Highly selective synthesis of <scp>d</scp>-amino acids from readily available <scp>l</scp>-amino acids by a one-pot biocatalytic stereoinversion cascade

Zhang, Danping; Jing, Xiaoran; Zhang, Wenli; Nie, Yao; Xu, Yan

doi:10.1039/c9ra06301c

Cited by 26 publications

(43 citation statements)

References 47 publications

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“…The plasmid pET-21b-MBP and the PmLAAD gene from P. mirabilis (GenBank accession no. EU669819.1) were stored in our laboratory [2,4]. The enzymes, oligonucleotides, and other reagents for DNA cloning and amplification were obtained from the Takara-Bio Co., Kawasaki, Japan and the Novagen Co., Madison, WI, USA.…”

Section: Methodsmentioning

confidence: 99%

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Active Expression of Membrane-Bound L-Amino Acid Deaminase from Proteus mirabilis in Recombinant Escherichia coli by Fusion with Maltose-Binding Protein for Enhanced Catalytic Performance

et al. 2020

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L-amino acid deaminases (LAADs) are membrane flavoenzymes that catalyze the deamination of neutral and aromatic L-amino acids to α-keto acids and ammonia. LAADs can be used to develop many important biotechnological applications. However, the transmembrane α-helix of LAADs restricts its soluble active expression and purification from a heterologous host, such as Escherichia coli. Herein, through fusion with the maltose-binding protein (MBP) tag, the recombinant E. coli BL21 (DE3)/pET-21b-MBP-PmLAAD was constructed and the LAAD from Proteus mirabilis (PmLAAD) was actively expressed as a soluble protein. After purification, the purified MBP-PmLAAD was obtained. Then, the catalytic activity of the MBP-PmLAAD fusion protein was determined and compared with the non-fused PmLAAD. After fusion with the MBP-tag, the catalytic efficiency of the MBP-PmLAAD cell lysate was much higher than that of the membrane-bound PmLAAD whole cells. The soluble MBP-PmLAAD cell lysate catalyzed the conversion of 100 mM L-phenylalanine (L-Phe) to phenylpyruvic acid (PPA) with a 100% yield in 6 h. Therefore, the fusion of the MBP-tag not only improved the soluble expression of the PmLAAD membrane-bound protein, but also increased its catalytic performance.

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Section: Methodsmentioning

confidence: 99%

“…L-amino acid deaminases (LAADs; EC 1.4.3.2) belong to a family of amino acid dehydrogenases that catalyze the formation of α-keto acid from L-amino acid and release ammonium and H 2 O as well [1][2][3][4]. LAADs have been identified in several bacterial genera including Proteus, Providencia, and Morganella [2,5].…”

Section: Introductionmentioning

confidence: 99%

Active Expression of Membrane-Bound L-Amino Acid Deaminase from Proteus mirabilis in Recombinant Escherichia coli by Fusion with Maltose-Binding Protein for Enhanced Catalytic Performance

et al. 2020

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“…From the operational point of view, high concentrations of ammonia are needed when using the reductive amination reaction, whereas the oxidative reaction yields α-keto acids when starting from amino acid substrates. Whereas most AADHs are L-enantioselective, D-AADHs (EC 1.4.99.1) have also been described (Vedha-Peters et al, 2006;De Wildeman et al, 2007;Hall and Bommarius, 2011;Li et al, 2012;Au et al, 2016;Akita et al, 2018;Zhang et al, 2019). This family of enzymes is greatly diverse, although in general, AADHs are promiscuous enzymes showing a high enantioselectivity (Xue et al, 2018).…”

Section: Amino Acid Dehydrogenase-based Mecsmentioning

confidence: 99%

“…More than 15 different enantioenriched and enantiopure D-α-AAS -including several Dphenylalanine derivatives-have been produced coupling a "real" L-AAD to engineered enantioselective meso-diaminopimelate dehydrogenase and a cofactor-recycling system (conversions from 45.3 to >99%, e.e. values ranging 52.1 to >99%; Figure 6B, Parmeggiani et al, 2016;Zhang et al, 2019). Racemic mixtures might be used as well as pure L-AAs, turning it into a more efficient and cheaper system.…”

Section: Amino Acid Dehydrogenase-based Mecsmentioning

confidence: 99%

“…L -AAD, WT or (engineered enantioselective meso-diaminopimelate dehydrogenase (DAPDH) and a cofactor-recycling system (e.g., FDH or GDH) were applied. Selected examples were extracted from Parmeggiani et al (2016) (left) and Zhang et al (2019) (right). (C) Conversion of L -methionine into L -ABA using immobilized L -methioninase (AfMETase) together with glutamate dehydrogenase (GluDH) on polyacrylamide and chitosan ( El-Sayed et al, 2015 ).…”

Section: Multienzymatic Cascades For the Production Of Ncaasmentioning

confidence: 99%

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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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Practical Multienzymatic Transformations: Combining Enzymes for the One‐pot Synthesis of Organic Molecules in a Straightforward Manner

Albarrán-Velo

González‐Granda

López-Agudo

et al. 2021

Biocatalysis for Practitioners

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Highly selective synthesis of d-amino acids from readily available l-amino acids by a one-pot biocatalytic stereoinversion cascade

Abstract: An efficient one-pot biocatalytic cascade was developed for synthesis of d-amino acids from readily available l-amino acids via stereoinversion.

Cited by 26 publications

References 47 publications

Active Expression of Membrane-Bound L-Amino Acid Deaminase from Proteus mirabilis in Recombinant Escherichia coli by Fusion with Maltose-Binding Protein for Enhanced Catalytic Performance

Active Expression of Membrane-Bound L-Amino Acid Deaminase from Proteus mirabilis in Recombinant Escherichia coli by Fusion with Maltose-Binding Protein for Enhanced Catalytic Performance

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

Practical Multienzymatic Transformations: Combining Enzymes for the One‐pot Synthesis of Organic Molecules in a Straightforward Manner

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