690295

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Stereoselective reduction of ethyl 4-chloro-3-oxobutanoate by fungi.

Y Saratani et al.

Bioscience, biotechnology, and biochemistry, 65(7), 1676-1679 (2001-08-23)

The enantioselectivity of ECAA to ECHB by eight fungi of four genus was evaluated. All strains showed (S)-selectivity, and Cylindrocarpon sclerotigenum IFO 31855 gave the highest yield and good optical purity (e.e.; >99%). Cell-free extract and acetone-dried cells of C.

Construction of a two-strain system for asymmetric reduction of ethyl 4-chloro-3-oxobutanoate to (S)-4-chloro-3-hydroxybutanoate ethyl ester.

Zhinan Xu et al.

Applied microbiology and biotechnology, 70(1), 40-46 (2005-09-22)

Escherichia coli M15 (pQE30-car0210) was constructed to express carbonyl reductase (CAR) by cloning the car gene from Candida magnoliae and inserting it into pQE30. By cultivating E. coli M15 (pQE30-car0210) and M15 (pQE30-gdh0310), 8.2-fold and 12.3-fold enhancements in specific enzymatic

Microwave-assisted synthesis of cyclopentanones using the relevant phosphorus ylides.

Faramarz Rostami-Charati et al.

Combinatorial chemistry & high throughput screening, 15(4), 354-357 (2012-01-24)

A one-pot synthesis of cyclopentanone derivatives from phosphorus ylide under lab-type microwave assisted methodology was described. The phosphorus ylides were obtained via the reaction of activated acetylenic compounds, ethyl 4-chloroacetoacetate and triphenylphosphine. The structure of phosphorus ylides was assigned by

Fungal aerobic reductive dechlorination of ethyl 2-chloroacetoacetate by Saccharomyces cerevisiae: mechanism of a novel type of microbial dehalogenation.

Gerhard Jörg et al.

Chembiochem : a European journal of chemical biology, 5(1), 87-92 (2003-12-26)

Saccharomyces cerevisiae reduces the beta-keto ester ethyl 2-chloroacetoacetate to the respective chiral cis- and trans-beta-hydroxy esters. In the course of chiral reduction, competing dehalogenation of the xenobiotic substrate to ethyl acetoacetate occurs, in a reaction mediated by cytosolic glutathione (GSH).

Purification and characterization of a novel NADH-dependent carbonyl reductase from Pichia stipitis involved in biosynthesis of optically pure ethyl (S)-4-chloro-3-hydroxybutanoate.

Hou Cao et al.

Bioresource technology, 102(2), 1733-1739 (2010-10-12)

A novel NADH-dependent dehydrogenases/reductases (SDRs) superfamily reductase (PsCRII) was isolated from Pichia stipitis. It produced ethyl (S)-4-chloro-3-hydroxybutanoate [(S)-CHBE] in greater than 99% enantiomeric excess. This enzyme was purified to homogeneity by ammonium sulfate precipitation followed by Q-Sepharose chromatography. Compared to

Robust NADH-regenerator: improved alpha-haloketone-resistant formate dehydrogenase.

H Yamamoto et al.

Applied microbiology and biotechnology, 67(1), 33-39 (2004-09-01)

Formate dehydrogenases (FDH) are useful for the regeneration of NADH, which is required for asymmetric reduction by several dehydrogenases and reductases. FDHs have relatively low activity and are labile, especially to alpha-haloketones, thus FDH cannot be applied to the industrial

Asymmetric reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate with two co-existing, recombinant Escherichia coli strains.

Ying Liu et al.

Biotechnology letters, 27(2), 119-125 (2005-02-11)

Two recombinant strains, E. coli M15 (pQE30-alr0307) and E. coli M15 (pQE30-gdh0310), which were constructed to express, respectively, an NADPH-dependent aldehyde reductase gene and a glucose dehydrogenase gene, were mixed in an appropriate ratio and used for the asymmetric reduction

Stereoselective reduction of ethyl 4-chloro-3-oxobutanoate by Escherichia coli transformant cells coexpressing the aldehyde reductase and glucose dehydrogenase genes.

M Kataoka et al.

Applied microbiology and biotechnology, 51(4), 486-490 (1999-05-26)

The asymmetric reduction of ethyl 4-chloro-3-oxobutanoate (COBE) to ethyl (R)-4-chloro-3-hydroxybutanoate [(R)-CHBE] using Escherichia coli cells, which coexpress both the aldehyde reductase gene from Sporobolomyces salmonicolor and the glucose dehydrogenase (GDH) gene from Bacillus megaterium as a catalyst was investigated. In

Cloning, overexpression, and mutagenesis of the Sporobolomyces salmonicolor AKU4429 gene encoding a new aldehyde reductase, which catalyzes the stereoselective reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (S)-4-chloro-3-hydroxybutanoate.

K Kita et al.

