Epoxide hydrolases as asymmetric catalysts

Archer, Ian

doi:10.1016/s0040-4020(97)00843-0

Cited by 113 publications

(28 citation statements)

References 93 publications

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“…Hydrolysis of epoxides is catalysed by epoxide hydrolases from various sources. 20 Enantioselective ring opening by amines has been carried out in the presence of liver microsomes and lipases. 21,22 The ring opening of an aliphatic epoxide by N 3 − was catalysed by an immobilised enzyme preparation from a Rhodococcus sp.…”

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confidence: 99%

Exploration of the biocatalytic potential of a halohydrin dehalogenase using chromogenic substrates

Spelberg

Tang

Gelder

et al. 2002

Tetrahedron: Asymmetry

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Abstract-Halohydrin dehalogenases are bacterial enzymes that catalyse the reversible formation of epoxides from vicinal halohydrins. A spectrophotometric assay for halohydrin dehalogenases based on the absorption difference between the halohydrin para-nitro-2-bromo-1-phenylethanol and the epoxide para-nitrostyrene oxide was developed. The enantioselectivity of ring-closure reactions catalysed by three different halohydrin dehalogenases could be estimated from the shape of progress curves. Evaluation of ring-opening reactions catalysed by halohydrin dehalogenase from Agrobacterium radiobacter AD1 established that, in addition to Cl − and Br − , nucleophiles such as N 3 − , CN − and NO 2 − are also accepted for the ring opening of para-nitrostyrene oxide. The ring-opening reactions with these nucleophiles resulted in highly enantioselective kinetic resolutions, which expands the scope of synthetically valuable conversions catalysed by a halohydrin dehalogenase.

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confidence: 99%

Exploration of the biocatalytic potential of a halohydrin dehalogenase using chromogenic substrates

Spelberg

Tang

Gelder

et al. 2002

Tetrahedron: Asymmetry

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“…It also reduce the in‰uence by other nucleophilic groups in the microorganisms which may aŠect ring-open of the epoxides. 22) Biomass (20 g wet) of the A. niger CGMCC 0496 fungus was suspended in a 500-ml three-necked, round-bottomed ‰ask which wasˆlled with 100 ml of a 0.1 M sodium phosphate buŠer (pH 8). The ‰ask was equipped with a mechanical stirrer while keeping the temperature at 259 C. Epoxide (±)-1 (100 mg) was added to the suspension as a solution in DMF (5 ml), and the mixture was stirred at 600 rpm.…”

Section: )mentioning

confidence: 99%

Enantioselective Hydrolysis ofo-Nitrostyrene Oxide by Whole Cells ofAspergillus nigerCGMCC 0496

Jin

2002

Bioscience, Biotechnology, and Biochemistry

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“…[10] Increasing attention has been paid to the potential use of epoxide hydrolases in the biocatalytic production of enantiopure epoxides from racemates. [11] It was shown that liver microsomes could be used for the stereoselective ring opening of epoxides with amines. [12] More recently, it has been reported that some commercially available lipases, such as porcine pancreatic lipase, which is available on a preparative scale, catalyzed the enantioselective ring opening of epoxides with 2-propylamine.…”

Section: Introductionmentioning

confidence: 99%

Enzymatic Ring‐Opening Polymerization of Oxiranes and Dicarboxylic Anhydrides

Soeda¹,

Okamoto²,

Toshima³

et al. 2002

Macromolecular Bioscience

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Oxiranes, such as glycidyl phenyl ether, benzyl glycidate, glycidyl methyl ether, and styrene oxide, were copolymerized with dicarboxylic anhydrides, such as succinic anhydride, phthalic anhydride, and maleic anhydride, by the action of an enzyme in a stepwise reaction to produce the corresponding polyesters containing some ether linkages having a maximum Mw of 13 500. Oxiranes, such as glycidol and glycidyl phenyl ether, were also homopolymerized and copolymerized with other oxiranes by the enzyme to produce the corresponding polyethers.Enzymatic polymerization of oxiranes and dicarboxylic anhydrides.magnified imageEnzymatic polymerization of oxiranes and dicarboxylic anhydrides.

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Epoxide hydrolases as asymmetric catalysts

Cited by 113 publications

References 93 publications

Exploration of the biocatalytic potential of a halohydrin dehalogenase using chromogenic substrates

Exploration of the biocatalytic potential of a halohydrin dehalogenase using chromogenic substrates

Enantioselective Hydrolysis ofo-Nitrostyrene Oxide by Whole Cells ofAspergillus nigerCGMCC 0496

Enzymatic Ring‐Opening Polymerization of Oxiranes and Dicarboxylic Anhydrides

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