Alteration of the Substrate Specificity of Benzoylformate Decarboxylase from <i>Pseudomonas putida</i> by Directed Evolution

Lingen, Bettina; Kolter-Jung, Doris; Dünkelmann, Pascal; Feldmann, Ralf; Grötzinger, Joachim; Pohl, Martina; Müller, Michael

doi:10.1002/cbic.200200475

Cited by 56 publications

(42 citation statements)

References 47 publications

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“…These advances include the use of enzymes of the type esterase, [29,43] lipase, [44a-b] hydantoinase, [45] epoxide hydrolase, [46] nitrilase, [47] aldolase, [48] monoamine oxidase, [49] Baeyer-Villiger monooxygenase, [50] transaminase, [51] benzoylformate decarboxylase, [52] phosphotriesterase, [53] P450, [54] reductase, [55] oxynitrilase, [56] and horse radish peroxidase. [57] Circular permutation, that is, the intramolecular relocation of the C and N termini of a protein, has been applied to the evolution of enantioselectivity with the lipase Candida antarctica B (CALB).…”

Section: Early Examples Of Directed Evolution Of Enantioselective Enzmentioning

confidence: 99%

Laboratory Evolution of Stereoselective Enzymes: A Prolific Source of Catalysts for Asymmetric Reactions

2010

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Asymmetric catalysis plays a key role in modern synthetic organic chemistry, with synthetic catalysts and enzymes being the two available options. During the latter part of the last century the use of enzymes in organic chemistry and biotechnology experienced a period of rapid growth. However, these biocatalysts have traditionally suffered from several limitations, including in many cases limited substrate scope, poor enantioselectivity, insufficient stability, and sometimes product inhibition. During the last 15 years, the genetic technique of directed evolution has been developed to such an extent that all of these long-standing problems can be addressed and solved. It is based on repeated cycles of gene mutagenesis, expression, and screening (or selection). This Review focuses on the directed evolution of enantioselective enzymes, which constitutes a fundamentally new approach to asymmetric catalysis. Emphasis is placed on the development of methods to make laboratory evolution faster and more efficient, thus providing chemists and biotechnologists with a rich and non-ending source of robust and selective catalysts for a variety of useful applications.

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Section: Early Examples Of Directed Evolution Of Enantioselective Enzmentioning

confidence: 99%

Laboratory Evolution of Stereoselective Enzymes: A Prolific Source of Catalysts for Asymmetric Reactions

2010

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“…[41,42] Während der letzten zehn Jahre haben andere Arbeitskreise mitgeholfen, das Konzept der gerichteten Evolution stereoselektiver Enzyme als Katalysatoren in der synthetischen organischen Chemie zu verallgemeinern unter Verwendung der oben skizzierten Mutagenese-Strategien. Diese Fortschritte schließen Enzyme ein vom Typ Esterase, [29,43] Lipase, [44a,b] Hydantoinase, [45] Epoxidehydrolase, [46] Nitrilase, [47] Aldolase, [48] Monoamin-Oxidase, [49] Baeyer-VilligerMonooxygenase, [50] Transaminase, [51] Benzoylformat-Decarboxylase, [52] Phosphotriesterase, [53] P450, [54] Reduktase, [55] Oxynitrilase [56] und Meerrettich-Peroxidase. [57] Zirkularpermutation, also die intramolekulare Neuplatzierung der Cund N-Termini eines Proteins, wurde zur Erhöhung der Enantioselektivität der Lipase aus Candida antarctica B (CALB) erfolgreich angewendet.…”

Section: Erste Beispiele Für Gerichtete Evolution Enantioselektiver Eunclassified

Gerichtete Evolution stereoselektiver Enzyme: Eine ergiebige Katalysator‐Quelle für asymmetrische Reaktionen

