Origin of the Enantioselectivity of Lipases Explained by a Stereo-Sensing Mechanism Operative at the Transition State

Bulletin of the Chemical Society of Japan

Volumn 71, Issue 2, 1998, Pages 443-453

  Ema, Tadashi ^a   Kobayashi, Juka ^a   Maeno, Soichi ^a   Sakai, Takashi ^a   Utaka, Masanori ^a  

^a OKAYAMA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0001215393     PISSN: 00092673     EISSN: None     Source Type: Journal    
DOI: 10.1246/bcsj.71.443     Document Type: Article

References (84)

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2. For leading reviews and books, see: a) J. B. Jones, Tetrahedron, 42, 3351 (1986); b) C.-S. Chen and C. J. Sih, Angew. Chem., Int. Ed. Engl., 28, 695 (1989); c) A. M. Klibanov, Ace. Chem. Res., 23, 114 (1990); d) "Lipases: Structure, Mechanism and Genetic Engineering," ed by L. Alberghina, R. D. Schmid, and R. Verger, VCH, Weinheim (1991); e) "Preparative Biotransformations: Whole Cell and Isolated Enzymes in Organic Synthesis," ed by S. M. Roberts, K. Wiggins, and G. Casy, John Wiley & Sons, Chichester (1993); f) C.-H. Wong and G. M. Whitesides, "Enzymes in Synthetic Organic Chemistry," Pergamon, Oxford (1994); g) "Enzyme Catalysis in Organic Synthesis," ed by K. Drauz and H. Waldmann, VCH, New York (1994), Vol. 1; h) K. Faber, "Biotransformations in Organic Chemistry," Springer-Verlag, Berlin (1995); i) "Enzymatic Reactions in Organic Media," ed by A. M. P. Koskinen and A. M. Klibanov, Blackie Academic, Glasgow (1996).
3. For leading reviews and books, see: a) J. B. Jones, Tetrahedron, 42, 3351 (1986); b) C.-S. Chen and C. J. Sih, Angew. Chem., Int. Ed. Engl., 28, 695 (1989); c) A. M. Klibanov, Ace. Chem. Res., 23, 114 (1990); d) "Lipases: Structure, Mechanism and Genetic Engineering," ed by L. Alberghina, R. D. Schmid, and R. Verger, VCH, Weinheim (1991); e) "Preparative Biotransformations: Whole Cell and Isolated Enzymes in Organic Synthesis," ed by S. M. Roberts, K. Wiggins, and G. Casy, John Wiley & Sons, Chichester (1993); f) C.-H. Wong and G. M. Whitesides, "Enzymes in Synthetic Organic Chemistry," Pergamon, Oxford (1994); g) "Enzyme Catalysis in Organic Synthesis," ed by K. Drauz and H. Waldmann, VCH, New York (1994), Vol. 1; h) K. Faber, "Biotransformations in Organic Chemistry," Springer-Verlag, Berlin (1995); i) "Enzymatic Reactions in Organic Media," ed by A. M. P. Koskinen and A. M. Klibanov, Blackie Academic, Glasgow (1996).
4. For leading reviews and books, see: a) J. B. Jones, Tetrahedron, 42, 3351 (1986); b) C.-S. Chen and C. J. Sih, Angew. Chem., Int. Ed. Engl., 28, 695 (1989); c) A. M. Klibanov, Ace. Chem. Res., 23, 114 (1990); d) "Lipases: Structure, Mechanism and Genetic Engineering," ed by L. Alberghina, R. D. Schmid, and R. Verger, VCH, Weinheim (1991); e) "Preparative Biotransformations: Whole Cell and Isolated Enzymes in Organic Synthesis," ed by S. M. Roberts, K. Wiggins, and G. Casy, John Wiley & Sons, Chichester (1993); f) C.-H. Wong and G. M. Whitesides, "Enzymes in Synthetic Organic Chemistry," Pergamon, Oxford (1994); g) "Enzyme Catalysis in Organic Synthesis," ed by K. Drauz and H. Waldmann, VCH, New York (1994), Vol. 1; h) K. Faber, "Biotransformations in Organic Chemistry," Springer-Verlag, Berlin (1995); i) "Enzymatic Reactions in Organic Media," ed by A. M. P. Koskinen and A. M. Klibanov, Blackie Academic, Glasgow (1996).
