Terminal Alkenes from Acrylic Acid Derivatives via Non‐Oxidative Enzymatic Decarboxylation by Ferulic Acid Decarboxylases

Aleku, Godwin A.; Prause, Christoph; Bradshaw-Allen, Ruth T.; Plasch, Katharina; Glueck, Silvia M.; Bailey, Susan; Payne, K.A.P.; Parker, David; Faber, Kurt; Leys, D.

doi:10.1002/cctc.201800643

Cited by 36 publications

(42 citation statements)

References 71 publications

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“…S15 b). The lower signal intensities obtained for the TAL-activity measurements, in comparison with the PAL-assay using l -Phe, might reflect the reported decreased catalytic efficiency of Sc FDC1within the decarboxylation of p -coumaric acid 43 , 57 , the product of the TAL-activity. However, ferulic acid decarboxylase of bacterial origin, e.g.…”

Section: Resultsmentioning

confidence: 90%

Fluorescent enzyme-coupled activity assay for phenylalanine ammonia-lyases

Moisă

Amariei

Nagy

et al. 2020

Sci Rep

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Phenylalanine ammonia-lyases (PALs) catalyse the non-oxidative deamination of l-phenylalanine to trans-cinnamic acid, while in the presence of high ammonia concentration the reverse reaction occurs. PALs have been intensively studied, however, their industrial applications for amino acids synthesis remained limited, mainly due to their decreased operational stability or limited substrate specificity. The application of extensive directed evolution procedures to improve their stability, activity or selectivity, is hindered by the lack of reliable activity assays allowing facile screening of PAL-activity within large-sized mutant libraries. Herein, we describe the development of an enzyme-coupled fluorescent assay applicable for PAL-activity screens at whole cell level, involving decarboxylation of trans-cinnamic acid (the product of the PAL reaction) by ferulic acid decarboxylase (FDC1) and a photochemical reaction of the produced styrene with a diaryltetrazole, that generates a detectable, fluorescent pyrazoline product. The general applicability of the fluorescent assay for PALs of different origin, as well as its versatility for the detection of tyrosine ammonia-lyase (TAL) activity have been also demonstrated. Accordingly, the developed procedure provides a facile tool for the efficient activity screens of large mutant libraries of PALs in presence of non-natural substrates of interest, being essential for the substrate-specificity modifications/tailoring of PALs through directed evolution-based protein engineering.

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Section: Resultsmentioning

confidence: 90%

Fluorescent enzyme-coupled activity assay for phenylalanine ammonia-lyases

Moisă

Amariei

Nagy

et al. 2020

Sci Rep

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“…The calculated energy profile for the carboxylation of para-vinylphenol to cinnamic acid suggests that the nucleophilic β-carbon atom of the vinyl-group attacks a CO 2 molecule rather than HCO 3 − . CO 2 is proposed to form through protonation of HCO 3 − by Glu 64, causing H 2 CO 3 decomposition to CO 2 and H 2 O. Ferulic acid decarboxylase enzyme (FDC) is currently used to promote decarboxylation reactions of a wide range of acrylic acid derivatives, yielding terminal alkenes with a conversion up to 99% [91].…”

Section: Para-hydroxystyrenes β-Carboxylation By Phenolic Acid Decarbmentioning

confidence: 99%

Carboxylation of Hydroxyaromatic Compounds with HCO3− by Enzyme Catalysis: Recent Advances Open the Perspective for Valorization of Lignin-Derived Aromatics

Tommasi

2019

Catalysts

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This review focuses on recent advances in the field of enzymatic carboxylation reactions of hydroxyaromatic compounds using HCO3− (as a CO2 source) to produce hydroxybenzoic and other phenolic acids in mild conditions with high selectivity and moderate to excellent yield. Nature offers an extensive portfolio of enzymes catalysing reversible decarboxylation of hydroxyaromatic acids, whose equilibrium can be pushed towards the side of the carboxylated products. Extensive structural and mutagenesis studies have allowed recent advances in the understanding of the reaction mechanism of decarboxylase enzymes, ultimately enabling an improved yield and expansion of the scope of the reaction. The topic is of particular relevance today as the scope of the carboxylation reactions can be extended to include lignin-related compounds in view of developing lignin biorefinery technology.

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“…[14] Furthermore, unlike other cofactor-dependent PADs, these enzymes do not require ap renylated flavin cofactor,w hich typically requires production by coexpression of the flavin prenyltransferase UbiX. [14,15] In a second step of the cascade, the enzymatically produced vinylphenols can then be furtherf unctionalized, for example, by aid of other enzymes, [16] oxidative dimerization [17] or by organometallic coupling reactions [18] as demonstrated here.…”

mentioning

confidence: 94%

3D‐Printed Phenacrylate Decarboxylase Flow Reactors for the Chemoenzymatic Synthesis of 4‐Hydroxystilbene

Peng

Mittmann

Wenger

et al. 2019

Chemistry A European J

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Continuous flow systems for chemical synthesis are becoming a major focus in organic chemistry and there is a growing interest in the integration of biocatalysts due to their high regio‐ and stereoselectivity. Methods established for 3D bioprinting enable the fast and simple production of agarose‐based modules for biocatalytic reactors if thermally stable enzymes are available. We report here on the characterization of four different cofactor‐free phenacrylate decarboxylase enzymes suitable for the production of 4‐vinylphenol and test their applicability for the encapsulation and direct 3D printing of disk‐shaped agarose‐based modules that can be used for compartmentalized flow microreactors. Using the most active and stable phenacrylate decarboxylase from Enterobacter spec. in a setup with four parallel reactors and a subsequent palladium(II) acetate‐catalysed Heck reaction, 4‐hydroxystilbene was synthesized from p‐coumaric acid with a total yield of 14.7 % on a milligram scale. We believe that, due to the convenient direct immobilization of any thermostable enzyme and straightforward tuning of the reaction sequence by stacking of modules with different catalytic activities, this simple process will facilitate the establishment and use of cascade reactions and will therefore be of great advantage for many research approaches.

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Terminal Alkenes from Acrylic Acid Derivatives via Non‐Oxidative Enzymatic Decarboxylation by Ferulic Acid Decarboxylases

Cited by 36 publications

References 71 publications

Fluorescent enzyme-coupled activity assay for phenylalanine ammonia-lyases

Fluorescent enzyme-coupled activity assay for phenylalanine ammonia-lyases

Carboxylation of Hydroxyaromatic Compounds with HCO3− by Enzyme Catalysis: Recent Advances Open the Perspective for Valorization of Lignin-Derived Aromatics

3D‐Printed Phenacrylate Decarboxylase Flow Reactors for the Chemoenzymatic Synthesis of 4‐Hydroxystilbene

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