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Volumn 2, Issue , 2012, Pages

Protease-catalysed direct asymmetric mannich reaction in organic solvent

Author keywords

[No Author keywords available]

Indexed keywords

ACETONITRILE; ACETONITRILE DERIVATIVE; MANNICH BASE; PRONASE; SOLVENT;

EID: 84868296507     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep00761     Document Type: Article
Times cited : (50)

References (25)
  • 2
  • 3
    • 0017272554 scopus 로고
    • Enzyme recruitment in evolution of new function
    • Jensen, R. A. Enzyme recruitment in evolution of new function. Ann. Rev. Microbiol. 30, 409-425 (1976).
    • (1976) Ann. Rev. Microbiol. , vol.30 , pp. 409-425
    • Jensen, R.A.1
  • 4
    • 0033117461 scopus 로고    scopus 로고
    • Catalytic promiscuity and the evolution of new enzymatic activities
    • DOI 10.1016/S1074-5521(99)80033-7
    • O'Brien, P. J. D. & Herschlag, D. Catalytic promiscuity and the evolution of new enzymatic activities. Chem. Biol. 6, R91-R105 (1999). (Pubitemid 29368405)
    • (1999) Chemistry and Biology , vol.6 , Issue.4
    • O'Brien, P.J.1    Herschlag, D.2
  • 5
    • 33748525883 scopus 로고    scopus 로고
    • Enzyme promiscuity: Evolutionary and mechanistic aspects
    • DOI 10.1016/j.cbpa.2006.08.011, PII S1367593106001189, Analytical Techniques/Mechanisms
    • Khersonsky, O., Roodveldt, C. & Tawfik, D. S. Enzyme promiscuity: evolutionary and mechanistic aspects. Curr. Opin. Chem. Biol. 10, 498-508 (2006). (Pubitemid 44375065)
    • (2006) Current Opinion in Chemical Biology , vol.10 , Issue.5 , pp. 498-508
    • Khersonsky, O.1    Roodveldt, C.2    Tawfik, D.S.3
  • 7
    • 77953623874 scopus 로고    scopus 로고
    • Enzyme promiscuity: A mechanistic and evolutionary perspective
    • Khersonsky, O. & Tawfik, D. S. Enzyme promiscuity: a mechanistic and evolutionary perspective. Annu. Rev. Biochem. 79, 471-505 (2010).
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 471-505
    • Khersonsky, O.1    Tawfik, D.S.2
  • 8
    • 0037396292 scopus 로고    scopus 로고
    • Enzymes with extra talents: Moonlighting functions and catalytic promiscuity
    • DOI 10.1016/S1367-5931(03)00032-2
    • Copley, S. D. Enzymes with extra talents: moonlighting functions and catalytic promiscuity. Curr. Opin. Chem. Biol. 7, 265-272 (2003). (Pubitemid 36514958)
    • (2003) Current Opinion in Chemical Biology , vol.7 , Issue.2 , pp. 265-272
    • Copley, S.D.1
  • 9
    • 59849106371 scopus 로고    scopus 로고
    • Protein promiscuity and its implications for biotechnology
    • Nobeli, I., Favia, A. D. & Thornton, J. M. Protein promiscuity and its implications for biotechnology. Nat. Biotechnol. 27, 157-167 (2009).
    • (2009) Nat. Biotechnol. , vol.27 , pp. 157-167
    • Nobeli, I.1    Favia, A.D.2    Thornton, J.M.3
  • 10
    • 77958046500 scopus 로고    scopus 로고
    • Hydrolases: Catalytically promiscuous enzymes for non-conventional reactions in organic synthesis
    • Busto, E., Gotor-Fernandez, V. & Gotor, V. Hydrolases: catalytically promiscuous enzymes for non-conventional reactions in organic synthesis. Chem. Soc. Rev. 39, 4504-4523 (2010).
    • (2010) Chem. Soc. Rev. , vol.39 , pp. 4504-4523
    • Busto, E.1    Gotor-Fernandez, V.2    Gotor, V.3
  • 11
    • 44649139781 scopus 로고    scopus 로고
    • Biocatalytic promiscuity: The first lipase-catalysed asymmetric aldol reaction