5. For leading reviews and books, see: a) J. B. Jones, Tetrahedron, 42, 3351 (1986); b) C.-S. Chen and C. J. Sih, Angew. Chem., Int. Ed. Engl., 28, 695 (1989); c) A. M. Klibanov, Ace. Chem. Res., 23, 114 (1990); d) "Lipases: Structure, Mechanism and Genetic Engineering," ed by L. Alberghina, R. D. Schmid, and R. Verger, VCH, Weinheim (1991); e) "Preparative Biotransformations: Whole Cell and Isolated Enzymes in Organic Synthesis," ed by S. M. Roberts, K. Wiggins, and G. Casy, John Wiley & Sons, Chichester (1993); f) C.-H. Wong and G. M. Whitesides, "Enzymes in Synthetic Organic Chemistry," Pergamon, Oxford (1994); g) "Enzyme Catalysis in Organic Synthesis," ed by K. Drauz and H. Waldmann, VCH, New York (1994), Vol. 1; h) K. Faber, "Biotransformations in Organic Chemistry," Springer-Verlag, Berlin (1995); i) "Enzymatic Reactions in Organic Media," ed by A. M. P. Koskinen and A. M. Klibanov, Blackie Academic, Glasgow (1996).
6. For leading reviews and books, see: a) J. B. Jones, Tetrahedron, 42, 3351 (1986); b) C.-S. Chen and C. J. Sih, Angew. Chem., Int. Ed. Engl., 28, 695 (1989); c) A. M. Klibanov, Ace. Chem. Res., 23, 114 (1990); d) "Lipases: Structure, Mechanism and Genetic Engineering," ed by L. Alberghina, R. D. Schmid, and R. Verger, VCH, Weinheim (1991); e) "Preparative Biotransformations: Whole Cell and Isolated Enzymes in Organic Synthesis," ed by S. M. Roberts, K. Wiggins, and G. Casy, John Wiley & Sons, Chichester (1993); f) C.-H. Wong and G. M. Whitesides, "Enzymes in Synthetic Organic Chemistry," Pergamon, Oxford (1994); g) "Enzyme Catalysis in Organic Synthesis," ed by K. Drauz and H. Waldmann, VCH, New York (1994), Vol. 1; h) K. Faber, "Biotransformations in Organic Chemistry," Springer-Verlag, Berlin (1995); i) "Enzymatic Reactions in Organic Media," ed by A. M. P. Koskinen and A. M. Klibanov, Blackie Academic, Glasgow (1996).
7. For leading reviews and books, see: a) J. B. Jones, Tetrahedron, 42, 3351 (1986); b) C.-S. Chen and C. J. Sih, Angew. Chem., Int. Ed. Engl., 28, 695 (1989); c) A. M. Klibanov, Ace. Chem. Res., 23, 114 (1990); d) "Lipases: Structure, Mechanism and Genetic Engineering," ed by L. Alberghina, R. D. Schmid, and R. Verger, VCH, Weinheim (1991); e) "Preparative Biotransformations: Whole Cell and Isolated Enzymes in Organic Synthesis," ed by S. M. Roberts, K. Wiggins, and G. Casy, John Wiley & Sons, Chichester (1993); f) C.-H. Wong and G. M. Whitesides, "Enzymes in Synthetic Organic Chemistry," Pergamon, Oxford (1994); g) "Enzyme Catalysis in Organic Synthesis," ed by K. Drauz and H. Waldmann, VCH, New York (1994), Vol. 1; h) K. Faber, "Biotransformations in Organic Chemistry," Springer-Verlag, Berlin (1995); i) "Enzymatic Reactions in Organic Media," ed by A. M. P. Koskinen and A. M. Klibanov, Blackie Academic, Glasgow (1996).
