Dynamic kinetic resolution: synthesis of optically active α-amino acid derivatives

Brown, Stuart A.; Parker, Marie Claire; Turner, Nicholas J.

doi:10.1016/s0957-4166(00)00108-7

Cited by 62 publications

(28 citation statements)

References 13 publications

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“…Lipases may also be useful in obtaining optically pure amino acids by catalyzing the enantioselective opening of stereochemically labile racemic precursors, such as azalactones (Limanto et al, 2005;Truppo and Hughes, 2011;Truppo et al, 2008) and oxazolones (Bevinakatti et al, 1990;Brown et al, 2000;Crich et al, 1993;Gu et al, 1992). Truppo and Hughes recently described a method to prepare the enantiopure ester of (S)-γ-fluoroleucine, an intermediate in the synthesis of the drug odanacatibe, from continuous enzymatic alcoholysis of its respective azalactone using CAL-B immobilized in polymethacrylate resin (Truppo and Hughes, 2011).…”

Section: Dynamic Kinetic Resolution Of Amino Acids and Derivativesmentioning

confidence: 98%

Lipases: Valuable catalysts for dynamic kinetic resolutions

Miranda

Souza

2015

Biotechnology Advances

183

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Section: Dynamic Kinetic Resolution Of Amino Acids and Derivativesmentioning

confidence: 98%

Lipases: Valuable catalysts for dynamic kinetic resolutions

Miranda

Souza

2015

Biotechnology Advances

183

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“…Lipases have been used for the rather efficient enzymatic DKR of azlactones [13][14][15][16] (note that no genuine "azlactonase" is known). Seebach et al reported that titanium taddolates, present in stoichiometric or substoichiometric amounts, effect the DKR of azlactones (up to 72 % ee).…”

Section: Dedicated To Professor Günter Helmchenmentioning

confidence: 99%

Highly Efficient Dynamic Kinetic Resolution of Azlactones by Urea‐Based Bifunctional Organocatalysts

et al. 2005

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“…of substrate 80 due to easy racemization of azlactones under conditions of lipase -catalyzed resolution via azlactone ring opening with an alcohol (Scheme 6.31 ) [109,110] . Using this resolution concept, N -benzoyl L -tert -leucine butyl ester, ( S ) -81 , has been synthesized with 94% yield and with 99.5% ee in the presence of a lipase from Mucor miehei .…”

Section: Hydrolysis Of Other Carboxylic Acid Derivatives and Other Fumentioning

confidence: 99%

Enzyme‐Catalyzed Asymmetric Synthesis

Gröger

2010

Catalytic Asymmetric Synthesis

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INTRODUCTIONBiocatalysis has been recognized over the past decades as a highly valuable tool for organic chemists to prepare enantiomerically pure molecules, so -called chiral building blocks, in a highly effi cient way. Besides a multitude of academic work, it is noteworthy that enzyme catalysis belongs to the standard repertoire in industry when facing challenging enantioselective synthetic routes. A broad range of biocatalytic methods is already in use in particular for large -scale manufacture of drug intermediates [1] .The research in the fi eld of enzyme catalysis has already been comprehensively reviewed some years ago [2] . Thus, the focus of the current review is on a selection of (particularly recently developed) enantioselective enzymatic reactions, which turned out to be highly useful and applicable in organic synthesis, fulfi lling criteria such as high productivity, substrate concentrations, conversions, and enantioselectivities. The presented methods are an interesting complementary tool to existing " classic organic " or " chemocatalytic asymmetric " methodologies. Among biocatalytic reactions, both resolution of racemates and asymmetric synthesis starting from prochiral substrates are attractive routes already applied, in part, in industry. A third type of biotechnological approach, which is not a subject of this review, are fermentation processes. A graphical summary of these three types of so -called " white biotechnology " methodologies is given in Scheme 6.1 .Hydrolases are the enzyme class most commonly applied as biocatalysts in organic chemistry. This is mainly due to the accessibility of these enzymes (used, e.g., in the textile and detergents industry), their suitability for transformations in organic media Catalytic Asymmetric Synthesis, Third Edition, Edited by Iwao Ojima 269 270 ENZYME-CATALYZED ASYMMETRIC SYNTHESIS (in particular when using lipases), and the lack of a need for cofactors. However, in recent years, we have also seen an increasing tendency to apply redox enzymes in organic syntheses as well as lyases in C -C bond formations and transferases. Isomerases also turned out to be very useful in particular in combination with hydrolases for dynamic kinetic resolutions. Thus, a broad range of biotransformations is available for organic chemists. A challenge, however, is the use of ATP cofactor -dependent enzymes, which contribute to only a negligible number of typical organic biotransformations (e.g., due to the high price of ATP).The fi eld of biocatalysis benefi ted signifi cantly from the tremendous progress in molecular biology. Highly effi cient methods for screening and optimization of biocatalysts (by, e.g., directed evolution in the latter case) have been developed, which allows access to tailor -made enzymes. Furthermore, the design of recombinant microorganisms gives access to highly productive whole -cell catalysts, which contain only the desired enzymes in large amount, thus signifi cantly reducing the required biomass for biotransformations compared with the use of...

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Dynamic kinetic resolution: synthesis of optically active α-amino acid derivatives

Cited by 62 publications

References 13 publications

Lipases: Valuable catalysts for dynamic kinetic resolutions

Lipases: Valuable catalysts for dynamic kinetic resolutions

Highly Efficient Dynamic Kinetic Resolution of Azlactones by Urea‐Based Bifunctional Organocatalysts

Enzyme‐Catalyzed Asymmetric Synthesis

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