Asymmetric hydrolysis of racemic para-nitrostyrene oxide using an epoxide hydrolase preparation from Aspergillus niger

Morisseau, Christophe; Nellaiah, H.; Archelas, Alain; Furstoss, R.; Baratti, J.

doi:10.1016/s0141-0229(97)00168-3

Cited by 71 publications

(23 citation statements)

References 22 publications

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“…Consequently, formation of enantiopure epoxides via a nonoxidative, preferably hydrolytic route like kinetic resolution of epoxide racemates is a very attractive option, and initial attempts have been made for the production of (S)-para-nitrostyrene oxide. Using partially purified enzyme preparations of Aspergillus niger to obtain high-volumetric activities, the quantitative formation of around 160 mM enantiopure (S)-para-nitrostyrene oxide in 5 h corresponding to an average volumetric rate of 533 U L tot −1 (5.3 g и (L tot h) −1 ) on a 2-to 10-mL scale was reported (Morisseau et al, 1997). This approach requires first synthesizing and purifying the epoxide-substrate, which is not necessary when using monooxygenases that directly use the (substituted) styrene as the substrate.…”

Section: Effectiveness Of Recombinant Epoxide Productionmentioning

confidence: 99%

Production of enantiopure styrene oxide by recombinantEscherichia coli synthesizing a two-component styrene monooxygenase

Panke

Wubbolts²,

Schmid³

et al. 2000

Biotechnol. Bioeng.

129

122

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Section: Effectiveness Of Recombinant Epoxide Productionmentioning

confidence: 99%

Production of enantiopure styrene oxide by recombinantEscherichia coli synthesizing a two-component styrene monooxygenase

Panke

Wubbolts²,

Schmid³

et al. 2000

Biotechnol. Bioeng.

129

122

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“…One year later, a cell-free extract from A. niger LCP 521 was used as a biocatalyst [97]. To improve the solubility of p-NSO in the reaction mixture 20% of a miscible solvent (DMSO or DMF) were added.…”

Section: Nitrostyrene Oxidementioning

confidence: 99%

Epoxide Hydrolases and their Application in Organic Synthesis

2016

Self Cite

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c h a p t e r 8 INTRODUCTIONOrganic chemists have become interested in enzymes as catalysts due to their high efficiencies and specificities. Moreover, recent progress in molecular biology and enzyme-related research areas enabled and simplified the production and purifica tion of recombinant enzymes in large quantities and their engineering toward tailormade biocatalysts using straightforward mutagenesis and screening techniques. This is also true for epoxide hydrolases (EHs), as evidenced by the many published research papers about the synthetic applications of naturally occurring or engi neered EHs. EHs catalyze the opening of oxirane rings, generating a vicinal diol as the final product ( Figure 8.1). From a synthetic chemistry point of view, the most valuable EHs are those with either (i) high enantioselectivities or (ii) a combination of low enantio preference with a high level of enantioconvergence. While the former generate enan tiopure epoxides with a maximum yield of 50% in a kinetic resolution process, the latter produce ideally an enantiopure diol product with a theoretical yield of 100%. Thus, EHs provide convenient access to enantiopure epoxides or diols from racemic epoxides. Furthermore, the enantiopure diols can then often be chemically trans formed back to the corresponding epoxides with no effect on the enantiomeric excess (ee). High values of enantioselectivity or enantioconvergence are a consequence of particular enzyme-substrate interactions, which can be modulated by specific reac tion conditions or through the exchange of specific amino acids of the biocatalyst. The final stereochemical outcome of an EH-catalyzed reaction depends solely on the regioselectivity coefficients, which determine the absolute configuration and the ee of the diol product when the reaction reaches 100% conversion. During the reaction, the oxirane ring of each enantiomer is often attacked at either carbon atom, resulting in a mixture of diol enantiomers (Figure 8.2). Unfortunately, several authors used the product-derived E-value, E P (calculated from c and ee P using Sih's equation; see Ref.[1]) for characterizing the stereochemistry of the diol formation of an EH-mediated hydrolysis reaction [2,3]. This is wrong and misleading for epoxide-opening reac tions since there are two possible positions of attack for each oxirane enantiomer. The ideal enantioconvergent EH leads to deracemization of a racemic mixture of an epox ide and exhibits reversed regioselectivity for either substrate enantiomer, that is,

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“…In lipases so called 'interfacial activation', where enzyme activity sharply increases when the substrate reaches the concentration where it forms a second phase, is ascribed to the presence of a cap (or lid) [17]. It has been demonstrated in several studies [18][19][20][21] that EH catalysed resolution of racemic epoxides benefit from high substrate concentrations with optimal results (improved rates and enantioselectivities) obtained at concentrations where the substrate was present as a second hydrophobic phase. It is thus tempting to consider the possibility of 'interfacial activation' as observed for lipases, where enzyme activity markedly increases when the substrate reaches the concentration where it forms a second Table 1.…”

Section: Classification Structure and Mechanismmentioning

confidence: 99%

Diversity of Epoxide Hydrolase Biocatalysts

Labuschagne¹

2006

COC

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Chiral epoxides and their derivatives are versatile intermediates for the synthesis of enantiopure organic chemicals. Chiral epoxides can be obtained through asymmetric epoxidation using either chemical catalysts or epoxidizing enzymes such as monooxygenases or chloroperoxidases. Alternatively hydrolytic kinetic resolution of racemic epoxides can yield a mixture containing, in an ideal situation, a single enantiomer of the remaining epoxide and a single enantiomer of the formed diol. Occasionally catalysts with complementary enantioselectivities and opposite regioselectivities can give through enantioconvergent hydrolysis one diol enantiomer in > 90% yield. Hydrolyses can also be performed with either metal catalysts or biological catalysts, mainly epoxide hydrolases. Epoxide hydrolases show great promise for the preparative scale hydrolysis of epoxides, because they are easy-to-use biocatalysts that accept a wide range of substrates, that do not require co-factors and that show improved activity when the substrate is present as a second water immiscible phase. X-ray structures for one fungal, one bacterial and two mammalian epoxide hydrolases are available as well as gene sequences for more than ninety five epoxide hydrolases. Expression systems in Escherichia coli and other hosts have also been developed and different assays suitable for high throughput screening have been developed and tested. The latter developments also made possible the first attempts at catalyst improvement through site directed mutagenesis and directed evolution. This review will give a comparative overview of the different types of epoxide hydrolases, which recently gave promising results for hydrolytic kinetic or enantioconvergent resolution of different types of epoxides and of results obtained with various recombinant epoxide hydrolases.

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Asymmetric hydrolysis of racemic para-nitrostyrene oxide using an epoxide hydrolase preparation from Aspergillus niger

Cited by 71 publications

References 22 publications

Production of enantiopure styrene oxide by recombinantEscherichia coli synthesizing a two-component styrene monooxygenase

Production of enantiopure styrene oxide by recombinantEscherichia coli synthesizing a two-component styrene monooxygenase

Epoxide Hydrolases and their Application in Organic Synthesis

Diversity of Epoxide Hydrolase Biocatalysts

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