Biocatalytic Enantioselective Oxidative CC Coupling by Aerobic CH Activation

Schrittwieser, Joerg H.; Resch, Verena; Sattler, Johann H.; Lienhart, Wolf‐Dieter; Durchschein, Katharina; Winkler, Andreas; Gruber, Karl; Macheroux, Peter; Kroutil, Wolfgang

doi:10.1002/anie.201006268

Cited by 74 publications

(48 citation statements)

References 63 publications

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“…It enabled working at solvent concentrations of 70% v/v and substrate concentrations of 20 g/L (Resch et al 2011). Thus, a set of racemic 1-substituted tetrahydroisoquinolines was synthesised starting from the corresponding N-phenylmethylamines and phenylacetic acid derivatives and subjected to reticuline oxidase-catalysed resolutions (Schrittwieser et al 2011a). These oxidase-mediated conversions yielded optically pure products products.…”

Section: Flavoprotein Oxidases In Biotechnologymentioning

confidence: 99%

Flavoprotein oxidases: classification and applications

Dijkman

Gonzalo

Mattevi

et al. 2013

Appl Microbiol Biotechnol

127

106

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This review provides an overview of oxidases that utilise a flavin cofactor for catalysis. This class of oxidative flavoenzymes has shown to harbour a large number of biotechnologically interesting enzymes. Applications range from their use as biocatalysts for the synthesis of pharmaceutical compounds to the integration in biosensors. Through the recent developments in genome sequencing, the number of newly discovered oxidases is steadily growing. Recent progress in the field of flavoprotein oxidase discovery and the obtained biochemical knowledge on these enzymes are reviewed. Except for a structure-based classification of known flavoprotein oxidases, also their potential in recent biotechnological applications is discussed.

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Section: Flavoprotein Oxidases In Biotechnologymentioning

confidence: 99%

Flavoprotein oxidases: classification and applications

Dijkman

Gonzalo

Mattevi

et al. 2013

Appl Microbiol Biotechnol

127

106

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“…2 Enzymes offer highly sustainable and efficient synthetic alternatives to current existing chemical methods, 3 providing access to enantiopure amines and derivatives with excellent selectivity. 4 Traditionally, hydrolases have been the biocatalysts of choice for the preparation of optically active amines through classical or dynamic kinetic resolutions of the corresponding racemates, 5 but the development of other classes of enzymes such as amine oxidases, 6 transaminases, 7 berberine bridge enzymes, 8 amine dehydrogenases 9 and more recently imine reductases 10 presents biotransformations as versatile tools for the development of highly efficient asymmetric transformations to prepare these compounds.…”

Section: Introductionmentioning

confidence: 99%

Biocatalytic Transamination for the Asymmetric Synthesis of Pyridylalkylamines. Structural and Activity Features in the Reactivity of Transaminases

et al. 2016

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ABSTRACT. A set of transaminases has been investigated for the biocatalytic amination of 1-(4-chloropyridin-2-yl)alkan-1-ones. The influence of the chain length of the n-1-alkanone at the C-2 position of the pyridine has been studied in the reaction with different (R)-and (S)-selective transaminases. Thus, enantiopure amines were isolated with high purity starting from a wide selection of prochiral ketones. On the one hand excellent yields (97->99% conversion, up to 93% isolated yield) and stereoselectivity values (>99% ee for both amine enantiomers) were found for n-1-alkanone linear short chain substituents such as ethanone or propanone. On the other hand, more hindered substrates were accepted only when using evolved enzymes such as an evolved variant of (R)-Arthrobacter (ArRmut11-TA). An initial common structural feature was the presence of a chlorine atom on the C-4 position of the pyridine core, which was found to increase the reactivity of the starting ketone, giving extra versatility for the introduction of other chemical functionalities towards more complex and applicable organic molecules. In order to gain a deeper understanding about the substrate specificity of different transaminases, additional structural features were considered by variation of the acetyl group position on the pyridine ring and the use of related acetophenone derivatives.

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“…Only recently the substrate scope of BBE was studied, being suitable for the KR of these types of substrates. [119] The deracemization of a series of benzylisoquinolines was achieved by simultaneous cyclic deracemization using the MAO/borane system coupled to a kinetic oxidative resolution catalyzed by BBE (Scheme 19). This three-step approach led to conversions up to 97% and excellent enantiopurities (ee >97%) into the (S)-berbines.…”

Section: Scheme 17mentioning

confidence: 99%

Why Leave a Job Half Done? Recent Progress in Enzymatic Deracemizations

Díaz‐Rodríguez¹,

Lavandera

Gotor³

2015

CGC

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Abstract. In recent years the usefulness of enzymatic systems to obtain a single stereoisomerically pure compound starting from a racemate has been expanded. Moreover, current advances in protein engineering, molecular biology and modeling tools are the basis to improve the catalytic properties of enzymes to face novel synthetic challenges. Also, medium engineering and novel immobilization methods of (bio)catalysts are enhancing the productivity of biocatalytic processes making them suitable for being scalable. The development of multienzymatic protocols and the combination of enzymes with other catalysts are providing a wide range of synthetic possibilities that are expanding the scope of these transformations even at industrial scale. Herein we will describe an overview of recent (chemo)enzymatic deracemizations, focusing on the strategy employed (dynamic kinetic resolution, stereoinversion, cyclic deracemization or enantioconvergent process), the type of substrate (e.g., alcohols, amines, carboxylic acid derivatives or carbonylic compounds), and the biocatalyst(s) used.

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Biocatalytic Enantioselective Oxidative CC Coupling by Aerobic CH Activation

Cited by 74 publications

References 63 publications

Flavoprotein oxidases: classification and applications

Flavoprotein oxidases: classification and applications

Biocatalytic Transamination for the Asymmetric Synthesis of Pyridylalkylamines. Structural and Activity Features in the Reactivity of Transaminases

Why Leave a Job Half Done? Recent Progress in Enzymatic Deracemizations

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