Applied and environmental microbiology, 65(12), 5207-5211 (1999-12-03)

We cloned and sequenced the gene encoding an NADPH-dependent aldehyde reductase (ARII) in Sporobolomyces salmonicolor AKU4429, which reduces ethyl 4-chloro-3-oxobutanoate (4-COBE) to ethyl (S)-4-chloro-3-hydroxybutanoate. The ARII gene is 1,032 bp long, is interrupted by four introns, and encodes a 37,315-Da

Highly efficient synthesis of chiral alcohols with a novel NADH-dependent reductase from Streptomyces coelicolor.

Li-Juan Wang et al.

Bioresource technology, 102(14), 7023-7028 (2011-05-17)

An NADH-dependent reductase (ScCR) from Streptomyces coelicolor was discovered by genome mining for carbonyl reductases. ScCR was overexpressed in Escherichia coli BL21, purified to homogeneity and its catalytic properties were studied. This enzyme catalyzed the asymmetric reduction of a broad

Efficient production of recombinant aldehyde reductase and its application for asymmetric reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate.

Keju Jing et al.

Preparative biochemistry & biotechnology, 35(3), 203-215 (2005-08-20)

An NADPH-dependent aldehyde reductase (ALR, EC1.1.1.2) gene is cloned from Sporobolomyces salmonicolor ZJUB 105, and inserted into plasmid pQE30 to construct the expression plasmid (pQE30-ALR). A variety of E. coli strains were employed as hosts to obtain transformants with pQE30-ALR

Characterization and identification of three novel aldo-keto reductases from Lodderomyces elongisporus for reducing ethyl 4-chloroacetoacetate.

Chenxi Ning et al.

Archives of biochemistry and biophysics, 564, 219-228 (2014-12-03)

Lodderomyces elongisporus LH703 isolated from soil samples contained three novel aldo-keto reductases (AKRs) (LEAKR 48, LEAKR 49, and LEAKR 50). The three enzymes were cloned, expressed, and purified to homogeneity for characterization. These three AKRs shared <40% amino acid identity

Purification and characterization of an alpha-haloketone-resistant formate dehydrogenase from Thiobacillus sp. strain KNK65MA, and cloning of the gene.

Hirokazu Nanba et al.

Bioscience, biotechnology, and biochemistry, 67(10), 2145-2153 (2003-10-31)

Thiobacillus sp. strain KNK65MA, which produced an NAD-dependent formate dehydrogenase (FDH) highly resistant to alpha-haloketones, was newly isolated, i.e., the enzyme showed no loss of activity after a 5-h incubation with alpha-haloketones, such as ethyl 4-chloro-3-oxobutanoate. The enzyme was also

Molecular cloning and overexpression of the gene encoding an NADPH-dependent carbonyl reductase from Candida magnoliae, involved in stereoselective reduction of ethyl 4-chloro-3-oxobutanoate.

Y Yasohara et al.

Bioscience, biotechnology, and biochemistry, 64(7), 1430-1436 (2000-08-17)

An NADPH-dependent carbonyl reductase (S1) isolated from Candida magnoliae catalyzed the reduction of ethyl 4-chloro-3-oxobutanoate (COBE) to ethyl (S)-4-chloro-3-hydroxybutanoate (CHBE), with a 100% enantiomeric excess, which is a useful chiral building block for the synthesis of pharmaceuticals. The gene encoding

A novel NADH-dependent carbonyl reductase from Kluyveromyces aestuarii and comparison of NADH-regeneration system for the synthesis of ethyl (S)-4-chloro-3-hydroxybutanoate.

Hiroaki Yamamoto et al.

Bioscience, biotechnology, and biochemistry, 68(3), 638-649 (2004-04-02)

To compare NADH-regeneration systems for the synthesis of (S)-4-chloro-3-hydroxybutanoate (ECHB), a novel NADH-dependent carbonyl reductase (KaCR1), which reduced ethyl 4-chloroacetoacetate (ECAA) to form (S)-ECHB, was screened and purified from Kluyveromyces aestuarii and a gene encoding KaCR1 was cloned. Glucose dehydrogenase

Purification and properties of a carbonyl reductase involved in stereoselective reduction of ethyl 4-chloro-3-oxobutanoate from Cylindrocarpon sclerotigenum IFO 31855.

Yuri Saratani et al.

Bioscience, biotechnology, and biochemistry, 67(6), 1417-1420 (2003-07-05)

A NADPH-dependent carbonyl reductase (CSCR1) was purified to homogeneity from Cylindrocarpon sclerotigenum IFO 31855. The enzyme catalyzed the stereoselective reduction of ethyl 4-chloro-3-oxobutanoate to the corresponding (S)-alcohol with a >99% enantiomer excess. The relative molecular mass of the enzyme was

Enantioselective bioconversion using Escherichia coli cells expressing Saccharomyces cerevisiae reductase and Bacillus subtilis glucose dehydrogenase.

Hyun Joo Park et al.