8. For leading reviews and books, see: a) J. B. Jones, Tetrahedron, 42, 3351 (1986); b) C.-S. Chen and C. J. Sih, Angew. Chem., Int. Ed. Engl., 28, 695 (1989); c) A. M. Klibanov, Ace. Chem. Res., 23, 114 (1990); d) "Lipases: Structure, Mechanism and Genetic Engineering," ed by L. Alberghina, R. D. Schmid, and R. Verger, VCH, Weinheim (1991); e) "Preparative Biotransformations: Whole Cell and Isolated Enzymes in Organic Synthesis," ed by S. M. Roberts, K. Wiggins, and G. Casy, John Wiley & Sons, Chichester (1993); f) C.-H. Wong and G. M. Whitesides, "Enzymes in Synthetic Organic Chemistry," Pergamon, Oxford (1994); g) "Enzyme Catalysis in Organic Synthesis," ed by K. Drauz and H. Waldmann, VCH, New York (1994), Vol. 1; h) K. Faber, "Biotransformations in Organic Chemistry," Springer-Verlag, Berlin (1995); i) "Enzymatic Reactions in Organic Media," ed by A. M. P. Koskinen and A. M. Klibanov, Blackie Academic, Glasgow (1996).
9. For leading reviews and books, see: a) J. B. Jones, Tetrahedron, 42, 3351 (1986); b) C.-S. Chen and C. J. Sih, Angew. Chem., Int. Ed. Engl., 28, 695 (1989); c) A. M. Klibanov, Ace. Chem. Res., 23, 114 (1990); d) "Lipases: Structure, Mechanism and Genetic Engineering," ed by L. Alberghina, R. D. Schmid, and R. Verger, VCH, Weinheim (1991); e) "Preparative Biotransformations: Whole Cell and Isolated Enzymes in Organic Synthesis," ed by S. M. Roberts, K. Wiggins, and G. Casy, John Wiley & Sons, Chichester (1993); f) C.-H. Wong and G. M. Whitesides, "Enzymes in Synthetic Organic Chemistry," Pergamon, Oxford (1994); g) "Enzyme Catalysis in Organic Synthesis," ed by K. Drauz and H. Waldmann, VCH, New York (1994), Vol. 1; h) K. Faber, "Biotransformations in Organic Chemistry," Springer-Verlag, Berlin (1995); i) "Enzymatic Reactions in Organic Media," ed by A. M. P. Koskinen and A. M. Klibanov, Blackie Academic, Glasgow (1996).
10. Abbreviations for the enzymes used in this paper: Rhizomucor miehei lipase = RML; Candida antarctica lipase (isoform B) = CAL; Pseudomonas cepacia lipase = PCL; Candida rugosa lipase = CRL; Humicola lanuginosa lipase = HLL.
11. For RML, see: a) A. M. Brzozowski, U. Derewenda, Z. S. Derewenda, G. G. Dodson, D. M. Lawson, J. P. Turkenburg, F. Bjorkling, B. Huge-Jensen, S. A. Patkar, and L. Thim, Nature, 351, 491 (1991); b) U. Derewenda, A. M. Brzozowski, D. M. Lawson, and Z. S. Derewenda, Biochemistry, 31, 1532 (1992). For human pancreatic lipase, see: c) F. K. Winkler, A. D'Arcy, and W. Hunziker, Nature, 343, 771 (1990). For Geotrichum candidum lipase, see: d) J. D. Schrag, Y. Li, S. Wu, and M. Cygler, Nature, 351, 761 (1991).
12. For RML, see: a) A. M. Brzozowski, U. Derewenda, Z. S. Derewenda, G. G. Dodson, D. M. Lawson, J. P. Turkenburg, F. Bjorkling, B. Huge-Jensen, S. A. Patkar, and L. Thim, Nature, 351, 491 (1991); b) U. Derewenda, A. M. Brzozowski, D. M. Lawson, and Z. S. Derewenda, Biochemistry, 31, 1532 (1992). For human pancreatic lipase, see: c) F. K. Winkler, A. D'Arcy, and W. Hunziker, Nature, 343, 771 (1990). For Geotrichum candidum lipase, see: d) J. D. Schrag, Y. Li, S. Wu, and M. Cygler, Nature, 351, 761 (1991).