    • DOI 10.1039/b803406k
    • Li, C., Feng, X.-W., Wang, N., Zhou, Y.-J. & Yu, X.-Q. Biocatalytic promiscuity: The first lipase-catalysed asymmetric aldol reaction. Green Chem 10, 616-618 (2008). (Pubitemid 351782878)
    • (2008) Green Chemistry , vol.10 , Issue.6 , pp. 616-618
    • Li, C.1    Feng, X.-W.2    Wang, N.3    Zhou, Y.-J.4    Yu, X.-Q.5
  • 12
    • 78651310908 scopus 로고    scopus 로고
    • Nuclease p1: A new biocatalyst for direct asymmetric aldol reaction under solvent-free conditions
    • Li, H.-H., He, Y.-H., Yuan, Y. & Zhi, G. Nuclease p1: a new biocatalyst for direct asymmetric aldol reaction under solvent-free conditions. Green Chem 13, 185-189 (2011).
    • (2011) Green Chem , vol.13 , pp. 185-189
    • Li, H.-H.1    He, Y.-H.2    Yuan, Y.3    Zhi, G.4
  • 13
    • 78651397152 scopus 로고    scopus 로고
    • The lipase-catalyzed asymmetric C-C Michael addition
    • Cai, J.-F., Guan, Z. & He, Y.-H. The lipase-catalyzed asymmetric C-C Michael addition. J. Mol. Catal. B: Enzym. 68, 240-244 (2011).
    • (2011) J. Mol. Catal. B: Enzym. , vol.68 , pp. 240-244
    • Cai, J.-F.1    Guan, Z.2    He, Y.-H.3
  • 14
    • 0027460684 scopus 로고
    • Chemoenzymatic synthesis of the C-13 side chain of taxol: Optically-Active 3-hydroxy-4-phenyl β-lactam derivatives
    • Brieva, R., Crich, J. Z. & Sih, C. J. Chemoenzymic synthesis of the C-13 side chain of taxol: optically active 3-hydroxy-4-phenyl.beta.-lactam derivatives. J. Org. Chem. 58, 1068-1075 (1993). (Pubitemid 23121436)
    • (1993) Journal of Organic Chemistry , vol.58 , Issue.5 , pp. 1068-1075
    • Brieva, R.1    Crich, J.Z.2    Sih, C.J.3
  • 15
    • 79959992526 scopus 로고    scopus 로고
    • Racemase activity of B. cepacia lipase leads to dual-function asymmetric dynamic kinetic resolution of a-Aminonitriles
    • Vongvilai, P. et al. Racemase activity of B. cepacia lipase leads to dual-function asymmetric dynamic kinetic resolution of a-Aminonitriles. Angew. Chem. Int. Ed. 50, 6592-6595 (2011).
    • (2011) Angew. Chem. Int. Ed. , vol.50 , pp. 6592-6595
    • Vongvilai, P.1
  • 16
    • 67649404699 scopus 로고    scopus 로고
    • Exploration of chiral induction on epoxides in lipase-catalyzed epoxidation of alkenes using (2R, 3S, 4R, 5S)-(-)-2, 3:4, 6-di-O- isopropylidiene-2-keto-L-gulonic acid monohydrate
    • Sarma, K., Goswami, A. & Goswami, B. C. Exploration of chiral induction on epoxides in lipase-catalyzed epoxidation of alkenes using (2R, 3S, 4R, 5S)-(-)-2, 3:4, 6-di-O-isopropylidiene-2-keto-L-gulonic acid monohydrate. Tetrahedron: Asymmetry 20, 1295-1300 (2009).
    • (2009) Tetrahedron: Asymmetry , vol.20 , pp. 1295-1300
    • Sarma, K.1    Goswami, A.2    Goswami, B.C.3
  • 17
    • 67649114374 scopus 로고    scopus 로고
    • Lipase-catalysed direct Mannich reaction in water: Utilization of biocatalytic promiscuity for C-C bond formation in a "one-pot" synthesis
    • Li, K. et al. Lipase-catalysed direct Mannich reaction in water: utilization of biocatalytic promiscuity for C-C bond formation in a "one-pot" synthesis. Green Chem. 11, 777-779 (2009).
    • (2009) Green Chem. , vol.11 , pp. 777-779
    • Li, K.1
  • 18
    • 78049268909 scopus 로고    scopus 로고
    • Utilization of biocatalytic promiscuity for direct Mannich reaction
