Biosynthesis of enantiopure ( S )-3-hydroxybutyrate from glucose through the inverted fatty acid β-oxidation pathway by metabolically engineered Escherichia coli

Gulevich, A. Yu.; Skorokhodova, A. Yu.; Sukhozhenko, A. V.; Дебабов, В. Г.

doi:10.1016/j.jbiotec.2017.01.009

Cited by 16 publications

(16 citation statements)

References 42 publications

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“…The two enantiomers of ethyl 3-hydroxybutyrate are important building blocks for the synthesis of valuable pharmaceuticals, [3][4][5] which can principally be prepared either by organic synthesis 8,9 or by biocatalytic methods. 12,13 However, traditional organic synthesis generally uses expensive chiral metal catalysts, harsh working conditions, and toxic organic solvents, thus bringing great pollutions to our environments. 9,13 The development of biocatalysis methods is of great importance in the preparation of valuable chiral building blocks represented by chiral ethyl 3-hydroxybutyrate.…”

Section: Discussionmentioning

confidence: 99%

“…For example, chiral ethyl 3‐hydroxybutyrate can be prepared through the reduction of corresponding ketone precursors using dehydrogenases as the biocatalysts . But the reduction reactions catalyzed by dehydrogenases require the involvement of expensive cofactors such as NADH or NADPH . Thus, another route for providing cofactors has to be established at the same time, which makes the enzymatic synthetic method derived from dehydrogenases more complicated.…”

Section: Introductionmentioning

confidence: 99%

“…10,11 But the reduction reactions catalyzed by dehydrogenases require the involvement of expensive cofactors such as NADH or NADPH. 12,13 Thus, another route for providing cofactors has to be established at the same time, which makes the enzymatic synthetic method derived from dehydrogenases more complicated.…”

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confidence: 99%

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Functional characterization of salt‐tolerant microbial esterase WDEst17 and its use in the generation of optically pure ethyl (R)‐3‐hydroxybutyrate

Wang

Zhang

et al. 2018

Chirality

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The two enantiomers of ethyl 3-hydroxybutyrate are important intermediates for the synthesis of a great variety of valuable chiral drugs. The preparation of chiral drug intermediates through kinetic resolution reactions catalyzed by esterases/lipases has been demonstrated to be an efficient and environmentally friendly method. We previously functionally characterized microbial esterase PHE21 and used PHE21 as a biocatalyst to generate optically pure ethyl (S)-3-hydroxybutyrate. Herein, we also functionally characterized one novel salt-tolerant microbial esterase WDEst17 from the genome of Dactylosporangium aurantiacum subsp. Hamdenensis NRRL 18085. Esterase WDEst17 was further developed as an efficient biocatalyst to generate (R)-3-hydroxybutyrate, an important chiral drug intermediate, with the enantiomeric excess being 99% and the conversion rate being 65.05%, respectively, after process optimization. Notably, the enantio-selectivity of esterase WDEst17 was opposite than that of esterase PHE21. The identification of esterases WDEst17 and PHE21 through genome mining of microorganisms provides useful biocatalysts for the preparation of valuable chiral drug intermediates.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Functional characterization of salt‐tolerant microbial esterase WDEst17 and its use in the generation of optically pure ethyl (R)‐3‐hydroxybutyrate

Wang

Zhang

et al. 2018

Chirality

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“…3HB can be produced in different ways: via chemical catalysis (Jaipuri et al 2004 ; Noyori et al 1987 ), via enzymatic or chemical degradation of polyhydroxybutyrate (PHB) (de Roo et al 2002 ; Lee et al 1999 , 2000 ), or via fermentation with metabolically engineered microorganisms (Gao et al 2002 ; Gulevich et al 2017 ; Lee and Lee 2003 ; Liu et al 2007 ; Matsumoto et al 2013 ; Tseng et al 2009 ). Direct production of 3HB from renewable raw materials using engineered strains is a promising approach that also avoids the extreme conditions required for chemical catalysis or the use of two consecutive processes for the route through PHB.…”