13. For RML, see: a) A. M. Brzozowski, U. Derewenda, Z. S. Derewenda, G. G. Dodson, D. M. Lawson, J. P. Turkenburg, F. Bjorkling, B. Huge-Jensen, S. A. Patkar, and L. Thim, Nature, 351, 491 (1991); b) U. Derewenda, A. M. Brzozowski, D. M. Lawson, and Z. S. Derewenda, Biochemistry, 31, 1532 (1992). For human pancreatic lipase, see: c) F. K. Winkler, A. D'Arcy, and W. Hunziker, Nature, 343, 771 (1990). For Geotrichum candidum lipase, see: d) J. D. Schrag, Y. Li, S. Wu, and M. Cygler, Nature, 351, 761 (1991).
14. For RML, see: a) A. M. Brzozowski, U. Derewenda, Z. S. Derewenda, G. G. Dodson, D. M. Lawson, J. P. Turkenburg, F. Bjorkling, B. Huge-Jensen, S. A. Patkar, and L. Thim, Nature, 351, 491 (1991); b) U. Derewenda, A. M. Brzozowski, D. M. Lawson, and Z. S. Derewenda, Biochemistry, 31, 1532 (1992). For human pancreatic lipase, see: c) F. K. Winkler, A. D'Arcy, and W. Hunziker, Nature, 343, 771 (1990). For Geotrichum candidum lipase, see: d) J. D. Schrag, Y. Li, S. Wu, and M. Cygler, Nature, 351, 761 (1991).
15. For CRL, see: e) P. Grochulski, F. Bouthillier, R. J. Kazlauskas, A. N. Serreqi, J. D. Schrag, E. Ziomek, and M. Cygler, Biochemistry, 33, 3494 (1994); f) M. Cygler, P. Grochulski, R. J. Kazlauskas, J. D. Schrag, F. Bouthillier, B. Rubin, A. N. Serreqi, and A. K. Gupta, J. Am. Chem. Soc., 116, 3180 (1994). For CAL, see; g) J. Uppenberg, M. T. Hansen, S. Patkar, and T. A. Jones, Structure, 2, 293 (1994). For Pseudomonas glumae lipase, see: h) M. E. M. Noble, A. Cleasby, L. N. Johnson, M. R. Egmond, and L. G. J.Frenken, FEBS Lett., 331, 123 (1993). For HLL, see: i) D. M. Lawson, A. M. Brzozowski, S. Rety, C. Verma, and G. G. Dodson, Protein Eng., 7, 543 (1994).
16. For CRL, see: e) P. Grochulski, F. Bouthillier, R. J. Kazlauskas, A. N. Serreqi, J. D. Schrag, E. Ziomek, and M. Cygler, Biochemistry, 33, 3494 (1994); f) M. Cygler, P. Grochulski, R. J. Kazlauskas, J. D. Schrag, F. Bouthillier, B. Rubin, A. N. Serreqi, and A. K. Gupta, J. Am. Chem. Soc., 116, 3180 (1994). For CAL, see; g) J. Uppenberg, M. T. Hansen, S. Patkar, and T. A. Jones, Structure, 2, 293 (1994). For Pseudomonas glumae lipase, see: h) M. E. M. Noble, A. Cleasby, L. N. Johnson, M. R. Egmond, and L. G. J.Frenken, FEBS Lett., 331, 123 (1993). For HLL, see: i) D. M. Lawson, A. M. Brzozowski, S. Rety, C. Verma, and G. G. Dodson, Protein Eng., 7, 543 (1994).
