, combining relevant mutations at both 97 and 232 positions, were constructed by site-directed mutagenesis. This work led to the isolation of one double substituted variant (D97A-V232F), which displays a total preference for the R-enantiomer. The highly reversed enantioselectivity of this variant is accompanied by a 4.5-fold enhancement of its activity toward the preferred enantiomer. The molecular docking of the R- and S-enantiomers in the wild-type enzyme and the D97A-V232F variant suggests that V232F mutation provides a more favorable stacking interaction for the phenyl group of the R-enantiomer, that could explain both the enhanced activity and the reversal of enantioselectivity. These results demonstrate the potential of rationally engineered mutations to further enhance enzyme activity and to modulate selectivity. Biotechnol. Bioeng. 2010;106: 852-859. Inverting enzyme enantioselectivity by protein engineering is still a great challenge. Lip2p lipase from Yarrowia lipolytica, which demonstrates a low S-enantioselectivity (E-value = 5) during the hydrolytic kinetic resolution of 2-bromo-phenyl acetic acid octyl esters (an important class of chemical intermediates in the pharmaceutical industry), was converted, by a rational engineering approach, into a totally R-selective enzyme (E-value > 200). This tremendous change in selectivity is the result of only two amino acid changes. The starting point of our strategy was the prior identification of two key positions, 97 and 232, for enantiomer discrimination. Four single substitution variants were recently identified as exhibiting a low inversion of selectivity coupled to a low-hydrolytic activity. On the basis of these results, six double substituted variants, combining relevant mutations at both 97 and 232 positions, were constructed by site-directed mutagenesis. This work led to the isolation of one double substituted variant (D97A-V232F), which displays a total preference for the R-enantiomer. The highly reversed enantioselectivity of this variant is accompanied by a 4.5-fold enhancement of its activity toward the preferred enantiomer. The molecular docking of the R- and S-enantiomers in the wild-type enzyme and the D97A-V232F variant suggests that V232F mutation provides a more favorable stacking interaction for the phenyl group of the R-enantiomer, that could explain both the enhanced activity and the reversal of enantioselectivity. These results demonstrate the potential of rationally engineered mutations to further enhance enzyme activity and to modulate selectivity.Inverting enzyme enantioselectivity by protein engineering is still a great challenge. Lip2p lipase from Yarrowia lipolytica, which demonstrates a low S-enantioselectivity (E-value = 5) during the hydrolytic kinetic resolution of 2-bromo-phenyl acetic acid octyl esters (an important class of chemical intermediates in the pharmaceutical industry), was converted, by a rational engineering approach, into a totally R-selective enzyme (E-value > 200). This tremendous change in selectivity is the result of only two amino acid changes. The starting point of our strategy was the prior identification of two key positions, 97 and 232, for enantiomer discrimination. Four single substitution variants were recently identified as exhibiting a low inversion of selectivity coupled to a low-hydrolytic activity. On the basis of these results, six double substituted variants, combining relevant mutations at both 97 and 232 positions, were constructed by site-directed mutagenesis. This work led to the isolation of one double substituted variant (D97A-V232F), which displays a total preference for the R-enantiomer. The highly reversed enantioselectivity of this variant is accompanied by a 4.5-fold enhancement of its activity toward the preferred enantiomer. The molecular docking of the R- and S-enantiomers in the wild-type enzyme and the D97A-V232F variant suggests that V232F mutation provides a more favorable stacking interaction for the phenyl group of the R-enantiomer, that could explain both the enhanced activity and the reversal of enantioselectivity. These results demonstrate the potential of rationally engineered mutations to further enhance enzyme activity and to modulate selectivity. |