Reetz

2010

Angewandte Chemie

130

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Asymmetrische Katalyse spielt eine Schlüsselrolle in der modernen synthetischen organischen Chemie, wobei künstliche Katalysatoren und Enzyme die zwei wichtigsten Optionen darstellen. Die Verwendung von Enzymen in der organischen Chemie und Biotechnologie hat in der zweiten Hälfte des vergangenen Jahrhunderts stark zugenommen, oft blieb jedoch der Anwendungsbereich aus mehreren Gründen eingeschränkt. Dazu gehören begrenzte Substratakzeptanz, geringe oder fehlende Stereoselektivität, unzureichende Stabilität und manchmal Produktinhibierung. Während der vergangenen 15 Jahre wurde die genetische Technik der gerichteten Evolution so weit entwickelt und verfeinert, dass all diese Probleme angegangen und in der Regel gelöst werden können. Sie basiert auf wiederholende Zyklen von Genmutagenese, Expression und Screening (oder Selektion). Der vorliegende Aufsatz fokussiert auf gerichtete Evolution stereoselektiver Enzyme, ein fundamental neuer Ansatz zur asymmetrischen Katalyse. Der Schwerpunkt liegt auf Methodenentwicklung in dem Bestreben, diese Art der Katalysator‐Optimierung einfacher, schneller und effizienter als in der Vergangenheit zu gestalten. Die neueren Methoden bescheren dem Chemiker und dem Biotechnologen robuste und selektive Katalysatoren für eine Vielzahl von nützlichen Anwendungen.

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“…The limitation for o-substituents was circumvented by the alteration of the substrate specificity of BFD via directed evolution [15]. BFD mutant L476Q and M365-L461S accepted o-substituents even though the mutated residues are not the ones that were directly involved in the binding of an acyl donor.…”

Section: Benzoylformate Decarboxylase (Bfd)mentioning

confidence: 99%

Thiamine Pyrophosphate Dependent Enzyme Catalyzed Reactions: Stereoselective C–C Bond Formations in Water

Demir¹,

Ayhan

Sopacı

2007

CLEAN Soil Air Water

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Enzymes are biodegradable and renewable resources that utilize water as the reaction solvent. Reactions catalyzed by enzymes are among the most effective, selective, and , green' processes available today. The advantages of using biocatalysts include their high degree of regio-and stereo-specificity, versatility, and high reaction rates under mild reaction conditions. Enzyme catalyzed enantioselective C -C bond formation reactions are rather important aspects of synthetic organic chemistry. Thiamine pyrophosphate (TPP) dependent enzymes, especially, have an important role in the stereoselective formation of C -C bonds. This review covers the recent advances in enzyme catalyzed asymmetric C -C bond formation using the most pronounced thiamine pyrophosphate dependent enzymes: acetohydroxyacid synthase, benzaldehyde lyase, benzoylformate decarboxylase, pyruvate decarboxylase, and phenylpyruvate decarboxylase. These enzymes are all capable of acyloin-type condensation reactions in water under mild conditions, in turn leading to chiral a-hydroxy ketones, which are versatile building blocks for the pharmaceutical and chemical industries. IntroductionThe , green chemistry' concept as proposed by P. T. Anastas in 1991 includes the design, development, and application of chemical processes and products in such a way as to avoid substances that are hazardous to human health and the environment [1]. The biocatalytic reactions that employ either enzymes or whole cells are well suited for green chemistry because mild reaction conditions are applied in these reactions by lowering the energy requirements; fewer by-products are formed as they are highly chemo-, regio-, and stereoselective, and multi-step chemical syntheses can be achieved within just a few steps via biocatalysis [1].Optically active a-oxyfunctionalized compounds, in particular, carboxylic acids, aldehydes, and ketones are indispensable building blocks for asymmetric synthesis due to their versatile functional groups, which can be easily transformed to other functionalities, e. g., diols, halo or amino derivatives, and epoxides [2].Of these a-oxyfunctionalized compounds, a-hydroxy ketones (acyloins) are especially important, see Fig. 1. The classical methodology for the synthesis of these compounds involves acyloin and benzoin condensation. The former includes C -C bond formation under reductive conditions while the latter involves C -C bond breaking,

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Alteration of the Substrate Specificity of Benzoylformate Decarboxylase from Pseudomonas putida by Directed Evolution

Cited by 56 publications

References 47 publications

Laboratory Evolution of Stereoselective Enzymes: A Prolific Source of Catalysts for Asymmetric Reactions

Laboratory Evolution of Stereoselective Enzymes: A Prolific Source of Catalysts for Asymmetric Reactions

Gerichtete Evolution stereoselektiver Enzyme: Eine ergiebige Katalysator‐Quelle für asymmetrische Reaktionen

Thiamine Pyrophosphate Dependent Enzyme Catalyzed Reactions: Stereoselective C–C Bond Formations in Water

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