Conversion of γ- and δ-Keto Esters into Optically Active Lactams. Transaminases in Cascade Processes

Advanced Synthesis and Catalysis

Volumn 360, Issue 4, 2018, Pages 686-695

  Mourelle Insua, Ángela ^a   Zampieri, Luiz Arthur ^a,b   Lavandera, Iván ^a   Gotor Fernández, Vicente ^a  

^a UNIVERSITY OF OVIEDO   (Spain)

^b FEDERAL UNIVERSITY OF CEARÁ   (Brazil)

Author keywords

Cascade reaction; Intramolecular cyclisation; Lactams; Stereoselective synthesis; Transaminase

Indexed keywords

EID: 85042134075     PISSN: 16154150     EISSN: 16154169     Source Type: Journal    
DOI: 10.1002/adsc.201701304     Document Type: Article

References (31)

1. M. A. Ogliaruso, J. F. Wolfe, Synthesis of Lactones and Lactams, John Wiley & Sons, Inc., West Sussex, 1993.
2. C. R. Pitts, T. Lectka, Chem. Rev. 2014, 114, 7930–7953;
3. G. S. Singh, S. Sudheesh, Arkivoc 2014, i, 227–385;
4. Y. Kumar, P. Singh, G. Bhargava, RSC Adv. 2016, 6, 99220–99250.
5. L.-W. Ye, C. Shu, F. Gagosz, Org. Biomol. Chem. 2014, 12, 1833–1845;
6. J. Caruano, G. G. Muccioli, R. Robiette, Org. Biomol. Chem. 2016, 14, 10134–10156.
7. J. Albarrán-Velo, D. González-Martínez, V. Gotor-Fernández, Biocatal. Biotransform. 2018, 36, 102–130.
8. E. Busto, V. Gotor-Fernández, V. Gotor, Chem. Rev. 2011, 111, 3998–4035.
9. See, for instance:
10. A. L. Gutman, E. Meyer, X. Yue, C. Abell, Tetrahedron Lett. 1992, 33, 3943–3946;
11. E. Stavila, K. Loos, Tetrahedron Lett. 2013, 54, 370–372;
12. C.-J. Aurell, S. Karlsson, F. Pontén, S. M. Andersen, Org. Process Res. Dev. 2014, 18, 1116–1119.
13. D. Koszelewski, D. Clay, K. Faber, W. Kroutil, J. Mol. Catal. B: Enzym. 2009, 60, 191–194;
14. M. D. Truppo, J. D. Rozzell, N. J. Turner, Org. Process Res. Dev. 2010, 14, 234–237;
15. C. K. Chung, P. G. Bulger, B. Kosjek, K. M. Belyk, N. Rivera, M. E. Scott, G. R. Humphrey, J. Limanto, D. C. Bachert, K. M. Emerson, Org. Process Res. Dev. 2014, 18, 215–227.
16. G. A. Aleku, S. P. France, H. Man, J. Mangas-Sanchez, S. L. Montgomery, M. Sharma, F. Leipold, S. Hussain, G. Grogan, N. J. Turner, Nat. Chem. 2017, 9, 961–969.
17. A. S. Touchy, S. M. A. Hakim Siddiki, K. Kon, K.-i. Shimizu, ACS Catal. 2014, 4, 3045–3050;
18. J. D. Vidal, M. J. Climent, P. Concepcion, A. Corma, S. Iborra, M. J. Sabater, ACS Catal. 2015, 5, 5812–5821.
19. C. E. Paul, M. Rodríguez-Mata, E. Busto, I. Lavandera, V. Gotor-Fernández, V. Gotor, S. García-Cerrada, J. Mendiola, O. De Frutos, I. Collado, Org. Process Res. Dev. 2014, 18, 788–792.
20. U. Kaulman, K. Smithies, M. E. B. Smith, H. C. Hailes, J. M. Ward, Enzyme Microb. Technol. 2007, 41, 628–637.
21. S. Pannuri, S. V. Kamat, A. R. M. Garcia, WO 2006/063336A2 20060615, Cambrex North Brunswick Inc., 2006.
22. Y. Yamada, A. Iwasaki, N. Kizaki, K. Matsumoto, Y. Ikenaka, M. Ogura, J. Hasegawa, (Kaneka Corporation), PCT Int. Appl. WO 9848030A1 19981029, 1998;
23. A. Iwasaki, Y. Yamada, N. Kizaki, Y. Ikenaka, J. Hasegawa, Appl. Microbiol. Biotechnol. 2006, 69, 499–505;
24. F. G. Mutti, C. S. Fuchs, D. Pressnitz, J. H. Sattler, W. Kroutil, Adv. Synth. Catal. 2011, 353, 3227–3233.
25. C. K. Savile, J. M. Janey, E. M. Mundorff, J. C. Moore, S. Tam, W. R. Jarvis, J. C. Colbeck, A. Krebber, F. J. Fleitz, J. Brands, P. N. Devine, G. W. Huisman, G. J. Georges, Science 2010, 329, 305–309.
26. F. Guo, P. Berglund, Green Chem. 2017, 19, 333–360.
27. 25=−21.3 (c=0.9, water) for the (S)-enantiomer. J. M. García, M. A. Maestro, M. Oiarbide, J. M. Odriozola, J. Razkin, C. Palomo, Org. Lett. 2009, 11, 3826–3829.
28. 2) for the (R)-enantiomer. M. Amat, N. Llor, J. Hidalgo, C. Escolano, J. Bosch, J. Org. Chem. 2003, 68, 1919–1928.
29. 2) for the (R)-enantiomer. M. N. Cheemala, P. Knochel, Org. Lett. 2007, 9, 3089–3092.
30. 2) for the (R)-enantiomer. D. Guijarro, O. Pablo, M. Yus, J. Org. Chem. 2013, 78, 3647–3654.
31. 3) for the (S)-enantiomer. R. Sallio, S. Lebrun, F. Agbossou-Niedercorn, C. Michon, E. Deniau, Tetrahedron: Asymmetry 2012, 23, 998–1004.