| Author | André, Isabelle Duquesne, Sophie Piamtongkam, Rungtiwa Marty, Alain Cambon, Emmanuelle Bordes, Florence |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/20506522$$D View this record in MEDLINE/PubMed https://hal.inrae.fr/hal-02956412$$DView record in HAL |
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| Notes | http://dx.doi.org/10.1002/bit.22770 ArticleID:BIT22770 Emmanuelle Cambon and Rungtiwa Piamtongkam, equally contributed to the study. ark:/67375/WNG-2S0KW0QV-H istex:6A2E29BAB549A4DA9A49ADFF8FA70287C70DF505 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 14 ObjectType-Article-1 ObjectType-Feature-2 content type line 23 |
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| References | Ceynowa J, Rauchfleisz M. 2003. High enantioselective resolution of racemic 2-arylpropionic acids in an enzyme membrane reactor. J Mol Catal B: Enzyme 23(1): 43. Bordes F, Cambon E, Dossat-Letisse V, André I, Croux C, Nicaud JM, Marty A. 2009. Improvement of Yarrowia lipolytica lipase enantioselectivity by using mutagenesis targeted to the substrate binding site. ChemBioChem 10(10): 1705-1713. DeLano WL. 2002. The PyMOL Molecular Graphics System (2002) on World Wide Web. CA, USA: San Carlos. http://www.pymol.org. Lafaquière V, Barbe S, Puech-Guenot S, Guieysse D, Cortés J, Monsan P, Siméon T, André I, Remaud-Siméon M. 2009. Control of lipase enantioselectivity by engineering the substrate binding site and access channel. ChemBioChem 10(17): 2760-2771. Choi G-S, Kim J-Y, Kim J-H, Ryu Y-W, Kim G-J. 2003. Construction and characterization of a recombinant esterase with high activity and enantioselectivity to (S)-ketoprofen ethyl ester. Protein Expr Purif 29(1): 85. Kramer B, Rarey M, Lengauer T. 1999. Evaluation of the FLEXX incremental construction algorithm for protein-ligand docking. Proteins 37(2): 228-241. Cancino M, Bauchart P, Sandoval G, Nicaud JM, André I, Dossat V, Marty A. 2008. A variant of Yarrowia lipolytica lipase with improved activity and enantioselectivity for resolution of 2-bromo-arylacetic acid esters. Tetrahedron: Asymmetry 19(13): 1608-1612. Rarey M, Kramer B, Lengauer T, Klebe G. 1996. A fast flexible docking method using an incremental construction algorithm. J Mol Biol 261(3): 470-489. Koga Y, Kato K, Nakano H, Yamane T. 2003. Inverting enantioselectivity of Burkholderia cepacia KWI-56 lipase by combinatorial mutation and high-throughput screening using single-molecule PCR and in vitro expression. J Mol Biol 331(3): 585-592. Pignede G, Wang H, Fudalej F, Gaillardin C, Seman M, Nicaud JM. 2000. Characterization of an extracellular lipase encoded by LIP2 in Yarrowia lipolytica . J Bacteriol 182(10): 2802-2810. Haughton L, Williams JMJ. 2001. Enzymatic hydrolysis and selective racemisation reactions of alpha-chloro esters. Synthesis-Stuttgart 6: 943-946. Zha D, Wilensek S, Hermes M, Jaeger KE, Reetz MT. 2001. Complete reversal of enantioselectivity of an enzyme-catalyzed reaction by directed evolution. Chem Commun 2001(24): 2664-2665. Bartsch S, Kourist R, Bornscheuer UT. 2008. Complete inversion of enantioselectivity towards acetylated tertiary alcohols by a double mutant of a Bacillus