Asymmetric synthesis of aromatic β‐amino acids using ω‐transaminase: Optimizing the lipase concentration to obtain thermodynamically unstable β‐keto acids

Mathew, Sam; Jeong, Sang Seom; Chung, Taeowan; Lee, Sang‐Hyeup; Yun, Hyungdon

doi:10.1002/biot.201500181

Cited by 37 publications

(26 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Organic syntheses by ω-TAs may suffer from unfavorable reaction equilibrium due to insufficient amount of amino donor [16]. To maximize the productivity of ω-TAs, shifting the equilibrium to the product using higher concentration of amino donor is extremely important [22]. Previously, while synthesizing ω-AmDDA from ω-OHDDA using AlkJ and Sp ω-TA, we found benzylamine (BA) as the best amino donor [10].…”

Section: Production Of ω-Ohdda Using Artssp450smentioning

confidence: 99%

Biosynthesis of Nylon 12 Monomer, ω-Aminododecanoic Acid Using Artificial Self-Sufficient P450, AlkJ and ω-TA

et al. 2018

Self Cite

View full text Add to dashboard Cite

ω-Aminododecanoic acid is considered as one of the potential monomers of Nylon 12, a high-performance member of the bioplastic family. The biosynthesis of ω-aminododecanoic acid from renewable sources is an attractive process in the polymer industry. Here, we constructed three artificial self-sufficient P450s (ArtssP450s) using CYP153A13 from Alcanivorax borkumensis and cytochrome P450 reductase (CPR) domains of natural self-sufficient P450s (CYP102A1, CYP102A5, and 102D1). Among them, artificial self-sufficient P450 (CYP153A13BM3CPR) with CYP102A1 CPR showed the highest catalytically activity for dodecanoic acid (DDA) substrate. This form of ArtssP450 was further co-expressed with ω-TA from Silicobacter pomeroyi and AlkJ from Pseudomonas putida GPo1. This single-cell system was used for the biotransformation of dodecanoic acid (DDA) to ω-aminododecanoic acid (ω-AmDDA), wherein we could successfully biosynthesize 1.48 mM ω-AmDDA from 10 mM DDA substrate in a one-pot reaction. The productivity achieved in the present study was five times higher than that achieved in our previously reported multistep biosynthesis method (0.3 mM).

show abstract

Section: Production Of ω-Ohdda Using Artssp450smentioning

confidence: 99%

Biosynthesis of Nylon 12 Monomer, ω-Aminododecanoic Acid Using Artificial Self-Sufficient P450, AlkJ and ω-TA

et al. 2018

Self Cite

View full text Add to dashboard Cite

show abstract

“…The first step involves the hydrolysis of the ester by a lipase originating from Candida rugosa, followed by the amination of the keto acid by an ω-transaminase (ω-TA) from Polaromonas sp. JS666 (Scheme 12) [65]. scope of the cascade, six different arenes (39a-f) were subjected to the biotransformation, showing large variations in conversion and selectivity.…”

Section: α-And β-Amino Acidsmentioning

confidence: 99%

Section: α-And β-Amino Acidsmentioning

confidence: 99%

Artificial Biocatalytic Linear Cascades to Access Hydroxy Acids, Lactones, and α- and β-Amino Acids

2018

View full text Add to dashboard Cite

α-, β-, and ω-Hydroxy acids, amino acids, and lactones represent common building blocks and intermediates for various target molecules. This review summarizes artificial cascades published during the last 10 years leading to these products. Renewables as well as compounds originating from fossil resources have been employed as starting material. The review provides an inspiration for new cascade designs and may be the basis to design variations of these cascades starting either from alternative substrates or extending them to even more sophisticated products.

show abstract

“…Overall yield and optical purity increased while waste was reduced [7]. The demand of amino acids, especially β-amino acids, as building blocks in bioactive molecules or peptidomimetics is high [10,11]. Kinetic resolution of β-amino acids was performed by Bea et al catalyzed by an ω-transaminase with high ee [9].…”

Section: Introductionmentioning

confidence: 99%

“…Kinetic resolution of β-amino acids was performed by Bea et al catalyzed by an ω-transaminase with high ee [9]. The demand of amino acids, especially β-amino acids, as building blocks in bioactive molecules or peptidomimetics is high [10,11]. For instance, a derivate from (R)-β-phenylalanine ((2R,3S)-N-benzoyl-3-phenylisoserine) is a functional part in the antitumor agent paclitaxel from Taxus brevifolia [12].…”

Section: Introductionmentioning

confidence: 99%

One‐step purification and immobilization of a β‐amino acid aminotransferase using magnetic (M‐PVA) beads

Dold

Cai

Rudat

2016

Engineering in Life Sciences

View full text Add to dashboard Cite

Aminotransferases (ATs) received much attention as biocatalyst in the last decades and are utilized for the synthesis of chiral amines, amino alcohols and amino acids. More recently, enzymatic synthesis of enantiopure β‐amino acids is of increasing interest, for their application in peptidomimetics or other drug related compounds. For economic process management it is of major interest to acquire reusable biocatalysts. This is achievable by immobilization of the enzymes. A wide range of immobilization techniques for ATs exists. Two of the most common procedures are entrapment in sol‐gel or calcium‐alginate and alternatively covalent binding to chitosan support. For these traditional immobilization techniques, high amounts of purified enzyme solutions are required which is cost intensive. A major step toward faster and straightforward immobilization is the insertion of affinity tags, like a His‐tag, to the enzyme coding gene. Immobilization on non‐porous polyvinyl magnetic micro beads functionalized with IDA (iminodiacetic acid) leads to a fast and easy one‐step purification and immobilization of a β‐amino acid AT from Variovorax paradoxus. For loading of the functionalized beads, three divalent metal ions (Ni2+, Co2+ and Cu2+) were tested. The best activity was obtained with Ni2+ and almost no activity was detected after loading the beads with Cu2+. The immobilized AT was successfully tested to synthesize several enantiopure β‐amino acids via kinetic resolution. Further examination and characterization of this immobilized AT showed improved stability compared to the crude cell extract. The immobilized AT revealed enhanced pH and thermal stability compared to the crude cell extract. High activity was preserved up to 38 days of storage at 4°C. Moreover, the use of magnetic beads allows an easy and mild recycling of the immobilized enzyme after the reaction, leading to an efficient reuse of the immobilized enzyme, for at least seven cycles.

show abstract

Asymmetric synthesis of aromatic β‐amino acids using ω‐transaminase: Optimizing the lipase concentration to obtain thermodynamically unstable β‐keto acids

Cited by 37 publications

References 22 publications

Biosynthesis of Nylon 12 Monomer, ω-Aminododecanoic Acid Using Artificial Self-Sufficient P450, AlkJ and ω-TA

Biosynthesis of Nylon 12 Monomer, ω-Aminododecanoic Acid Using Artificial Self-Sufficient P450, AlkJ and ω-TA

Artificial Biocatalytic Linear Cascades to Access Hydroxy Acids, Lactones, and α- and β-Amino Acids

One‐step purification and immobilization of a β‐amino acid aminotransferase using magnetic (M‐PVA) beads

Contact Info

Product

Resources

About