Journal of microbiology and biotechnology, 20(9), 1300-1306 (2010-10-05)

Ethyl (R, S)-4-chloro-3-hydroxybutanoate (ECHB) is a useful chiral building block for the synthesis of L-carnitine and hypercholesterolemia drugs. The yeast reductase, YOL151W (GenBank locus tag), exhibits an enantioselective reduction activity, converting ethyl-4-chlorooxobutanoate (ECOB) exclusively into (R)-ECHB. YOL151W was generated in

Asymmetric synthesis of (S)-ethyl-4-chloro-3-hydroxybutanoate using Candida parapsilosis ATCC 7330.

Tarjan Kaliaperumal et al.

Journal of industrial microbiology & biotechnology, 37(2), 159-165 (2009-11-10)

Asymmetric reduction of ethyl-4-chloro-3-oxobutanoate to (S)-ethyl-4-chloro-3-hydroxybutanoate in aqueous medium by resting cells of Candida parapsilosis ATCC 7330 was optimized. The influence of culture parameters (inoculum size, inoculum age and biocatalyst harvest time) and reaction parameters (co-substrate, resting cell, pH and

Applying slow-release biocatalysis to the asymmetric reduction of ethyl 4-chloroacetoacetate.

Jer-Yiing Houng et al.

Biotechnology letters, 25(1), 17-21 (2003-07-29)

Amberlite XAD 2 resin enhanced the asymmetric reduction of ethyl 4-chloroacetoacetate (ECA) to S-4-chloro-3-hydroxybutyric acid ethyl ester as catalyzed by Saccharomyces cerevisiae. The absorbed ECA was released slowly to the solution during the reaction so that the substrate inhibition and

A novel carbonyl reductase from Pichia stipitis for the production of ethyl (S)-4-chloro-3-hydroxybutanoate.

Qi Ye et al.

Biotechnology letters, 31(4), 537-542 (2009-01-07)

An NADPH-dependent carbonyl reductase (PsCR) gene from Pichia stipitis was cloned. It contains an open reading frame of 849 bp encoding 283 amino acids whose sequence had less than 60% identity to known reductases that produce ethyl (S)-4-chloro-3-hydroxybutanoates (S-CHBE). When

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

Ming-An Yu et al.

Journal of industrial microbiology & biotechnology, 34(2), 151-156 (2006-10-18)

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)

Biosimulation of drug metabolism--a yeast based model.

I Pieper et al.

European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences, 36(1), 157-170 (2008-12-02)

Computationally predicting the metabolic fates of drugs is a very complex task which is owed not only to the huge and diverse biochemical network in the living cell, but also to the majority of in vivo transformations that occur through

A novel reductase from Candida albicans for the production of ethyl (S)-4-chloro-3-hydroxybutanoate.

Mingdong An et al.

Bioscience, biotechnology, and biochemistry, 76(6), 1210-1212 (2012-07-14)

A novel NADPH-dependent reductase (CaCR) from Candida albicans was cloned for the first time. It catalyzed asymmetric reduction to produce ethyl (S)-4-chloro-3-hydroxybutanoate ((S)-CHBE). It contained an open reading frame of 843 bp encoding 281 amino acids. When co-expressed with a

High-level production of heterologous proteins using untreated cane molasses and corn steep liquor in Escherichia coli medium.

Qi Ye et al.

Applied microbiology and biotechnology, 87(2), 517-525 (2010-03-24)

To develop an economical industrial medium, untreated cane molasses (UCM) was tested as a carbon source for fermentation culturing of Escherichia coli. To test the industrial application of this medium, we chose a strain co-expressing a carbonyl reductase (PsCR) and

Development of a substrate-coupled biocatalytic process driven by an NADPH-dependent sorbose reductase from Candida albicans for the asymmetric reduction of ethyl 4-chloro-3-oxobutanoate.

Ping Cai et al.

Biotechnology letters, 34(12), 2223-2227 (2012-08-25)

A substrate-coupled biocatalytic process was developed based on the reactions catalyzed by an NADPH-dependent sorbose reductase (SOU1) from Candida albicans in which ethyl 4-chloro-3-oxobutanoate (COBE) was reduced to (S)-4-chloro-3-hydroxybutanoate [(S)-CHBE], while NADPH was regenerated by the same enzyme via oxidation

Synthesis of optically pure ethyl (S)-4-chloro-3-hydroxybutanoate by Escherichia coli transformant cells coexpressing the carbonyl reductase and glucose dehydrogenase genes.

N Kizaki et al.

Applied microbiology and biotechnology, 55(5), 590-595 (2001-06-21)

The asymmetric reduction of ethyl 4-chloro-3-oxobutanoate (COBE) to ethyl (S)-4-chloro-3-hydroxybutanoate ((S)-CHBE) was investigated. Escherichia coli cells expressing both the carbonyl reductase (S1) gene from Candida magnoliae and the glucose dehydrogenase (GDH) gene from Bacillus megaterium were used as the catalyst.

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