subtilis esterase. Angew Chem Int Ed Engl 47: 1508-1511. Cambon E, Piamtongkam R, Bordes F, Duquesne S, Laguerre S, Nicaud J, Marty A. 2010. A new Yarrowia lipolytica expression system: an efficient tool for rapid and reliable kinetic analysis of improved enzymes. Enzyme Microb Technol Submitted. Steenkamp L, Brady D. 2003. Screening of commercial enzymes for the enantioselective hydrolysis of R,S-naproxen ester. Enzyme Microb Technol 32(3-4): 472. Guieysse D, Sandoval G, Faure L, Nicaud J-M, Monsan P, Marty A. 2004. New efficient lipase from Yarrowia lipolytica for the resolution of 2-bromo-arylacetic acid esters. Tetrahedron: Asymmetry 15(22): 3539. Guieysse D, Salagnad C, Monsan P, Remaud-Simeon M. 2003. Lipase-catalyzed enantioselective transesterification toward esters of 2-bromo-tolylacetic acids. Tetrahedron: Asymmetry 14(3): 317-323. Jones MM, Williams JMJ. 1998. Dynamic kinetic resolution in the hydrolysis of an a-bromo ester. Chem Commun 1998(22): 2519-2520. Bordes F, Fudalej F, Dossat V, Nicaud JM, Marty A. 2007. A new recombinant protein expression system for high-throughput screening in the yeast Yarrowia lipolytica . J Microbiol Methods 70(3): 493-502. Ivancic M, Valinger G, Gruber K, Schwab H. 2007. Inverting enantioselectivity of Burkholderia gladioli esterase EstB by directed and designed evolution. J Biotechnol 129(1): 109-122. Brady D, Steenkamp L, Skein E, Chaplin JA, Reddy S. 2004. Optimisation of the enantioselective biocatalytic hydrolysis of naproxen ethyl ester using ChiroCLEC-CR. Enzyme Microb Technol 34(3-4): 283-291. Reetz MT, Wang LW, Bocola M. 2006. Directed evolution of enantioselective enzymes: Iterative cycles of CASTing for probing protein-sequence space. Angew Chem Int Ed Engl 45(8): 1236-1241. Overbeeke PLA, Jongejan JA. 2003. Enantioselectivity of Candida rugosa lipase in the hydrolysis of 2-chloropropionic acid methyl ester. J Mol Catal B: Enzyme 21(1-2): 89. Ahmed SN, Kazlauskas RJ, Morinville AH, Grochulski P, Schrag JD, Cygler M. 1994. Enantioselectivity of Candida rugosa lipase toward carboxylic acids: A predictive rule from substrate mapping and X-ray crystallography. Biocatal Biotransform 9(1): 209-225. 1994; 9 1998; 1998 2007; 129 2009; 10 2006; 45 2001; 6 2010 2008; 19 2004; 15 2004; 34 1999; 37 2008; 47 2000; 182 1996; 261 2003; 14 2007; 70 2003; 29 2002 2003; 331 2003; 21 2003; 32 2001; 2001 2003; 23 e_1_2_6_21_1 e_1_2_6_10_1 e_1_2_6_20_1 DeLano WL (e_1_2_6_11_1) 2002 e_1_2_6_9_1 e_1_2_6_8_1 e_1_2_6_19_1 e_1_2_6_5_1 e_1_2_6_4_1 e_1_2_6_7_1 e_1_2_6_6_1 e_1_2_6_13_1 e_1_2_6_25_1 e_1_2_6_14_1 e_1_2_6_24_1 e_1_2_6_3_1 e_1_2_6_23_1 e_1_2_6_2_1 e_1_2_6_12_1 e_1_2_6_22_1 e_1_2_6_17_1 e_1_2_6_18_1 e_1_2_6_15_1 e_1_2_6_16_1 |
| References_xml | – reference: Brady D, Steenkamp L, Skein E, Chaplin JA, Reddy S. 2004. Optimisation of the enantioselective biocatalytic hydrolysis of naproxen ethyl ester using ChiroCLEC-CR. Enzyme Microb Technol 34(3-4): 283-291. – reference: Kramer B, Rarey M, Lengauer T. 1999. Evaluation of the FLEXX incremental construction algorithm for protein-ligand docking. Proteins 37(2): 228-241. – reference: Overbeeke PLA, Jongejan JA. 2003. Enantioselectivity of Candida rugosa lipase in the hydrolysis of 2-chloropropionic acid methyl ester. J Mol Catal B: Enzyme 21(1-2): 89. – reference: Reetz MT, Wang LW, Bocola M. 2006. Directed evolution of enantioselective enzymes: Iterative cycles of CASTing for probing protein-sequence space. Angew Chem Int Ed Engl 45(8): 1236-1241. – reference: Haughton L, Williams JMJ. 2001. Enzymatic hydrolysis and selective racemisation reactions of alpha-chloro esters. Synthesis-Stuttgart 6: 943-946. – reference: Bordes F, Fudalej F, Dossat V, Nicaud JM, Marty A. 2007. A