Kinetic Resolution of 3-Fluoroalanine Using a Fusion Protein of<scp>D</scp>-Amino Acid Oxidase with<i>Vitroscilla</i>Hemoglobin

Seo, Young-Man; Khang, Yong‐Ho; Yun, Hyungdon

doi:10.1271/bbb.110122

Cited by 8 publications

(4 citation statements)

References 17 publications

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“…These α-fluoroalkyl α-amino acids motifs can be found in various domains, such as enzyme inhibitors or bioactive small molecules. The most known example is the use of fluorinated amino acids as potential irreversible inhibitors of pyridoxal phosphate (PLP)-dependent enzymes such as decarboxylases, transaminases, and racemases [ 83 , 84 , 85 ]. For instance, β,β,β-trifluoroalanine is a well-known suicide substrate of PLP-dependent enzymes [ 83 , 86 , 87 , 88 ] ( Scheme 45 ).…”

Section: Applicationsmentioning

confidence: 99%

Asymmetric α-Fluoroalkyl-α-Amino Acids: Recent Advances in Their Synthesis and Applications

Picois,

Boutahri,

Milbeo

et al. 2024

Molecules

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Due to the specific properties provided by fluorine atoms to biomolecules, amino acids with fluorinated side chains are of great interest for medicinal chemistry and chemical biology. Among them, α-fluoroalkyl-α-amino acids constitute a unique class of compounds. In this review, we outline the strategies adopted for their syntheses in enantiopure or enantioenriched forms and their incorporation into peptides. We then describe the consequences of the introduction of fluorine atoms in these compounds for the modulation of their hydrophobicity and the control of their conformation. Emerging applications are presented in the areas of enzyme inhibition, medicinal chemistry, hydrolytic stability of peptides, antimicrobial peptides, PET, and 19F NMR probes.

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Section: Applicationsmentioning

confidence: 99%

Asymmetric α-Fluoroalkyl-α-Amino Acids: Recent Advances in Their Synthesis and Applications

Picois,

Boutahri,

Milbeo

et al. 2024

Molecules

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“…Gox belongs to the group of oxidases, a subclass of oxidoreductases that require molecular oxygen for their catalytic process. Several studies have focused on the role of VHb in enhancing the catalytic activity of various oxidases (Khang et al 2003;Liu et al 2021;Seo et al 2011;Wang et al 2022). Previous research demonstrated that fusing VHb with d-amino acid oxidases (DAOs) from Rhodotorula gracilis or Trigonopsis variabilis significantly improved the catalytic efficiency of DAOs in synthesizing 7-aminocephalosporanic acid (Khang et al 2003;Ma et al 2009;Seo et al 2011).…”

Section: Introductionmentioning

confidence: 99%

“…Several studies have focused on the role of VHb in enhancing the catalytic activity of various oxidases (Khang et al 2003;Liu et al 2021;Seo et al 2011;Wang et al 2022). Previous research demonstrated that fusing VHb with d-amino acid oxidases (DAOs) from Rhodotorula gracilis or Trigonopsis variabilis significantly improved the catalytic efficiency of DAOs in synthesizing 7-aminocephalosporanic acid (Khang et al 2003;Ma et al 2009;Seo et al 2011). In a recent study by Wang et al (2022), the effect of VHb on the catalytic efficiency of five oxidases, including DAO from T. variabilis (TvDAO), Gox, alcohol oxidase from Pichia pastoris (AOX), p-hydroxymandelate synthase from Amycolatopsis orientalis (AoHMS), and l-glutamate oxidase (LGOX), was systematically investigated.…”

Section: Introductionmentioning

confidence: 99%

Improving glucose oxidase catalysis in Aspergillus niger via Vitreoscilla hemoglobin fusion protein

Liu,

Zhang,

Liang

et al. 2024

Appl Microbiol Biotechnol

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Oxygen is crucial for converting glucose to gluconic acid catalyzed by glucose oxidase (Gox). However, industrial gluconic acid production faces oxygen supply limitations. To enhance Gox efficiency, Vitreoscilla hemoglobin (VHb) has been considered as an efficient oxygen transfer carrier. This study identified GoxA, a specific isoform of Gox in the industrial gluconic acid-producing strain of Aspergillus niger. Various forms of VHb expression in A. niger were tested to improve GoxA's catalytic efficiency. Surprisingly, the expression of free VHb, both intracellularly and extracellularly, did not promote gluconic acid production during shake flask fermentation. Then, five fusion proteins were constructed by linking Gox and VHb using various methods. Among these, VHb-GS1-GoxA, where VHb's C-terminus connected to GoxA's N-terminus via the flexible linker GS1, demonstrated a significantly higher Kcat/Km value (96% higher) than GoxA. Unfortunately, the expression of VHb-GS1-GoxA in A. niger was limited, resulting in a low gluconic acid production of 3.0 g/L. To overcome the low expression problem, single-and dual-strain systems were designed with tools of SpyCatcher/SpyTag and Snoop-Catcher/SnoopTag. In these systems, Gox and VHb were separately expressed and then self-assembled into complex proteins. Impressively, the single-strain system outperformed the GoxA overexpression strain S1971, resulting in 23% and 9% higher gluconic acid production under 0.6 vvm and 1.2 vvm aeration conditions in the bioreactor fermentation, respectively. The successful construction of Gox and VHb fusion or complex proteins, as proposed in this study, presents promising approaches to enhance Gox catalytic efficiency and lower aerodynamic costs in gluconic acid production.

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“…One unit of BCAT was defined as the amount of enzyme catalyzing the formation of 1 µmol of L-tert-leucine per minute in 100 mM phosphate buffer (pH 7.5) containing 10 mM trimethylpyruvate and 10 mM Glu at 37 o C. The specific activity of the purified BCAT was 7.8 U/mg. Chiral analysis of tert-leucine was performed using a C 18 Symmetry column (Waters, MA, USA) with a Waters HPLC system at 254 nm after the derivatization of the sample with 3,4,6-tetra-O-acetyl-β-D-glucopyranosyl isothiocyanate (GITC) [11]. Separation of each enantiomer was achieved through an isocratic elution with a mixture of 50% methanol and 50% water (0.1% TFA) at a flow rate of 1.0 ml/min.…”

mentioning

confidence: 99%

Enzymatic Synthesis of L-tert-Leucine with Branched Chain Aminotransferase

Seo

Yun²

2011

J. Microbiol. Biotechnol.

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In this study, we demonstrated the asymmetric synthesis of L-tert-leucine from trimethylpyruvate using branchedchain aminotransferase (BCAT) from Escherichia coli in the presence of L-glutamate as an amino donor. Since BCAT was severely inhibited by 2-ketoglutarate, in order to overcome this here, we developed a BCAT/aspartate aminotransferase (AspAT) and BCAT/AspAT/pyruvate decarboxylase (PDC) coupling reaction. In the BCAT/ AspAT/PDC coupling reaction, 89.2 mM L-tert-leucine (ee >99%) was asymmetrically synthesized from 100 mM trimethylpyruvate.

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Kinetic Resolution of 3-Fluoroalanine Using a Fusion Protein ofD-Amino Acid Oxidase withVitroscillaHemoglobin

Cited by 8 publications

References 17 publications

Asymmetric α-Fluoroalkyl-α-Amino Acids: Recent Advances in Their Synthesis and Applications

Asymmetric α-Fluoroalkyl-α-Amino Acids: Recent Advances in Their Synthesis and Applications

Improving glucose oxidase catalysis in Aspergillus niger via Vitreoscilla hemoglobin fusion protein

Enzymatic Synthesis of L-tert-Leucine with Branched Chain Aminotransferase

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