5 results about "Epoxide metabolism" patented technology

This invention discloses a method for preparing 1,2-pentanediol, comprising using 2-pentanone as a substrate, adding 2-keto reductase, linalool dehydratase, formate dehydrogenase, lysozyme, coenzyme NAD+, and water to react and obtain n-pentene. The obtained n-pentene is then thoroughly mixed with ethanol. This mixture is then fed into a reaction system containing olefin monooxygenase, epoxide hydrolase, formate dehydrogenase, lysozyme, coenzyme NAD+, MgSO4, and water using a fed-batch method. After the n-pentene and ethanol mixture has been completely added, the reaction continues for a period of time, followed by extraction to obtain 1,2-pentanediol. This preparation method uses 2-pentanone as a raw material, catalyzing the synthesis of 2-pentanol via 2-keto reductase. 2-pentanol is then catalyzed by a dehydrating enzyme to generate n-pentene, which is then catalyzed by an olefin monooxygenase to generate 1,2-epoxypentane. Finally, epoxide hydrolase ring-opens the 1,2-pentanediol. This process requires only four enzymatic catalytic reactions for efficient synthesis.

The application provides a stilbene compound, a pharmaceutical composition and application thereof, relates to the technical field of medicinal chemistry, and the main skeleton of the compound is a stilbene with a urea group; a series of high-activity stilbene compounds are obtained by expanding different substituents on both sides of the urea group and synthesizing a stilbene side skeleton containing an advantage structure of a natural product; the IC50 value of the high-activity stilbene compound to soluble epoxide hydrolase inhibition reaches the nanomolar level, indicating that the stilbene compound has a high inhibition effect on soluble epoxide hydrolase inhibition enzyme, so that the inhibition effect on inflammation can be realized by inhibiting soluble epoxide hydrolase inhibition enzyme, and the stilbene compound has a good application prospect.

This application discloses an epoxide hydrolase gene cloned from Angelica dahurica. AdEH1 and AdEH2 and its encoded proteins and applications, among which, AdEH 1 and AdEH2 The nucleotide sequences are shown in SEQ ID NO: 1 and SEQ ID NO: 2, respectively, and the amino acid sequences encoding the proteins are shown in SEQ ID NO: 3 and SEQ ID NO: 4, respectively. AdEH1 and AdEH2 The encoded protein possesses epoxide hydrolase catalytic activity, capable of catalyzing the oxidation of imperatorin and angelica root to produce hydrated oxidized imperatorin and angelica root. This application identifies the gene. AdEH1 and AdEH2 Its key role in the biosynthesis of furanocoumarins provides core gene resources for the regulation and green large-scale synthesis of furanocoumarin components in Angelica dahurica, and also provides technical support for the accurate detection of related compounds.

This invention relates to the field of pharmaceutical technology, providing memantine derivatives, their preparation methods, and their application in the preparation of drugs for treating soluble cyclooxygenase-mediated diseases. The memantine derivatives provided by this invention have typical urea or amide structures. The urea and amide structures serve as the primary pharmacophores of sEH (hydrophobic epoxide hemoglobin). The memantine moiety, as a hydrophobic segment, interacts with the receptor hydrophobically. Molecular docking shows that the memantine moiety, as a hydrophobic segment, interacts with the receptor hydrophobically, particularly when both R1 and R2 are methyl groups, which enhances the van der Waals forces. Therefore, the memantine derivatives provided by this invention exhibit high inhibitory activity against human (HsEH) and murine sEH (MsEH), and can be used as sEH inhibitors in the preparation of drugs for treating soluble cyclooxygenase-mediated diseases, showing broad application prospects.

This invention discloses an epoxide hydrolase mutant, biomaterials, products, and applications. Compared to the wild-type epoxide hydrolase, this mutant possesses one or more amino acid residue mutations at positions 108, 131, and 256. The catalytic activity of this series of mutants is significantly improved compared to the wild-type enzyme, with the most preferred mutant being F108V / D131N / E256V. (S) - Epoxyphenylethane formation (S) When synthesizing 1,2-ethylene glycol, the yield can reach 93% under optimal reaction conditions. Furthermore, the reaction conditions for the catalytic synthesis of chiral 1,2-ethylene glycol using this series of mutants are mild, and the production process is environmentally friendly, demonstrating excellent industrial application value.