new recombinant protein expression system for high-throughput screening in the yeast Yarrowia lipolytica . J Microbiol Methods 70(3): 493-502. – reference: Choi G-S, Kim J-Y, Kim J-H, Ryu Y-W, Kim G-J. 2003. Construction and characterization of a recombinant esterase with high activity and enantioselectivity to (S)-ketoprofen ethyl ester. Protein Expr Purif 29(1): 85. – reference: Lafaquière V, Barbe S, Puech-Guenot S, Guieysse D, Cortés J, Monsan P, Siméon T, André I, Remaud-Siméon M. 2009. Control of lipase enantioselectivity by engineering the substrate binding site and access channel. ChemBioChem 10(17): 2760-2771. – reference: Guieysse D, Sandoval G, Faure L, Nicaud J-M, Monsan P, Marty A. 2004. New efficient lipase from Yarrowia lipolytica for the resolution of 2-bromo-arylacetic acid esters. Tetrahedron: Asymmetry 15(22): 3539. – reference: Bartsch S, Kourist R, Bornscheuer UT. 2008. Complete inversion of enantioselectivity towards acetylated tertiary alcohols by a double mutant of a Bacillus subtilis esterase. Angew Chem Int Ed Engl 47: 1508-1511. – reference: Zha D, Wilensek S, Hermes M, Jaeger KE, Reetz MT. 2001. Complete reversal of enantioselectivity of an enzyme-catalyzed reaction by directed evolution. Chem Commun 2001(24): 2664-2665. – reference: Pignede G, Wang H, Fudalej F, Gaillardin C, Seman M, Nicaud JM. 2000. Characterization of an extracellular lipase encoded by LIP2 in Yarrowia lipolytica . J Bacteriol 182(10): 2802-2810. – reference: Cancino M, Bauchart P, Sandoval G, Nicaud JM, André I, Dossat V, Marty A. 2008. A variant of Yarrowia lipolytica lipase with improved activity and enantioselectivity for resolution of 2-bromo-arylacetic acid esters. Tetrahedron: Asymmetry 19(13): 1608-1612. – reference: Rarey M, Kramer B, Lengauer T, Klebe G. 1996. A fast flexible docking method using an incremental construction algorithm. J Mol Biol 261(3): 470-489. – reference: Ahmed SN, Kazlauskas RJ, Morinville AH, Grochulski P, Schrag JD, Cygler M. 1994. Enantioselectivity of Candida rugosa lipase toward carboxylic acids: A predictive rule from substrate mapping and X-ray crystallography. Biocatal Biotransform 9(1): 209-225. – reference: Cambon E, Piamtongkam R, Bordes F, Duquesne S, Laguerre S, Nicaud J, Marty A. 2010. A new Yarrowia lipolytica expression system: an efficient tool for rapid and reliable kinetic analysis of improved enzymes. Enzyme Microb Technol Submitted. – reference: Jones MM, Williams JMJ. 1998. Dynamic kinetic resolution in the hydrolysis of an a-bromo ester. Chem Commun 1998(22): 2519-2520. – reference: Ivancic M, Valinger G, Gruber K, Schwab H. 2007. Inverting enantioselectivity of Burkholderia gladioli esterase EstB by directed and designed evolution. J Biotechnol 129(1): 109-122. – reference: DeLano WL. 2002. The PyMOL Molecular Graphics System (2002) on World Wide Web. CA, USA: San Carlos. http://www.pymol.org. – reference: Koga Y, Kato K, Nakano H, Yamane T. 2003. Inverting enantioselectivity of Burkholderia cepacia KWI-56 lipase by combinatorial mutation and high-throughput screening using single-molecule PCR and in vitro expression. J Mol Biol 331(3): 585-592. – reference: Bordes F, Cambon E, Dossat-Letisse V, André I, Croux C, Nicaud JM, Marty A. 2009. Improvement of Yarrowia lipolytica lipase enantioselectivity by using mutagenesis targeted to the substrate binding site. ChemBioChem 10(10): 1705-1713. – reference: Ceynowa J, Rauchfleisz M. 2003. High enantioselective resolution of racemic 2-arylpropionic acids in an enzyme membrane reactor. J Mol Catal B: Enzyme 23(1): 43. – reference: Guieysse D, Salagnad C, Monsan P, Remaud-Simeon M. 2003. Lipase-catalyzed enantioselective transesterification toward esters of 