Section: Introductionmentioning

confidence: 99%

“…Secondly, thioesterase TesB, a native E. coli enzyme, has been reported to hydrolyze β-hydroxyacyl-CoA thioesters (Barnes and Wakil 1968 ; Barnes et al 1970 ). Enhanced productivity of both enantiomers (R and S) of 3HB was reported by overexpression of tesB in recombinant E. coli (Gao et al 2002 ; Gulevich et al 2017 ; Liu et al 2007 ; Tseng et al 2009 ). This enzyme was also reported to play an important role in 3-hydroxydecanoyl-CoA hydrolysis (Zheng et al 2004 ).…”

Section: Introductionmentioning

confidence: 99%

The role of the acyl-CoA thioesterase “YciA” in the production of (R)-3-hydroxybutyrate by recombinant Escherichia coli

Guevara-Martínez

Pérez-Zabaleta

Gustavsson

et al. 2019

Appl Microbiol Biotechnol

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Biotechnologically produced ( R )-3-hydroxybutyrate is an interesting pre-cursor for antibiotics, vitamins, and other molecules benefitting from enantioselective production. An often-employed pathway for ( R )-3-hydroxybutyrate production in recombinant E. coli consists of three-steps: (1) condensation of two acetyl-CoA molecules to acetoacetyl-CoA, (2) reduction of acetoacetyl-CoA to ( R )-3-hydroxybutyrate-CoA, and (3) hydrolysis of ( R )-3-hydroxybutyrate-CoA to ( R )-3-hydroxybutyrate by thioesterase. Whereas for the first two steps, many proven heterologous candidate genes exist, the role of either endogenous or heterologous thioesterases is less defined. This study investigates the contribution of four native thioesterases (TesA, TesB, YciA, and FadM) to ( R )-3-hydroxybutyrate production by engineered E. coli AF1000 containing a thiolase and reductase from Halomonas boliviensis . Deletion of yciA decreased the ( R )-3-hydroxybutyrate yield by 43%, whereas deletion of tesB and fadM resulted in only minor decreases. Overexpression of yciA resulted in doubling of ( R )-3-hydroxybutyrate titer, productivity, and yield in batch cultures. Together with overexpression of glucose-6-phosphate dehydrogenase, this resulted in a 2.7-fold increase in the final ( R )-3-hydroxybutyrate concentration in batch cultivations and in a final ( R )-3-hydroxybutyrate titer of 14.3 g L −1 in fed-batch cultures. The positive impact of yciA overexpression in this study, which is opposite to previous results where thioesterase was preceded by enzymes originating from different hosts or where ( S )-3-hydroxybutyryl-CoA was the substrate, shows the importance of evaluating thioesterases within a specific pathway and in strains and cultivation conditions able to achieve significant product titers. While directly relevant for ( R )-3-hydroxybutyrate production, these findings also contribute to pathway improvement or decreased by-product formation for other acyl-CoA-derived products. Electronic supplementary material The online version of this article (10.1007/s00253-019-09707-0) contains supplementary material, which is available to authorized users.

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Production of cellulosic butyrate and 3-hydroxybutyrate in engineered Escherichia coli

Miscevic

Srirangan

Kefale

et al. 2019

Appl Microbiol Biotechnol

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Biosynthesis of enantiopure ( S )-3-hydroxybutyrate from glucose through the inverted fatty acid β-oxidation pathway by metabolically engineered Escherichia coli

Cited by 16 publications

References 42 publications

Functional characterization of salt‐tolerant microbial esterase WDEst17 and its use in the generation of optically pure ethyl (R)‐3‐hydroxybutyrate

Functional characterization of salt‐tolerant microbial esterase WDEst17 and its use in the generation of optically pure ethyl (R)‐3‐hydroxybutyrate

The role of the acyl-CoA thioesterase “YciA” in the production of (R)-3-hydroxybutyrate by recombinant Escherichia coli

Production of cellulosic butyrate and 3-hydroxybutyrate in engineered Escherichia coli

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