Biosynthesis of the Nylon 12 Monomer, ω‐Aminododecanoic Acid with Novel CYP153A, AlkJ, and ω‐TA Enzymes

Ahsan, Md. Murshidul; Jeon, Hyeongtag; Nadarajan, Sivakumar; Chung, Taeowan; Yoo, Hee-Wang; Kim, Byung‐Gee; Patil, Mahesh D.

doi:10.1002/biot.201700562

Cited by 35 publications

(36 citation statements)

References 52 publications

(101 reference statements)

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“…Thus, whole cells expressing the enzyme of interest for the biosynthetic applications are advantageous [47]. Besides the cost effective and simpler handling of whole-cell biotransformations, an added advantage includes the utility of the enzyme production machinery of the fully functional living organism [48,49]. Also, the implementation of biocatalytic syntheses using whole-cell biotransformations is advantageous regarding the regeneration of the redox cofactors [50].…”

Section: Kinetic Resolution Of Racemic Amines Using E Coli Whole Celmentioning

confidence: 99%

Kinetic Resolution of Racemic Amines to Enantiopure (S)-amines by a Biocatalytic Cascade Employing Amine Dehydrogenase and Alanine Dehydrogenase

et al. 2019

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Amine dehydrogenases (AmDHs) efficiently catalyze the NAD(P)H-dependent asymmetric reductive amination of prochiral carbonyl substrates with high enantioselectivity. AmDH-catalyzed oxidative deamination can also be used for the kinetic resolution of racemic amines to obtain enantiopure amines. In the present study, kinetic resolution was carried out using a coupled-enzyme cascade consisting of AmDH and alanine dehydrogenase (AlaDH). AlaDH efficiently catalyzed the conversion of pyruvate to alanine, thus recycling the nicotinamide cofactors and driving the reaction forward. The ee values obtained for the kinetic resolution of 25 and 50 mM rac-α-methylbenzylamine using the purified enzymatic systems were only 54 and 43%, respectively. The use of whole-cells apparently reduced the substrate/product inhibition, and the use of only 30 and 40 mgDCW/mL of whole-cells co-expressing AmDH and AlaDH efficiently resolved 100 mM of rac-2-aminoheptane and rac-α-methylbenzylamine into the corresponding enantiopure (S)-amines. Furthermore, the applicability of the reaction protocol demonstrated herein was also successfully tested for the efficient kinetic resolution of wide range of racemic amines.

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Section: Kinetic Resolution Of Racemic Amines Using E Coli Whole Celmentioning

confidence: 99%

Kinetic Resolution of Racemic Amines to Enantiopure (S)-amines by a Biocatalytic Cascade Employing Amine Dehydrogenase and Alanine Dehydrogenase

et al. 2019

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“…Furthermore, a surge in demand for enantiopure pharmaceuticals, owing to the regulations imposed by various regulatory agencies, can be addressed using the exquisite mixture of enantio‐, regio‐ and, chemoselectivity displayed by enzymes ,. Enzymes can also be employed in multi‐enzymatic one‐pot cascades which can execute the synthesis of complex compounds from cheaper starting materials, most importantly, avoiding the purification of the intermediates …”

Section: Introductionmentioning

confidence: 99%

Biocatalyzed C−C Bond Formation for the Production of Alkaloids

2018

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Traditional methods of chemical synthesis of alkaloids exhibit various problems such as lack of enantioselectivity, the use of toxic chemical and intermediates, and multiple numbers of synthetic steps. Consequently, various enzymatic methods for the formation of CÀC bonds in the alkaloid skeleton have been developed. Herein, we report advances achieved in the enzymatic or chemo-enzymatic synthesis of pharmaceutically important alkaloids that employ three CÀC bond forming enzymes: two Pictet-Spenglerases and the oxidative CÀC bond forming flavoenzyme Berberine Bridge Enzyme. Protein engi-neering studies, improving the substrate scope of these enzymes, and thereby leading to the synthesis of non-natural alkaloids possessing higher or newer pharmacological activities, are also discussed. Furthermore, the integration of these biocatalysts with other enzymes, in multi-enzymatic cascades for the enantioselective synthesis of alkaloids, is also reviewed. Current results suggest that these enzymes hold great promise for the generation of CÀC bonds in the selective synthesis of alkaloid compounds possessing diverse pharmacological properties.

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“…In particular, long chain ω-hydroxy fatty acids (ω-OHFAs) contain two functional groups-hydroxy and carboxyl groups-at their ends, and they can therefore be further oxidized to fatty aldehydes, dicarboxylic acids, and oxo-fatty acids. Recently, it was reported that dodecanoic acid (DDA) can be efficiently transformed to ω-amino dodecanoic acid (ω-AmDDA) by utilizing different enzymes like Cytochrome P450 monooxygenases, alcohol dehydrogenases (AlkJ), alkane hydroxylase AlkBGT, Baeyer-Villiger monooxygenases (BVMOs), esterases, and ω-transaminases (ω-TAs) [8][9][10]. ω-AmDDA is a very important monomer for the synthesis of Nylon 12, along with other aliphatic polyamides.…”

Section: Introductionmentioning

confidence: 99%

“…ω-AmDDA is a very important monomer for the synthesis of Nylon 12, along with other aliphatic polyamides. Owing to its extraordinary heat-, abrasion-, chemical-, UV-, and scratch-resistance capabilities, Nylon 12 is frequently used as a coating agent on fuel and braking systems in most passenger cars [9,10]. Usually, Nylon 12 is industrially produced from the monomer ω-laurolactam through ring opening polymerization, the chemical synthesis of which is initiated by the trimerization of 1,3-butadiene originating from steam cracking (200-300 • C) of crude oil [9,10].…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2018

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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).

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Biosynthesis of the Nylon 12 Monomer, ω‐Aminododecanoic Acid with Novel CYP153A, AlkJ, and ω‐TA Enzymes

Cited by 35 publications

References 52 publications

Kinetic Resolution of Racemic Amines to Enantiopure (S)-amines by a Biocatalytic Cascade Employing Amine Dehydrogenase and Alanine Dehydrogenase

Kinetic Resolution of Racemic Amines to Enantiopure (S)-amines by a Biocatalytic Cascade Employing Amine Dehydrogenase and Alanine Dehydrogenase

Biocatalyzed C−C Bond Formation for the Production of Alkaloids

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

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