    • He, T. et al. Utilization of biocatalytic promiscuity for direct Mannich reaction. J. Mol. Catal. B: Enzym. 67, 189-194 (2010).
    • (2010) J. Mol. Catal. B: Enzym. , vol.67 , pp. 189-194
    • He, T.1
  • 19
    • 78549255263 scopus 로고    scopus 로고
    • A novel trypsin-catalyzed three-component Mannich reaction
    • Chai, S.-J., Lai, Y.-F., Zheng, H. & Zhang, P.-F. A novel trypsin-catalyzed three-component Mannich reaction. Helv. Chim. Acta 93, 2231-2236 (2010).
    • (2010) Helv. Chim. Acta , vol.93 , pp. 2231-2236
    • Chai, S.-J.1    Lai, Y.-F.2    Zheng, H.3    Zhang, P.-F.4
  • 20
    • 80052806973 scopus 로고    scopus 로고
    • Use of protease from Bacillus licheniformis as promiscuous catalyst for organic synthesis: Applications in C-C and C-N bond formation reactions
    • López-Iglesias, M., Busto, E., Gotor, V. & Gotor-Fernández, V. Use of protease from Bacillus licheniformis as promiscuous catalyst for organic synthesis: applications in C-C and C-N bond formation reactions. Adv. Synth. Catal. 353, 2345-2353 (2011).
    • (2011) Adv. Synth. Catal. , vol.353 , pp. 2345-2353
    • López-Iglesias, M.1    Busto, E.2    Gotor, V.3    Gotor-Fernández, V.4
  • 22
    • 0029592705 scopus 로고
    • The Candida antarctica lipase B catalysed kinetic resolution of seudenol in non-Aqueous media of controlled water activity
    • DOI 10.1016/0957-4166(95)00399-1
    • Orrenius, C., Norin, T., Hult, K. & Carrea, G. The Candida antarctica lipase B catalysed kinetic resolution of seudenol in non-Aqueous media of controlled water activity. Tetrahedron: Asymmetry 6, 3023-3030 (1995). (Pubitemid 26022199)
    • (1995) Tetrahedron Asymmetry , vol.6 , Issue.12 , pp. 3023-3030
    • Orrenius, C.1    Norin, T.2    Hult, K.3    Carrea, G.4
  • 23
    • 0343907203 scopus 로고    scopus 로고
    • Water activity control in enzymatic esterification processes
    • DOI 10.1016/S0141-0229(97)00027-6, PII S0141022997000276
    • Wehtje, E., Kaur, J., Adlercreutz, P., Chand, S. & Mattiasson, B. Water activity control in enzymatic esterification processes. Enzyme Microb. Technol. 21, 502-510 (1997). (Pubitemid 27489046)
    • (1997) Enzyme and Microbial Technology , vol.21 , Issue.7 , pp. 502-510
    • Wehtje, E.1    Kaur, J.2    Adlercreutz, P.3    Chand, S.4    Mattiasson, B.5
  • 24
    • 0033180037 scopus 로고    scopus 로고
    • Hydroxynitrile lyase-catalyzed synthesis of cyanohydrins in organic solvents Parameters influencing activity and enantiospecificity
    • DOI 10.1016/S0141-0229(99)00055-1, PII S0141022999000551
    • Costes, D., Wehtje, E. & Adlercreutz, P. Hydroxynitrile lyase-catalyzed synthesis of cyanohydrins in organic solvents: Parameters influencing activity and enantiospecificity. Enzyme Microb. Technol. 25, 384-391 (1999). (Pubitemid 29364339)
    • (1999) Enzyme and Microbial Technology , vol.25 , Issue.3-5 , pp. 384-391
    • Costes, D.1    Wehtje, E.2    Adlercreutz, P.3
  • 25
    • 67849103981 scopus 로고    scopus 로고
    • Active-site motions and polarity enhance catalytic turnover of hydrated subtilisin dissolved in organic solvents
    • Hudson, E. P. et al. Active-site motions and polarity enhance catalytic turnover of hydrated subtilisin dissolved in organic solvents. J. Am. Chem. Soc. 131, 4294-4300 (2009).
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 4294-4300
    • Hudson, E.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.