2-bromo-tolylacetic acids. Tetrahedron: Asymmetry 14(3): 317-323. – reference: Steenkamp L, Brady D. 2003. Screening of commercial enzymes for the enantioselective hydrolysis of R,S-naproxen ester. Enzyme Microb Technol 32(3-4): 472. – volume: 47 start-page: 1508 year: 2008 end-page: 1511 article-title: Complete inversion of enantioselectivity towards acetylated tertiary alcohols by a double mutant of a esterase publication-title: Angew Chem Int Ed Engl – volume: 37 start-page: 228 issue: 2 year: 1999 end-page: 241 article-title: Evaluation of the FLEXX incremental construction algorithm for protein‐ligand docking publication-title: Proteins – volume: 261 start-page: 470 issue: 3 year: 1996 end-page: 489 article-title: A fast flexible docking method using an incremental construction algorithm publication-title: J Mol Biol – volume: 9 start-page: 209 issue: 1 year: 1994 end-page: 225 article-title: Enantioselectivity of lipase toward carboxylic acids: A predictive rule from substrate mapping and X‐ray crystallography publication-title: Biocatal Biotransform – volume: 19 start-page: 1608 issue: 13 year: 2008 end-page: 1612 article-title: A variant of lipase with improved activity and enantioselectivity for resolution of 2‐bromo‐arylacetic acid esters publication-title: Tetrahedron: Asymmetry – volume: 15 start-page: 3539 issue: 22 year: 2004 article-title: New efficient lipase from for the resolution of 2‐bromo‐arylacetic acid esters publication-title: Tetrahedron: Asymmetry – volume: 331 start-page: 585 issue: 3 year: 2003 end-page: 592 article-title: Inverting enantioselectivity of KWI‐56 lipase by combinatorial mutation and high‐throughput screening using single‐molecule PCR and in vitro expression publication-title: J Mol Biol – volume: 129 start-page: 109 issue: 1 year: 2007 end-page: 122 article-title: Inverting enantioselectivity of esterase EstB by directed and designed evolution publication-title: J Biotechnol – volume: 45 start-page: 1236 issue: 8 year: 2006 end-page: 1241 article-title: Directed evolution of enantioselective enzymes: Iterative cycles of CASTing for probing protein‐sequence space publication-title: Angew Chem Int Ed Engl – volume: 1998 start-page: 2519 issue: 22 year: 1998 end-page: 2520 article-title: Dynamic kinetic resolution in the hydrolysis of an a‐bromo ester publication-title: Chem Commun – volume: 70 start-page: 493 issue: 3 year: 2007 end-page: 502 article-title: A new recombinant protein expression system for high‐throughput screening in the yeast publication-title: J Microbiol Methods – year: 2002 – volume: 6 start-page: 943 year: 2001 end-page: 946 article-title: Enzymatic hydrolysis and selective racemisation reactions of alpha‐chloro esters publication-title: Synthesis‐Stuttgart – volume: 34 start-page: 283 issue: 3–4 year: 2004 end-page: 291 article-title: Optimisation of the enantioselective biocatalytic hydrolysis of naproxen ethyl ester using ChiroCLEC‐CR publication-title: Enzyme Microb Technol – volume: 182 start-page: 2802 issue: 10 year: 2000 end-page: 2810 article-title: Characterization of an extracellular lipase encoded by LIP2 in publication-title: J Bacteriol – volume: 32 start-page: 472 issue: 3–4 year: 2003 article-title: Screening of commercial enzymes for the enantioselective hydrolysis of R,S‐naproxen ester publication-title: Enzyme Microb Technol – volume: 10 start-page: 1705 issue: 10 year: 2009 end-page: 1713 article-title: Improvement of lipase enantioselectivity by using mutagenesis targeted to the substrate binding site publication-title: ChemBioChem – volume: 2001 start-page: 2664 issue: 24 year: 2001 end-page: 2665 article-title: Complete reversal of enantioselectivity of an enzyme‐catalyzed reaction