Esterase catalysed enantioselective ring closure

Abstract

Porcine liver esterase catalyses the reaction of γ-amino esters in water to give a mixture of the corresponding γ-lactam and the hydrolysis product, deacylation of the acyl enzyme intermediate by ring closure occurs with a high enantioselectivity giving an ee of 90% for the formation of (S)-5-phenyl-2-pyrrolidone from racemic ethyl 4-phenyl-4-aminobutanoate.

References

1. M. I. Page and A. Williams, Organic and BioOrganic Mechanisms, Longmans, London, 1997.
2. P. Barton, A. P. Laws and M. I. Page, J. Chem. Soc., Perkin Trans. 2, 1994, 2021.
3. A. C. Satterthwaite and W. P. Jencks, J. Am. Chem. Soc., 1974, 96, 7018.
4. Y. Pocker and E. Green, J. Am. Chem. Soc., 1976, 98, 6197.
5. A. J. Kirby, T. G. Mujahid and P. Camilleri, J. Chem. Soc., Perkin Trans. 2, 1979, 1610; T. C. Bruice and S. J. Benkovic, J. Am. Chem. Soc., 1963, 85, 1.
6. A. L. Gutman, E. Meyer, X. Yue and C. Abell, Tetrahedron Lett., 1992, 33, 3493.
7. S. Takayama, S. T. Lee, S.-C. Hung and C.-H. Wong, Chem. Commun., 1999, 127.
8. D. Farb and W. P. Jencks, Arch. Biochem. Biophys., 1980, 203, 227.
9. P. Barton and M. I. Page, J. Chem. Soc., Perkin Trans. 2, 1993, 2317.
10. P. Barton and M. I. Page, Tetrahedron, 1992, 47, 7731.