One‐Pot Cascade Biotransformation for Efficient Synthesis of Benzyl Alcohol and Its Analogs

Liu, Lijun; Yingguo, Zhu; Chen, Yu-Fen; Chen, Huiyu; Fan, Cong; Mo, Qiwen; Yuan, Jifeng

doi:10.1002/asia.201901680

Cited by 29 publications

(24 citation statements)

References 41 publications

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“…When the recombinant E. coli was fed with 5 mM of m ‐f‐DL‐phenylalanine as substrate, 2.54 mM m ‐fluorobenzylamine was obtained (Figure 2b), whereas m ‐fluoro‐D‐phenylalanine remained nearly unreacted during the biotransformation process (Figure S3). LAAD from P. mirabilis predominantly catalyzes the deamination of L‐amino acids [22] and it has been used for resolving the racemic mixture of D and L‐amino acids [21] . Current observations also suggested that LAAD is a good candidate for resolving the racemic mixture of nonnatural amino acids.…”

Section: Resultsmentioning

confidence: 99%

“…As shown from Figure 2a and Figure S2 Figure S3). LAAD from P. mirabilis predominantly catalyzes the deamination of L-amino acids [22] and it has been used for resolving the racemic mixture of D and L-amino acids. [21] Current observations also suggested that LAAD is a good candidate for resolving the racemic mixture of nonnatural amino acids.…”

Section: Synthesis Of Benzylamine Analogues Via One-pot Whole-cell Bimentioning

confidence: 99%

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One‐Pot Synthesis of Aromatic Amines from Renewable Feedstocks via Whole‐Cell Biocatalysis

et al. 2020

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Green and sustainable synthesis of chemicals using biocatalysis is emerging as an alternative to the traditional chemical methods. Here, we reported the establishment of two artificial enzymatic cascades for the synthesis of benzylamine, 2‐phenylethylamine and their analogues from renewable feedstocks via whole‐cell biocatalysis approach. A five‐step enzymatic cascade containing L‐amino acid deaminase (LAAD), hydroxymandelate synthase (HmaS), (S)‐mandelate dehydrogenase (SMDH), benzoylformate decarboxylase (BFD) and ω‐transaminase (ω‐TA) was developed to produce benzylamine from L‐phenylalanine. We also obtained p‐hydroxybenzylamine and m‐fluorobenzylamine with >98 % conversion from L‐tyrosine and m‐fluoro‐phenylalanine. In addition, a three‐step enzymatic cascade comprising LAAD, α‐keto acid decarboxylase (KDC) and ω‐TA was designed for the synthesis of 2‐phenylethylamine, tyramine and m‐fluorophenylethylamine. In summary, we have developed one‐pot whole‐cell biocatalysis system for benzylamine and 2‐phenylethylamine synthesis, which might be amendable for synthesizing other amine compounds in a green and sustainable manner.

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Section: Resultsmentioning

confidence: 99%

Section: Synthesis Of Benzylamine Analogues Via One-pot Whole-cell Bimentioning

confidence: 99%

One‐Pot Synthesis of Aromatic Amines from Renewable Feedstocks via Whole‐Cell Biocatalysis

et al. 2020

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“…Recently, PmLAAD has been expressed together with two additional enzymes in an artificial enzyme cascade in E. coli with the aim to produce benzyl alcohol analogs. This approach demonstrated the ability of PmLAAD to produce optically pure D-m-fluoro-phenylalanine from the corresponding racemic mixture [58]. In addition, a 4-point variant of this enzyme has been exploited to produce D-phenylalanine, exhibiting a conversion of 49.5% after 7 h [59].…”

Section: Production Of D-amino Acids By Enantioselective Deamination/deracemization Using L-amino Acid Deaminasementioning

confidence: 99%

Advances in Enzymatic Synthesis of D-Amino Acids

Pollegioni¹,

Rosini²,

Molla³

2020

IJMS

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In nature, the D-enantiomers of amino acids (D-AAs) are not used for protein synthesis and during evolution acquired specific and relevant physiological functions in different organisms. This is the reason for the surge in interest and investigations on these “unnatural” molecules observed in recent years. D-AAs are increasingly used as building blocks to produce pharmaceuticals and fine chemicals. In past years, a number of methods have been devised to produce D-AAs based on enantioselective enzymes. With the aim to increase the D-AA derivatives generated, to improve the intrinsic atomic economy and cost-effectiveness, and to generate processes at low environmental impact, recent studies focused on identification, engineering and application of enzymes in novel biocatalytic processes. The aim of this review is to report the advances in synthesis of D-AAs gathered in the past few years based on five main classes of enzymes. These enzymes have been combined and thus applied to multi-enzymatic processes representing in vitro pathways of alternative/exchangeable enzymes that allow the generation of an artificial metabolism for D-AAs synthetic purposes.

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“…Moreover, ortho and meta fluorinated mandelic acids were also synthesized in the same method (Yields = 37 ± 0.4% and 47 ± 1.8%). Also starting from substrate fluoro- l -phenylalanine, fluoro-benzyl alcohol was successfully synthesized in a multi-enzymatic system of five enzymes, including LAAD, HMS, l -mandelate dehydrogenase (LMDH), benzoylformate decarboxylase (BFD), and phenylacetaldehyde reductase (PAR) (Yield = 633.17 mg/L) (Figure S11 ) (Liu et al 2020 ).…”

Section: Enzymatic Synthesis Of Fluorinated Compoundsmentioning

confidence: 99%

Enzymatic synthesis of fluorinated compounds

Cheng

2021

Appl Microbiol Biotechnol

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Fluorinated compounds are widely used in the fields of molecular imaging, pharmaceuticals, and materials. Fluorinated natural products in nature are rare, and the introduction of fluorine atoms into organic compound molecules can give these compounds new functions and make them have better performance. Therefore, the synthesis of fluorides has attracted more and more attention from biologists and chemists. Even so, achieving selective fluorination is still a huge challenge under mild conditions. In this review, the research progress of enzymatic synthesis of fluorinated compounds is summarized since 2015, including cytochrome P450 enzymes, aldolases, fluoroacetyl coenzyme A thioesterases, lipases, transaminases, reductive aminases, purine nucleoside phosphorylases, polyketide synthases, fluoroacetate dehalogenases, tyrosine phenol-lyases, glycosidases, fluorinases, and multienzyme system. Of all enzyme-catalyzed synthesis methods, the direct formation of the C-F bond by fluorinase is the most effective and promising method. The structure and catalytic mechanism of fluorinase are introduced to understand fluorobiochemistry. Furthermore, the distribution, applications, and future development trends of fluorinated compounds are also outlined. Hopefully, this review will help researchers to understand the significance of enzymatic methods for the synthesis of fluorinated compounds and find or create excellent fluoride synthase in future research. Key points • Fluorinated compounds are distributed in plants and microorganisms, and are used in imaging, medicine, materials science . • Enzyme catalysis is essential for the synthesis of fluorinated compounds . • The loop structure of fluorinase is the key to forming the C-F bond . Supplementary Information The online version contains supplementary material available at 10.1007/s00253-021-11608-0.

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One‐Pot Cascade Biotransformation for Efficient Synthesis of Benzyl Alcohol and Its Analogs

Cited by 29 publications

References 41 publications

One‐Pot Synthesis of Aromatic Amines from Renewable Feedstocks via Whole‐Cell Biocatalysis

One‐Pot Synthesis of Aromatic Amines from Renewable Feedstocks via Whole‐Cell Biocatalysis

Advances in Enzymatic Synthesis of D-Amino Acids

Enzymatic synthesis of fluorinated compounds

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