Efficient production of the Nylon 12 monomer ω-aminododecanoic acid methyl ester from renewable dodecanoic acid methyl ester with engineered Escherichia coli

Ladkau, Nadine; Aßmann, Miriam; Schrewe, Manfred; Julsing, Mattijs K.; Schmid, Andreas; Bühler, Bruno

doi:10.1016/j.ymben.2016.02.011

Cited by 71 publications

(62 citation statements)

References 47 publications

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“…Dodecanoic acid methyl ester was also converted via the same cascade to give 12‐aminododecanoic acid methyl ester. The biotransformation was significantly improved through further engineering the E. coli catalyst by introducing outer membrane porin AlkL (increase substrate uptake), alcohol dehydrogenase AlkJ (increase oxidation of alcohol), and alanine dehydrogenase AlaDH (regenerate l ‐alanine for CvTA) …”

Section: Recent Development Of Whole‐cell Cascade Biotransformationsmentioning

confidence: 99%

Whole‐Cell Cascade Biotransformations for One‐Pot Multistep Organic Synthesis

2018

ChemCatChem

107

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Performing one‐pot multi‐catalysis reactions is a revolutionary tool for multistep synthesis, representing a fast‐developing theme in catalysis field. To develop cascade reactions, enzymes are ideal catalysts due to their compatible reaction conditions. The implementation of enzyme cascades in recombinant microbial cells provides easily available self‐replicating catalysts for facile one‐pot biotransformations to produce a wide range of high‐value (chiral) chemicals. In this minireview, we summarize the recent development of whole‐cell cascade biotransformations according to the types of substrates, ranging from petrochemicals to biochemicals. Furthermore, we provide general instructions for the establishment of in vivo enzyme cascades, discuss the encountered problems and the corresponding solutions, and highlight the promising directions for future advance.

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Section: Recent Development Of Whole‐cell Cascade Biotransformationsmentioning

confidence: 99%

Whole‐Cell Cascade Biotransformations for One‐Pot Multistep Organic Synthesis

2018

ChemCatChem

107

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“…[2] For instance, chiral amines and lactones were produced in a high yield from alcohols through enzyme cascade reactions involving alcohol dehydrogenases (ADHs) and amine transaminases (ATAs) with redox-recycling ADHs (e. g., lactate dehydrogenases and amine dehydrogenases) and Baeyer-Villiger monooxygenases. [4] The nicotinamide cofactors were provided by cellular carbon metabolism, while the amino donor (i. e., alanine) was regenerated by the alanine dehydrogenase inside cells. [4] The nicotinamide cofactors were provided by cellular carbon metabolism, while the amino donor (i. e., alanine) was regenerated by the alanine dehydrogenase inside cells.…”

Section: Introductionmentioning

confidence: 99%

Enzyme Cascade Reactions for the Biosynthesis of Long Chain Aliphatic Amines from Renewable Fatty Acids

et al. 2019

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Enzyme cascade reactions for the synthesis of long chain aliphatic amines such as (Z)-12aminooctadec-9-enoic acid, 10-or 12-aminooctadecanoic acid, and 10-amino-12-hydroxyoctadecanoic acid from renewable fatty acids were investigated. (Z)-12-aminooctadec-9-enoic acid was produced from ricinoleic acid ((Z)-12-hydroxyoctadec-9-enoic acid) via (Z)-12-ketooctadec-9-enoic acid with a conversion of 71% by a two-step in vivo biotransformation involving a long chain secondary alcohol dehydrogenase (SADH) from Micrococcus luteus and a variant of the amine transaminase (ATA) from Vibrio fluvialis. 10-Aminooctadecanoic acid was prepared from oleic acid ((Z)-octadec-9-enoic acid) via 10-hydroxyoctadecanoic acid and 10-ketooctadecanoic acid by an in vivo three-step biocatalysis reaction involving not only the SADH and ATA variants, but also a fatty acid double bond hydratase (OhyA) from Stenotrophomonas maltophilia. 10-Aminooctadecanoic acid was produced at a total rate of 4.4 U/g dry cells with a conversion of 87% by recombinant Escherichia coli expressing the SADH and ATA variants, and OhyA simultaneously. In addition, bulky aliphatic amines could also be produced by the isolated enzymes (i. e., the SADH, the ATA variants, and a nicotinamide adenine dinucleotide (NADH) oxidase from Lactobacillus brevis) with methylbenzylamine or benzylamine as amino donor. This study thus contributes to the biosynthesis of long chain aliphatic amines having two large substituents next to the amine functionality.

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“…[1] Industrially important reaction classes, such as oxidative-reductive transformations, often require reduced electron donors, namely nicotinamide cofactors. As ar esult, biocatalysis is becoming an important pillar of catalysis fort he preparation of specialty and platform chemicals.…”

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confidence: 99%