Synthesis of enantiopure l-(5-phenylfuran-2-yl)alanines by a sequential multienzyme process

Bencze, László Csaba; Komjáti, Balázs; Pop, Laura; Paizs, Csaba; Irimie, Florin Dan; Nagy, József; Poppe, László; Toşa, Monica Ioana

doi:10.1016/j.tetasy.2015.08.004

Cited by 4 publications

(8 citation statements)

References 28 publications

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“…A chemoenzymatic approach taking advantage of lipase and acylase I has been used for the production of enantiopure L -α-NcAAs starting from N -acetyl-α-AAs ( Podea et al, 2008 ; Bencze et al, 2015 ). However, it is important to highlight that acylase I alone allows deracemization of these compounds, without the need of the lipase mediated DKR.…”

Section: Multienzymatic Cascades For the Production Of Ncaasmentioning

confidence: 99%

Overview on Multienzymatic Cascades for the Production of Non-canonical α-Amino Acids

Martínez‐Rodríguez

Torres

Sánchez

et al. 2020

Front. Bioeng. Biotechnol.

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The 22 genetically encoded amino acids (AAs) present in proteins (the 20 standard AAs together with selenocysteine and pyrrolysine), are commonly referred as proteinogenic AAs in the literature due to their appearance in ribosome-synthetized polypeptides. Beyond the borders of this key set of compounds, the rest of AAs are generally named imprecisely as non-proteinogenic AAs, even when they can also appear in polypeptide chains as a result of post-transductional machinery. Besides their importance as metabolites in life, many of D-α-and L-α-"non-canonical" amino acids (NcAAs) are of interest in the biotechnological and biomedical fields. They have found numerous applications in the discovery of new medicines and antibiotics, drug synthesis, cosmetic, and nutritional compounds, or in the improvement of protein and peptide pharmaceuticals. In addition to the numerous studies dealing with the asymmetric synthesis of NcAAs, many different enzymatic pathways have been reported in the literature allowing for the biosynthesis of NcAAs. Due to the huge heterogeneity of this group of molecules, this review is devoted to provide an overview on different established multienzymatic cascades for the production of non-canonical D-α-and L-α-AAs, supplying neophyte and experienced professionals in this field with different illustrative examples in the literature. Whereas the discovery of new or newly designed enzymes is of great interest, dusting off previous enzymatic methodologies by a "back and to the future" strategy might accelerate the implementation of new or improved multienzymatic cascades.

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Section: Multienzymatic Cascades For the Production Of Ncaasmentioning

confidence: 99%

Overview on Multienzymatic Cascades for the Production of Non-canonical α-Amino Acids

Martínez‐Rodríguez

Torres

Sánchez

et al. 2020

Front. Bioeng. Biotechnol.

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“…[23] Recently, L-(5-phenylfuran-2-yl)-α-alanines were also synthesized by a sequential multienzyme process. [24] In this work, we disclose our results on the lipase-catalyzed resolution of several new, exotically substituted phenylfuranbased -amino esters (rac-3a-d), by applying enantioselective hydrolysis. The real challenge to overcome has been the low solubility of substrates in organic solvents.…”

Section: Introductionmentioning

confidence: 98%

“…We have already described highly stereoselective, lipase‐ or baker's yeast‐mediated procedures for the kinetic resolution of racemic 1‐(5‐phenylfuran‐2‐yl)ethanols, ethane‐1,2‐diols, and ethanones . Recently, l ‐(5‐phenylfuran‐2‐yl)‐α‐alanines were also synthesized by a sequential multienzyme process …”

Section: Introductionmentioning

confidence: 99%

Covalently Immobilized Lipases are Efficient Stereoselective Catalysts for the Kinetic Resolution of rac‐(5‐Phenylfuran‐2‐yl)‐β‐alanine Ethyl Ester Hydrochlorides

Nagy

Galla

Bencze³

et al. 2017

Eur J Org Chem

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Lipase‐catalyzed enzymatic resolution of several new, exotic and variously substituted rac‐(5‐phenylfuran‐2‐yl)‐β‐alanine ethyl esters was investigated. Given the structural instability of unsubstituted rac‐(5‐phenylfuran‐2‐yl)‐β‐alanine ethyl ester, we used the stable hydrochloride salt of this rac‐heteroaryl‐3‐aminopropanoic acid ethyl ester as potential substrate to increase the scope of the reaction. Optimization experiments revealed an efficient procedure for both analytical‐ and preparative‐scale (S)‐selective hydrolysis of several racemic β‐amino ester hydrochlorides in NH4OAc buffer (20 mm, pH 5.8) at 30 °C. Enzymatic resolutions were performed with covalently bound lipase AK from Pseudomonas fluorescens and lipase PS from Burkholderia cepacia on Immobead T2‐150 as catalyst. Seven out of eight new resolution products were successfully isolated and appropriately characterized.

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“…The enzymatic DKR of oxazolones was successfully employed for the synthesis of various alanine derivatives [9,10,11,12,13,14]. The oxazolones, due to the low p Ka of the C-4 proton and their inherent reactivity towards lipase-catalysed alcoholysis [9], are excellent substrates for the DKR reaction (Scheme 1).…”

Section: Introductionmentioning

confidence: 99%

“…If the spontaneous racemisation is faster than the enzymatic alcoholysis, there is no need to use racemisation agents as in the case of the chemoenzymatic procedures developed for the synthesis of benzofuranyl and benzotiophenyl alanines [13]. However, in case of the recently-reported DKR of phenylfuranyl derivatives, the enzymatic reactions showed higher velocity than the substrate racemisation, forcing the use of triethylamine as racemisation agent, which decreased the enzyme selectivity [14]. In order to alleviate the selectivity decrease caused by the racemisation agent, herein we describe the use of single-walled carbon nanotubes (SWCNT)-bound diethylaminoethanol in the lipase-catalysed dynamic kinetic resolution of the arylthiazole-based oxazolones.…”

Section: Introductionmentioning

confidence: 99%

Heterocycles 36. Single-Walled Carbon Nanotubes-Bound N,N-Diethyl Ethanolamine as Mild and Efficient Racemisation Agent in the Enzymatic DKR of 2-Arylthiazol-4-yl-alanines

et al. 2015

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Abstract:In this paper we describe the chemoenzymatic synthesis of enantiopure L-2-arylthiazol-4-yl alanines starting from their racemic N-acetyl derivatives; by combining the lipase-catalysed dynamic kinetic resolution of oxazol-5(4H)-ones with a chemical and an enzymatic enantioselective hydrolytic step affording the desired products in good yields (74%-78%) and high enantiopurities (ee > 99%). The developed procedure exploits the utility of the single-walled carbon nanotubes-bound diethylaminoethanol as mild and efficient racemisation agent for the dynamic kinetic resolution of the corresponding oxazolones.

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Synthesis of enantiopure l-(5-phenylfuran-2-yl)alanines by a sequential multienzyme process

Cited by 4 publications

References 28 publications

Overview on Multienzymatic Cascades for the Production of Non-canonical α-Amino Acids

Overview on Multienzymatic Cascades for the Production of Non-canonical α-Amino Acids

Covalently Immobilized Lipases are Efficient Stereoselective Catalysts for the Kinetic Resolution of rac‐(5‐Phenylfuran‐2‐yl)‐β‐alanine Ethyl Ester Hydrochlorides

Heterocycles 36. Single-Walled Carbon Nanotubes-Bound N,N-Diethyl Ethanolamine as Mild and Efficient Racemisation Agent in the Enzymatic DKR of 2-Arylthiazol-4-yl-alanines

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