Enzymatic Resolution of Racemic Ethyl-2,2- Dimethylcyclopropanecarboxylate To<i>S</i>-(+)-2,2- Dimethylcyclopropanecarboxylic Acid in a Polar Organic Solvent—Water Medium

Ren, Feng; Wang, Pu; Huang, Jin; He, Jianguo

doi:10.5504/bbeq.2012.0109

Cited by 4 publications

(2 citation statements)

References 20 publications

(21 reference statements)

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“…using biotechnological processes [6][7][8]. Wang's group tested five commercial immobilized lipases from different organisms, and Novozym 435 was found to have high enantioselectivity and activity toward enzymatic resolution of racemic (±)-DmCpCe [9,10]. Yeom et al investigated the enantioselective production of (S)-2,2-dimethylcyclopropane carboxylic acid in 53 Rhodococcus and Pseudomonas related strains, and found that Rhodococcus erythropolis ATCC 25544 exhibited the highest enantioselectivity [11].…”

Section: Several Efforts Have Been Reported Towards Biocatalytic Syntmentioning

confidence: 99%

Rational design of a carboxylic esterase RhEst1 based on computational analysis of substrate binding

Chen

Luan

et al. 2015

Journal of Molecular Graphics and Modelling

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A new carboxylic esterase RhEst1 which catalyzes the hydrolysis of (S)-(+)-2,2-dimethylcyclopropanecarboxylate (S-DmCpCe), the key chiral building block of cilastatin, was identified and subsequently crystallized in our previous work. Mutant RhEst1A147I/V148F/G254A was found to show a 5-fold increase in the catalytic activity. In this work, molecular dynamic simulations were performed to elucidate the molecular determinant of the enzyme activity. Our simulations show that the substrate binds much more strongly in the A147I/V148F/G254A mutant than in wild type, with more hydrogen bonds formed between the substrate and the catalytic triad and the oxyanion hole. The OH group of the catalytic residue Ser101 in the mutant is better positioned to initiate the nucleophilic attack on S-DmCpCe. Interestingly, the "170-179" loop which is involved in shaping the catalytic sites and facilitating the product release shows remarkable dynamic differences in the two systems. Based on the simulation results, six residues were identified as potential "hot-spots" for further experimental testing. Consequently, the G126S and R133L mutants show higher catalytic efficiency as compared with the wild type. This work provides molecular-level insights into the substrate binding mechanism of carboxylic esterase RhEst1, facilitating future experimental efforts toward developing more efficient RhEst1 variants for industrial applications.

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Section: Several Efforts Have Been Reported Towards Biocatalytic Syntmentioning

confidence: 99%

Rational design of a carboxylic esterase RhEst1 based on computational analysis of substrate binding

Chen

Luan

et al. 2015

Journal of Molecular Graphics and Modelling

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“…However, residual activity of the lipase from T. lanuginosus decreased to 10% in the 2nd reaction cycle. Although DMF was a desirable solvent to dissolve the N ‐acetyl‐ l ‐leucine, this solvent may inactivate the lipase (Plou et al., ; Ren, Wang, Huang, & He, ).…”

Section: Resultsmentioning

confidence: 99%

A Novel Modified Lipid: Enzymatic Esterification of 2‐Monoacylglycerol with N‐acetyl‐l‐leucine

Çavdar

Yanık

Göğüş

et al. 2018

Journal of Food Science

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A novel modified lipid was synthesized by enzymatic incorporation of a "hydrophobic and essential amino acid derivative" into 2-monoacylglycerol. This modified lipid contains mainly oleic acid at sn-2 position and N-acetyl-l-leucine at sn-1,3 positions. The product behaved as an oil above 10 °C. Caloric value of the novel oil-like product was reduced by 18.65%. The modified lipid may have the potential for replacement with the oil in food products such as margarine, shortenings, salad dressing, and mayonnaise.

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Protein termini relocation plus random mutation: A new strategy for finding key sites in esterase evolution

Chen

et al. 2018

Molecular Catalysis

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Enzymatic Resolution of Racemic Ethyl-2,2- Dimethylcyclopropanecarboxylate ToS-(+)-2,2- Dimethylcyclopropanecarboxylic Acid in a Polar Organic Solvent—Water Medium

Cited by 4 publications

References 20 publications

Rational design of a carboxylic esterase RhEst1 based on computational analysis of substrate binding

Rational design of a carboxylic esterase RhEst1 based on computational analysis of substrate binding

A Novel Modified Lipid: Enzymatic Esterification of 2‐Monoacylglycerol with N‐acetyl‐l‐leucine

Protein termini relocation plus random mutation: A new strategy for finding key sites in esterase evolution

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