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Volumn 3, Issue 1, 1999, Pages 11-15

Dynamic kinetic resolution

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL; ENZYME; MANDELATE RACEMASE; METAL;

EID: 0033023975     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(99)80003-9     Document Type: Article
Times cited : (139)

References (19)
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  • 2
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  • 5
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    • Controlled racemisation of optically active organic compounds: Prospects for asymmetric transformation
    • This is an excellent account of racemisation protocols.
    • Ebbers EJ, Ariaans GJA, Houbiers JPM, Bruggink A, Zwanenburg B Controlled racemisation of optically active organic compounds: prospects for asymmetric transformation. Tetrahedron. 53:1997;9417-9476. This is an excellent account of racemisation protocols.
    • (1997) Tetrahedron , vol.53 , pp. 9417-9476
    • Ebbers, E.J.1    Ariaans, G.J.A.2    Houbiers, J.P.M.3    Bruggink, A.4    Zwanenburg, B.5
  • 6
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    • Production of R-(-)-mandelic acid from manelonitrile by Alcaligenes faecalis ATCC-8750
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  • 7
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    • Lipase-catalysed kinetic resolution with in situ racemisation one-pot synthesis of optically active cyanohydrin acetates from aldehydes
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  • 8
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    • One-pot synthesis of optically active cyanohydrin acetates from aldehydes via lipase-catalysed kinetic resolution coupled with in situ formation and racemisation of cyanohydrins
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  • 9
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    • Enzymes and transition metal complexes in tandem-a new concept for dynamic kinetic resolution
    • This paper highlights the tandem use of transition metals as a new concept in dynamic kinetic resolution.
    • Stürmer R Enzymes and transition metal complexes in tandem-a new concept for dynamic kinetic resolution. Angew Chem Int Ed Engl. 36:1997;1173-1174. This paper highlights the tandem use of transition metals as a new concept in dynamic kinetic resolution.
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    • Stürmer, R.1
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    • Lipase-catalysed dynamic kinetic resolution of chiral amines: Use of palladium as the racemization catalyst
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  • 12
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    • Enymatic resolution of alcohols coupled with ruthenium-catalysed racemisation of the substrate alcohol
    • This is a good example of this racemisation protocol.
    • Larsson ALE, Persson BA, Bäckvall J-E Enymatic resolution of alcohols coupled with ruthenium-catalysed racemisation of the substrate alcohol. Angew Chem Int Ed Engl. 36:1997;1211-1212. This is a good example of this racemisation protocol.
    • (1997) Angew Chem Int Ed Engl , vol.36 , pp. 1211-1212
    • Larsson, A.L.E.1    Persson, B.A.2    Bäckvall, J.-E.3
  • 15
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    • Synthesis of homochiral L-(S)-tert-leucine via a lipase catalysed dynamic resolution process
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    • Dynamic enzymatic resolution of thioesters
    • This is an excellent comprehensive study.
    • Um P-J, Drueckhammer DG Dynamic enzymatic resolution of thioesters. J Am Chem SoC. 120:1998;5605-5610. This is an excellent comprehensive study.
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  • 18
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    • Production of ring-substituted D-phenylglycines by Microbial or enzymatic hydroysis/deracemisation of the corresponding DL-hydantoins
    • This paper demonstrates the use of dynamic kinetic resolution in the synthesis of desirable synthons.
    • Garcia MJ, Azerad R Production of ring-substituted D-phenylglycines by Microbial or enzymatic hydroysis/deracemisation of the corresponding DL-hydantoins. Tetrahedron - Asymmetry. 8:1997;85-92. This paper demonstrates the use of dynamic kinetic resolution in the synthesis of desirable synthons.
    • (1997) Tetrahedron - Asymmetry , vol.8 , pp. 85-92
    • Garcia, M.J.1    Azerad, R.2
  • 19
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    • Large-scale production of Mandelate racemase by Pseudomonas putida ATCC 12633: Optimization of enzyme induction and development of a stable crude enzyme preparation
    • This paper highlights the use of enzymes as racemising agents.
    • Stecher H, Felfer U, Faber K Large-scale production of Mandelate racemase by Pseudomonas putida ATCC 12633: optimization of enzyme induction and development of a stable crude enzyme preparation. J Biotechnol. 56:1997;33-40. This paper highlights the use of enzymes as racemising agents.
    • (1997) J Biotechnol , vol.56 , pp. 33-40
    • Stecher, H.1    Felfer, U.2    Faber, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.