Thiamine‐Diphosphate‐Dependent Enzymes as Catalytic Tools for the Asymmetric Benzoin‐Type Reaction

Giovannini, Pier Paolo; Bortolini, Olga; Massi, Alessandro

doi:10.1002/ejoc.201600228

Cited by 35 publications

(22 citation statements)

References 128 publications

(163 reference statements)

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“…The resulting constructs were confirmed by DNA sequencing, restricted with NdeI and XhoI, and the coding gene was ligated into the corresponding sites of pET-28a vector (Merck Millipore, Amsterdam, The Netherlands), introducing a (His) 6 -tag at the N-terminus of budC gene product.…”

Section: Construction Of Pet-28a Budc Expression Vectormentioning

confidence: 99%

“…2 To date all chemical approaches [3][4][5] and most of the biochemical approaches [6][7][8] only allow the formation of one of the two chiral products: either the α-hydroxy ketones or vicinal diols. A particular challenge is the development of methodologies allowing for the targeted selective synthesis of both α-hydroxy ketones and vicinal diols, in particular with aliphatic side chains (Scheme 1).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Assessing the stereoselectivity of Serratia marcescens CECT 977 2,3-butanediol dehydrogenase

Médici

Stammes

Kwakernaak

et al. 2017

Catal. Sci. Technol.

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α-Hydroxy ketones and vicinal diols constitute well-known building blocks in organic synthesis. Here we describe one enzyme that enables the enantioselective synthesis of both building blocks starting from diketones. The enzyme 2,3-butanediol dehydrogenase (BudC) from S. marcescens CECT 977 belongs to the NADH-dependent metal-independent short-chain dehydrogenases/reductases family (SDR) and catalyses the selective asymmetric reductions of prochiral α-diketones to the corresponding α-hydroxy ketones and diols. BudC is highly active towards structurally diverse diketones in combination with nicotinamide cofactor regeneration systems. Aliphatic diketones, cyclic diketones and alkyl phenyl diketones are well accepted, whereas their derivatives possessing two bulky groups are not converted. In the reverse reaction vicinal diols are preferred over other substrates with hydroxy/keto groups in non-vicinal positions.

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Section: Construction Of Pet-28a Budc Expression Vectormentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Assessing the stereoselectivity of Serratia marcescens CECT 977 2,3-butanediol dehydrogenase

Médici

Stammes

Kwakernaak

et al. 2017

Catal. Sci. Technol.

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“…These encouraging results prompted us to investigate the activity of Ao:DCPIP OR in benzoin‐type reactions between donor 1 and various aliphatic aldehydes 7 as acceptors (Scheme , route c). In fact, apart from acetoin, which represents a case study,, few other α ‐hydroxy ketones of type 8 (Scheme , route c) have been produced exploiting the ThDP‐dependent enzyme pyruvate decarboxylase (PDC). Furthermore, the conversion levels were low and, for most products, the enantiomeric excess ( ee ) was not determined…”

Section: Resultsmentioning

confidence: 99%

Enzymatic Cross‐Benzoin‐Type Condensation of Aliphatic Aldehydes: Enantioselective Synthesis of 1‐Alkyl‐1‐hydroxypropan‐2‐ones and 1‐Alkyl‐1‐hydroxybutan‐2‐ones

et al. 2018

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Benzoin-type reactions have been intensively exploited as a synthetic strategy for the preparation of a-hydroxy ketones. Thiamine diphosphate (ThDP) dependent enzymes are excellent catalysts for asymmetric versions of such reaction types. In particular, in cross-benzoin condensations of aromatic reactants and mixed aromatic/aliphatic reactions, use of these enzymes has resulted in high levels of chemo-, regio-and stereoselectivity. The present work, which confirms this trend for aliphatic reactants, outlines results obtained in the formal cross-benzoin-type condensation of the 'umpoled' acetaldehyde and propionaldehyde with various aliphatic aldehydes catalyzed by the ThDP-dependent enzyme acetoin:dichlorophenolindophenol oxidoreductase (Ao:DCPIP OR). In these reactions, 3-hydroxy-3-methylbutan-2-one (methylacetoin) was used as the activated acetaldehyde donor, while 4-hydroxy-4-methylhexan-3-one was employed for the first time as the precursor of activated propionaldehyde. With the exception of 3hydroxypentan-2-one and 3-hydroxyhexan-2-one, which were obtained in almost racemic form by the condensation of methylacetoin with propanal and butanal, respectively, all other products achieved from reactions performed using the same donor with more hindered aldehyde acceptors were obtained with high conversions (89-99%) and in good to high enantiomeric excess (72-99% ee). In a similar way, high conversions (75-99%) and good ee (76-99%) were observed in reactions performed with the same set of aldehyde acceptors, but using 4-hydroxy-4-methylhexan-3-one as propionyl anion donor. This is the first time that most of the products described herein have been prepared via benzoin-type condensation.

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“…R-configured benzoin adducts are usually obtained by BAL-catalyzed reactions. [16] Them ajor stereochemical outcome was thus unbiased by the structure of these connected dibenzaldehyde substrates. [17] In summary,weuncovered the unprecedented capacity of BALt oc atalyze intramolecular asymmetric benzoin reactions.T his discovery was accomplished by using aromatic aldehyde derivatives connected by al inker chain.…”

Section: Angewandte Chemiementioning

confidence: 99%

Intramolecular Benzoin Reaction Catalyzed by Benzaldehyde Lyase from Pseudomonas Fluorescens Biovar I

Hernández

Parella

Petrillo³

et al. 2017

Angew Chem Int Ed

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Intramolecular benzoin reactions catalyzed by benzaldehyde lyase from Pseudomonas fluorescens biovar I (BAL) are reported. The structure of the substrates envisaged for this reaction consists of two benzaldehyde derivatives linked by an alkyl chain. The structural requirements needed to achieve the intramolecular carbon-carbon bond reaction catalyzed by BAL were established. Thus, a linker consisting of a linear alkyl chain of three carbon atoms connected through ether-type bonds to the 2 and 2' positions of two benzaldehyde moieties, which could be substituted with either Cl, Br, or OCH at either the 3 and 3' or 5 and 5' positions, were suitable substrates for BAL. Reactions with 61-84 % yields of the intramolecular product and ee values between 64 and 98 %, were achieved.

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Thiamine‐Diphosphate‐Dependent Enzymes as Catalytic Tools for the Asymmetric Benzoin‐Type Reaction

Cited by 35 publications

References 128 publications

Assessing the stereoselectivity of Serratia marcescens CECT 977 2,3-butanediol dehydrogenase

Assessing the stereoselectivity of Serratia marcescens CECT 977 2,3-butanediol dehydrogenase

Enzymatic Cross‐Benzoin‐Type Condensation of Aliphatic Aldehydes: Enantioselective Synthesis of 1‐Alkyl‐1‐hydroxypropan‐2‐ones and 1‐Alkyl‐1‐hydroxybutan‐2‐ones

Intramolecular Benzoin Reaction Catalyzed by Benzaldehyde Lyase from Pseudomonas Fluorescens Biovar I

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