by directed evolution publication-title: Chem Commun – volume: 23 start-page: 43 issue: 1 year: 2003 article-title: High enantioselective resolution of racemic 2‐arylpropionic acids in an enzyme membrane reactor publication-title: J Mol Catal B: Enzyme – volume: 29 start-page: 85 issue: 1 year: 2003 article-title: Construction and characterization of a recombinant esterase with high activity and enantioselectivity to (S)‐ketoprofen ethyl ester publication-title: Protein Expr Purif – volume: 21 start-page: 89 issue: 1–2 year: 2003 article-title: Enantioselectivity of lipase in the hydrolysis of 2‐chloropropionic acid methyl ester publication-title: J Mol Catal B: Enzyme – volume: 14 start-page: 317 issue: 3 year: 2003 end-page: 323 article-title: Lipase‐catalyzed enantioselective transesterification toward esters of 2‐bromo‐tolylacetic acids publication-title: Tetrahedron: Asymmetry – volume: 10 start-page: 2760 issue: 17 year: 2009 end-page: 2771 article-title: Control of lipase enantioselectivity by engineering the substrate binding site and access channel publication-title: ChemBioChem – year: 2010 article-title: A new expression system: an efficient tool for rapid and reliable kinetic analysis of improved enzymes publication-title: Enzyme Microb Technol Submitted – ident: e_1_2_6_23_1 doi: 10.1002/anie.200502746 – ident: e_1_2_6_16_1 doi: 10.1039/a807232i – ident: e_1_2_6_2_1 doi: 10.3109/10242429408992121 – ident: e_1_2_6_8_1 doi: 10.1016/j.tetasy.2008.06.009 – ident: e_1_2_6_12_1 doi: 10.1016/S0957-4166(02)00784-X – ident: e_1_2_6_24_1 doi: 10.1016/S0141-0229(02)00335-6 – ident: e_1_2_6_19_1 doi: 10.1002/cbic.200900439 – ident: e_1_2_6_21_1 doi: 10.1128/JB.182.10.2802-2810.2000 – volume-title: The PyMOL Molecular Graphics System (2002) on World Wide Web year: 2002 ident: e_1_2_6_11_1 – ident: e_1_2_6_14_1 doi: 10.1055/s-2001-13395 – ident: e_1_2_6_3_1 doi: 10.1002/anie.200704606 – ident: e_1_2_6_4_1 doi: 10.1016/j.mimet.2007.06.008 – ident: e_1_2_6_22_1 doi: 10.1006/jmbi.1996.0477 – ident: e_1_2_6_20_1 doi: 10.1016/S1381-1177(02)00143-1 – ident: e_1_2_6_15_1 doi: 10.1016/j.jbiotec.2006.10.007 – ident: e_1_2_6_17_1 doi: 10.1016/S0022-2836(03)00782-4 – ident: e_1_2_6_5_1 doi: 10.1002/cbic.200900215 – ident: e_1_2_6_13_1 doi: 10.1016/j.tetasy.2004.09.008 – ident: e_1_2_6_6_1 doi: 10.1016/j.enzmictec.2003.11.002 – ident: e_1_2_6_9_1 doi: 10.1016/S1381-1177(03)00066-3 – ident: e_1_2_6_10_1 doi: 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| Snippet | Inverting enzyme enantioselectivity by protein engineering is still a great challenge. Lip2p lipase from Yarrowia lipolytica, which demonstrates a low... Inverting enzyme enantioselectivity by protein engineering is still a great challenge. Lip2p lipase from Yarrowia lipolytica , which demonstrates a low S... |
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| SubjectTerms | Acetates - metabolism Acetic acid Amino Acid Substitution Amino acids Bioengineering Biotechnology enantioselectivity Enzymatic activity enzyme evolution Enzyme kinetics Esters Fungal Proteins - genetics Fungal Proteins - metabolism Hydrocarbons, Brominated - metabolism Life Sciences lipase Lipase - genetics Lipase - metabolism Molecular Dynamics Simulation Mutagenesis Mutagenesis, Site-Directed Mutation Pharmaceutical industry Phenylacetates - metabolism Protein folding rational engineering Stereoisomerism Substrate Specificity Yarrowia - enzymology Yarrowia lipolytica |
| Title | Rationally engineered double substituted variants of Yarrowia lipolytica lipase with enhanced activity coupled with highly inverted enantioselectivity towards 2-bromo phenyl acetic acid esters |
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