Highly enantioselective reduction of ethyl 4-chloro-3-oxobutanoate to L- and D- 3-hydroxyesters with baker’s yeast

Forni, Arrigo; Caselli, Emilia; Prati, Fabio; Bucciarelli, Maria; Torre, Giovanni

doi:10.3998/ark.5550190.0003.b06

Cited by 5 publications

(2 citation statements)

References 13 publications

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“…Optically active R-or S-ethyl 4-chloro-3-hydroxybutanoate (R-or S-CHBE) is one of very useful chiral building block for enantiomerically pure pharmaceuticals [1], such as L-carnitine or HMG-COA-reductase inhibitors and 1, 4-dihydropyridine-type β-blockers, respectively. Of the two enantiomers, (R) -is in greater demand yet less readily available [2].…”

Section: Introductionmentioning

confidence: 99%

Asymmetric Synthesis of Ethyl (R)-4-Chloro-3-Hydroxybutanoate with a Two Recombinant Escherichia coli System

Jing

Ban

2013

AMR

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The asymmetric reduction of ethyl 4-chloro-acetoacetate (CAAE) to ethyl (R)-4-chloro-3- hydroxybutanoate (R-CHBE) biocatalysed by the aldehyde reductase of Sporobolomyces salmonicolor expressed in E. coli M15 (pQE30-alr) in combination with regeneration of NADPH by the glucose dehydrogenase of Bacillus megaterium expressed in E. coli M15 (pQE30-gdh) was reported. The bioreduction was carried out in a two-phase reaction system with n-butyl acetate as an organic solvent. Bioconversion of 300 mmol CAAE with a final yield of 97.5 % and an enantiometric excess of 99 % was achieved without the addition of cofactor NADPH.

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Section: Introductionmentioning

confidence: 99%

Asymmetric Synthesis of Ethyl (R)-4-Chloro-3-Hydroxybutanoate with a Two Recombinant Escherichia coli System

Jing

Ban

2013

AMR

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“…10 Several enzymes from various microorganisms have been found to be able to produce (S)-1b, 11-17 whereas (R)-1b is in great demand yet less readily available. 18, 19 A recombinant aldehyde reductase from Sporobolomyces salmonicolor has been utilized to produce (R)-1b…”

Section: Introductionmentioning

confidence: 99%

Highly stereoselective reduction of prochiral ketones by a bacterial reductase coupled with cofactor regeneration

Wang

et al. 2011

Org. Biomol. Chem.

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A carbonyl reductase gene (yueD) from Bacillus sp. ECU0013 was heterologously overexpressed in Escherichia coli, and the encoded protein (BYueD) was purified to homogeneity and characterized. The NADPH-dependent reductase showed a broad substrate spectrum towards different aromatic ketones, and α- and β-ketoesters. Although the enantioselectivity was high to moderate for the reduction of α-ketoesters, all the tested β-ketoesters and aromatic ketones were reduced to the corresponding chiral alcohols in enantiomerically pure forms. Furthermore, the practical applicability of this enzyme was evaluated for the reduction of ethyl 4-chloro-3-oxobutanoate (1a). Using Escherichia coli cells coexpressing BYueD and glucose dehydrogenase, 215 g L(-1) (1.3 M) of 1a was stoichiometrically converted to ethyl (R)-4-chloro-3-hydroxybutanoate ((R)-1b) in an aqueous-toluene biphasic system by using a substrate fed-batch strategy, resulting in an overall hydroxyl product yield of 91.7% with enantiomeric purity of 99.6% ee.

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Bioconversion of ethyl 4-chloro-3-oxobutanoate by permeabilized fresh brewer’s yeast cells in the presence of allyl bromide

Wei

Zhao

et al. 2006

J Ind Microbiol Biotechnol

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Ethyl(R)-4-chloro-3-hydroxybutanoate ((R)-CHBE) are obtained by cetyltrimetylammonium bromide (CTAB) permeabilized fresh brewer's yeast whole cells bioconversion of ethyl 4-chloro-3-oxobutanoate (COBE ) in the presence of allyl bromide. The results showed that the activities of alcohol dehydrogenase (ADH) and glucose-6-phosphate dehydrogenase (G6PDH) in CTAB permeabilized brewer's yeast cells increased 525 and 7.9-fold, respectively, compared with that in the nonpermeabilized cells and had high enantioselectivity to convert COBE to (R)-CHBE. As one of co-substrates, glucose-6-phosphate was preprepared using glucose phosphorylation by hexokinase-catalyzed of CTAB permeabilized brewer's yeast cells. In a two phase reaction system with n-butyl acetate as organic solvent and with 2-propanol and glucose-6-phosphate as co-substrates, the highest (R)-CHBE concentration of 447 mM was obtained with 110-130 g/l of the CTAB permeabilized cells at optimized pH, temperature, feeding rate and the shake speed of 125 r/min. The yield and enantiomeric excess (ee) of (R)-CHBE reached 99.5 and 99%, respectively, within 6 h.

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Highly enantioselective reduction of ethyl 4-chloro-3-oxobutanoate to L- and D- 3-hydroxyesters with baker’s yeast

Cited by 5 publications

References 13 publications

Asymmetric Synthesis of Ethyl (<i>R</i>)-4-Chloro-3-Hydroxybutanoate with a Two Recombinant <i>Escherichia coli</i> System

Asymmetric Synthesis of Ethyl (<i>R</i>)-4-Chloro-3-Hydroxybutanoate with a Two Recombinant <i>Escherichia coli</i> System

Highly stereoselective reduction of prochiral ketones by a bacterial reductase coupled with cofactor regeneration

Bioconversion of ethyl 4-chloro-3-oxobutanoate by permeabilized fresh brewer’s yeast cells in the presence of allyl bromide

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