17. For CRL, see: e) P. Grochulski, F. Bouthillier, R. J. Kazlauskas, A. N. Serreqi, J. D. Schrag, E. Ziomek, and M. Cygler, Biochemistry, 33, 3494 (1994); f) M. Cygler, P. Grochulski, R. J. Kazlauskas, J. D. Schrag, F. Bouthillier, B. Rubin, A. N. Serreqi, and A. K. Gupta, J. Am. Chem. Soc., 116, 3180 (1994). For CAL, see; g) J. Uppenberg, M. T. Hansen, S. Patkar, and T. A. Jones, Structure, 2, 293 (1994). For Pseudomonas glumae lipase, see: h) M. E. M. Noble, A. Cleasby, L. N. Johnson, M. R. Egmond, and L. G. J.Frenken, FEBS Lett., 331, 123 (1993). For HLL, see: i) D. M. Lawson, A. M. Brzozowski, S. Rety, C. Verma, and G. G. Dodson, Protein Eng., 7, 543 (1994).
18. For CRL, see: e) P. Grochulski, F. Bouthillier, R. J. Kazlauskas, A. N. Serreqi, J. D. Schrag, E. Ziomek, and M. Cygler, Biochemistry, 33, 3494 (1994); f) M. Cygler, P. Grochulski, R. J. Kazlauskas, J. D. Schrag, F. Bouthillier, B. Rubin, A. N. Serreqi, and A. K. Gupta, J. Am. Chem. Soc., 116, 3180 (1994). For CAL, see; g) J. Uppenberg, M. T. Hansen, S. Patkar, and T. A. Jones, Structure, 2, 293 (1994). For Pseudomonas glumae lipase, see: h) M. E. M. Noble, A. Cleasby, L. N. Johnson, M. R. Egmond, and L. G. J.Frenken, FEBS Lett., 331, 123 (1993). For HLL, see: i) D. M. Lawson, A. M. Brzozowski, S. Rety, C. Verma, and G. G. Dodson, Protein Eng., 7, 543 (1994).
19. For CRL, see: e) P. Grochulski, F. Bouthillier, R. J. Kazlauskas, A. N. Serreqi, J. D. Schrag, E. Ziomek, and M. Cygler, Biochemistry, 33, 3494 (1994); f) M. Cygler, P. Grochulski, R. J. Kazlauskas, J. D. Schrag, F. Bouthillier, B. Rubin, A. N. Serreqi, and A. K. Gupta, J. Am. Chem. Soc., 116, 3180 (1994). For CAL, see; g) J. Uppenberg, M. T. Hansen, S. Patkar, and T. A. Jones, Structure, 2, 293 (1994). For Pseudomonas glumae lipase, see: h) M. E. M. Noble, A. Cleasby, L. N. Johnson, M. R. Egmond, and L. G. J.Frenken, FEBS Lett., 331, 123 (1993). For HLL, see: i) D. M. Lawson, A. M. Brzozowski, S. Rety, C. Verma, and G. G. Dodson, Protein Eng., 7, 543 (1994).
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51. For computational calculations regarding the stereoelectronic effect, see: a) S. David, O. Eisenstein, W. J. Hehre, L. Salem, and R. Hoffmann, J. Am. Chem. Soc., 95, 3806 (1973); b) J.-M. Lehn and G. Wipff, J. Am. Chem. Soc., 96, 4048 (1974); c) J.-M. Lehn, G. Wipff, and H.-B. Bürgi, Helv. Chim. Acta, 57, 493 (1974); d) D. G. Gorenstein, J. B. Findlay, B. A. Luxon, and D. Kar, J. Am. Chem. Soc., 99, 3473 (1977); e) K. Taira and D. G. Gorenstein, Bull. Chem. Soc. Jpn., 60, 3625 (1987).
52. For computational calculations regarding the stereoelectronic effect, see: a) S. David, O. Eisenstein, W. J. Hehre, L. Salem, and R. Hoffmann, J. Am. Chem. Soc., 95, 3806 (1973); b) J.-M. Lehn and G. Wipff, J. Am. Chem. Soc., 96, 4048 (1974); c) J.-M. Lehn, G. Wipff, and H.-B. Bürgi, Helv. Chim. Acta, 57, 493 (1974); d) D. G. Gorenstein, J. B. Findlay, B. A. Luxon, and D. Kar, J. Am. Chem. Soc., 99, 3473 (1977); e) K. Taira and D. G. Gorenstein, Bull. Chem. Soc. Jpn., 60, 3625 (1987).
