Metabolic engineering of fatty acyl-ACP reductase-dependent pathway to improve fatty alcohol production in Escherichia coli

Liu, Ran; Zhu, Fayin; Lü, Lei; Fu, Aisi; Lu, Jiming; Deng, Zixin; Liu, Tiangang

doi:10.1016/j.ymben.2013.12.004

Cited by 97 publications

(72 citation statements)

References 64 publications

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“…2C, and 3A,C). Sometimes the inherent AHR activity was enough so that no further overexpression was needed (Liu et al, 2014). In our work, there still some fatty aldehydes were not transformed (Figs.…”

Section: Selection Of Ahrs and Adsmentioning

confidence: 50%

“…Firstly, β-oxidation of FFAs was blocked by knocking out fadD or fadE. In previous work, knocking out fadD or fadE improved FFAs accumulation (Lennen et al, 2010;Lu et al, 2008;Steen et al, 2010;Xu et al, 2013b;Zhang et al, 2012), and was also applied to increase fatty alcohols production (Liu et al, 2014). In our expression system, however, the odd-chain fatty alcohols production was severely decreased after knocking-out either fadD or fadE (Fig.…”

Section: Fine-tuning Fatty Acids Metabolism Further Improves Fatty Almentioning

confidence: 68%

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Biosynthesis of odd-chain fatty alcohols in Escherichia coli

Cao

Xiao

Liu

et al. 2015

Metabolic Engineering

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Section: Selection Of Ahrs and Adsmentioning

confidence: 50%

Section: Fine-tuning Fatty Acids Metabolism Further Improves Fatty Almentioning

confidence: 68%

Biosynthesis of odd-chain fatty alcohols in Escherichia coli

Cao

Xiao

Liu

et al. 2015

Metabolic Engineering

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“…Some of the enzymes of this group prefer acylCoA as the substrate, while others act more efficiently on acyl-ACP substrates, so will generate products from CoA-dependent fatty acid beta-oxidation or ACP-dependent fatty acid synthesis pathways, respectively, both of which are being investigated through metabolic engineering [101,102]. Interestingly, some of them are able to reduce fatty acid acyl-CoA/ACP directly to long-chain alcohols, requiring oxidation of two molecules of NAD(P)H, instead of one [103].…”

Section: Ec 121: Aldehyde Dehydrogenasesmentioning

confidence: 99%

Review of NAD(P)H-dependent oxidoreductases: Properties, engineering and application

Vidal

Kelly

Mordaka

et al. 2018

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

212

137

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A B S T R A C T NAD(P)H-dependent oxidoreductases catalyze the reduction or oxidation of a substrate coupled to the oxidation or reduction, respectively, of a nicotinamide adenine dinucleotide cofactor NAD(P)H or NAD(P) + . NAD(P)Hdependent oxidoreductases catalyze a large variety of reactions and play a pivotal role in many central metabolic pathways. Due to the high activity, regiospecificity and stereospecificity with which they catalyze redox reactions, they have been used as key components in a wide range of applications, including substrate utilization, the synthesis of chemicals, biodegradation and detoxification. There is great interest in tailoring NAD(P)H-dependent oxidoreductases to make them more suitable for particular applications. Here, we review the main properties and classes of NAD(P)H-dependent oxidoreductases, the types of reactions they catalyze, some of the main protein engineering techniques used to modify their properties and some interesting examples of their modification and application.

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“…This type of approach allows quantitative characterization of biological networks and prototyping of metabolic pathways for production of valuable compounds (Goerke et al, 2008;Hodgman and Jewett, 2012;Krutsakorn et al, 2013;Liu et al, 2014).…”

Section: Introductionmentioning

confidence: 99%