53. For computational calculations regarding the stereoelectronic effect, see: a) S. David, O. Eisenstein, W. J. Hehre, L. Salem, and R. Hoffmann, J. Am. Chem. Soc., 95, 3806 (1973); b) J.-M. Lehn and G. Wipff, J. Am. Chem. Soc., 96, 4048 (1974); c) J.-M. Lehn, G. Wipff, and H.-B. Bürgi, Helv. Chim. Acta, 57, 493 (1974); d) D. G. Gorenstein, J. B. Findlay, B. A. Luxon, and D. Kar, J. Am. Chem. Soc., 99, 3473 (1977); e) K. Taira and D. G. Gorenstein, Bull. Chem. Soc. Jpn., 60, 3625 (1987).
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64. 16c)
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67. 3)
68. 2 = -90.1° →- 122.5°.
69. 3)
70. 3b)
71. -1 (substrate) = -22.1 (3), -4.1 (4), -23.6 (5). These enantioselectivities estimated are higher limit, because even a small shift of the atoms which were fixed in our calculations could relax the strain to reduce the enantioselectivity.
72. 3i)
73. Figure 6a can explain the high enantioselectivities generally observed for 2-alkanols because the methyl group attached to the chiral carbon of the (R)-enantiomers is unlikely to disturb the triangular wall considerably. The experimentally observed trend that as the smaller substituent (M) is more bulky both the enantioselectivity and reactivity are lowered can be explained by the smaller substituent of the (R)-enantiomer giving a steric pressure against the triangular wall (see Fig. 6a).
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76. 3e)
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80. 5e)
81. For other approaches to understand the factors determining the stereoselectivity of hydrolytic enzymes, see: a) M. Norin, K. Huit, A. Mattson, and T. Norin, Biocatalysis, 7, 131 (1993); b) T. Lee and J. B. Jones, J. Am. Chem. Soc., 118, 502 (1996); c) V. Martichonok and J. B. Jones, J. Am. Chem. Soc., 118, 950 (1996); d) T. Ke, C. R. Wescott, and A. M. Klibanov, J. Am. Chem. Soc., 118, 3366 (1996).
82. For other approaches to understand the factors determining the stereoselectivity of hydrolytic enzymes, see: a) M. Norin, K. Huit, A. Mattson, and T. Norin, Biocatalysis, 7, 131 (1993); b) T. Lee and J. B. Jones, J. Am. Chem. Soc., 118, 502 (1996); c) V. Martichonok and J. B. Jones, J. Am. Chem. Soc., 118, 950 (1996); d) T. Ke, C. R. Wescott, and A. M. Klibanov, J. Am. Chem. Soc., 118, 3366 (1996).
83. For other approaches to understand the factors determining the stereoselectivity of hydrolytic enzymes, see: a) M. Norin, K. Huit, A. Mattson, and T. Norin, Biocatalysis, 7, 131 (1993); b) T. Lee and J. B. Jones, J. Am. Chem. Soc., 118, 502 (1996); c) V. Martichonok and J. B. Jones, J. Am. Chem. Soc., 118, 950 (1996); d) T. Ke, C. R. Wescott, and A. M. Klibanov, J. Am. Chem. Soc., 118, 3366 (1996).
84. For other approaches to understand the factors determining the stereoselectivity of hydrolytic enzymes, see: a) M. Norin, K. Huit, A. Mattson, and T. Norin, Biocatalysis, 7, 131 (1993); b) T. Lee and J. B. Jones, J. Am. Chem. Soc., 118, 502 (1996); c) V. Martichonok and J. B. Jones, J. Am. Chem. Soc., 118, 950 (1996); d) T. Ke, C. R. Wescott, and A. M. Klibanov, J. Am. Chem. Soc., 118, 3366 (1996).