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Journal articles on the topic 'Epoxide hydrolase'

Author: Grafiati

Published: 4 June 2021

Last updated: 26 July 2025

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1

van Loo, Bert, Jaap Kingma, Michael Arand, Marcel G. Wubbolts, and Dick B. Janssen. "Diversity and Biocatalytic Potential of Epoxide Hydrolases Identified by Genome Analysis." Applied and Environmental Microbiology 72, no. 4 (2006): 2905–17. http://dx.doi.org/10.1128/aem.72.4.2905-2917.2006.

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ABSTRACT Epoxide hydrolases play an important role in the biodegradation of organic compounds and are potentially useful in enantioselective biocatalysis. An analysis of various genomic databases revealed that about 20% of sequenced organisms contain one or more putative epoxide hydrolase genes. They were found in all domains of life, and many fungi and actinobacteria contain several putative epoxide hydrolase-encoding genes. Multiple sequence alignments of epoxide hydrolases with other known and putative α/β-hydrolase fold enzymes that possess a nucleophilic aspartate revealed that these enzy

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2

Edqvist, J., and I. Farbos. "Characterization of a Euphorbia lagascae epoxide hydrolase gene that is induced early during germination." Biochemical Society Transactions 28, no. 6 (2000): 855–56. http://dx.doi.org/10.1042/bst0280855.

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In Euphorbia lagascae the major fatty acid in triacylglycerol is the epoxidated fatty acid vernolic acid (cis- 12-epoxyoctadeca-cis-9-enoic acid). The enzymic reactions occurring during the catabolism of epoxidated fatty acids during germination are not known, but it seems likely that the degradation requires the activity of an epoxide hydrolase. Epoxide hydrolases are a group of functionally related enzymes that catalyse the cofactor-independent hydrolysis of epoxides to their corresponding vicinal diols by the addition of a water molecule. Here we report the cloning and characterization of a

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3

van der Werf, Mariët J., Karin M. Overkamp, and Jan A. M. de Bont. "Limonene-1,2-Epoxide Hydrolase fromRhodococcus erythropolis DCL14 Belongs to a Novel Class of Epoxide Hydrolases." Journal of Bacteriology 180, no. 19 (1998): 5052–57. http://dx.doi.org/10.1128/jb.180.19.5052-5057.1998.

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ABSTRACT An epoxide hydrolase from Rhodococcus erythropolisDCL14 catalyzes the hydrolysis of limonene-1,2-epoxide to limonene-1,2-diol. The enzyme is induced when R. erythropolis is grown on monoterpenes, reflecting its role in the limonene degradation pathway of this microorganism. Limonene-1,2-epoxide hydrolase was purified to homogeneity. It is a monomeric cytoplasmic enzyme of 17 kDa, and its N-terminal amino acid sequence was determined. No cofactor was required for activity of this colorless enzyme. Maximal enzyme activity was measured at pH 7 and 50°C. None of the tested inhibitors or m

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4

McKay, J. A., R. J. Weaver, G. I. Murray, S. W. Ewen, W. T. Melvin, and M. D. Burke. "Localization of microsomal epoxide hydrolase in normal and neoplastic human kidney." Journal of Histochemistry & Cytochemistry 43, no. 6 (1995): 615–20. http://dx.doi.org/10.1177/43.6.7769232.

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Microsomal epoxide hydrolase is a xenobiotic metabolizing enzyme that catalyzes the conversion of toxic and carcinogenic epoxides to less toxic dihydrodiols. The cellular localization and distribution of microsomal epoxide hydrolase were investigated for the first time in normal and neoplastic human kidney. Light microscopic immunohistochemical studies using an alkaline phosphatase-anti-alkaline phosphatase technique showed that in normal kidney there was a wide distribution of epoxide hydrolase immunoreactivity. The main localization of epoxide hydrolase immunoreactivity was to the proximal a

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5

Serrano-Hervás, Eila, Marc Garcia-Borràs, and Sílvia Osuna. "Exploring the origins of selectivity in soluble epoxide hydrolase from Bacillus megaterium." Organic & Biomolecular Chemistry 15, no. 41 (2017): 8827–35. http://dx.doi.org/10.1039/c7ob01847a.

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Epoxide hydrolase (EH) enzymes catalyze the hydration of racemic epoxides to yield their corresponding vicinal diols. In this work, the Bacillus megaterium epoxide hydrolase (BmEH)-mediated hydrolysis of racemic styrene oxide (rac-SO) and its para-nitro styrene oxide (rac-p-NSO) derivative are computationally investigated using density functional theory (DFT).

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6

Wijekoon, C. P., P. H. Goodwin, and T. Hsiang. "The involvement of two epoxide hydrolase genes, NbEH1.1 and NbEH1.2, of Nicotiana benthamiana in the interaction with Colletotrichum destructivum, Colletotrichum orbiculare or Pseudomonas syringae pv. tabaci." Functional Plant Biology 35, no. 11 (2008): 1112. http://dx.doi.org/10.1071/fp08160.

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Epoxide hydrolase hydrates epoxides to vicinal diols in the phyto-oxylipin peroxygenase pathway resulting in the production of epoxy alcohols, dihydrodiols, triols and epoxides, including many lipid epoxides associated with resistance. Two epoxide hydrolase genes from Nicotiana benthamiana L., NbEH1.1 and NbEH1.2, were amplified from coding DNA of leaves during a susceptible response to the hemibiotrophic pathogens, Colletotrichum destructivum O’Gara, Colletotrichum orbiculare Berk. and Mont. von Arx. or Pseudomonas syringae pv. tabaci Wolf and Foster, or the hypersensitive resistance response

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7

Tormet-González, Gabriela D., Carolina Wilson, Gabriel Stephani de Oliveira, Jademilson Celestino dos Santos, Luciana G. de Oliveira, and Marcio Vinicius Bertacine Dias. "An epoxide hydrolase from endophytic Streptomyces shows unique structural features and wide biocatalytic activity." Acta Crystallographica Section D Structural Biology 76, no. 9 (2020): 868–75. http://dx.doi.org/10.1107/s2059798320010402.

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The genus Streptomyces is characterized by the production of a wide variety of secondary metabolites with remarkable biological activities and broad antibiotic capabilities. The presence of an unprecedented number of genes encoding hydrolytic enzymes with industrial appeal such as epoxide hydrolases (EHs) reveals its resourceful microscopic machinery. The whole-genome sequence of Streptomyces sp. CBMAI 2042, an endophytic actinobacterium isolated from Citrus sinensis branches, was explored by genome mining, and a putative α/β-epoxide hydrolase named B1EPH2 and encoded by 344 amino acids was se

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8

Madacki, Jan, Martin Kopál, Mary Jackson, and Jana Korduláková. "Mycobacterial Epoxide Hydrolase EphD Is Inhibited by Urea and Thiourea Derivatives." International Journal of Molecular Sciences 22, no. 6 (2021): 2884. http://dx.doi.org/10.3390/ijms22062884.

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The genome of the human intracellular pathogen Mycobacterium tuberculosis encodes an unusually large number of epoxide hydrolases, which are thought to be involved in lipid metabolism and detoxification reactions needed to endure the hostile environment of host macrophages. These enzymes therefore represent suitable targets for compounds such as urea derivatives, which are known inhibitors of soluble epoxide hydrolases. In this work, we studied in vitro the effect of the thiourea drug isoxyl on six epoxide hydrolases of M. tuberculosis using a fatty acid substrate. We show that one of the prot

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9

Yu, Zhigang, Benjamin B. Davis, Christophe Morisseau, et al. "Vascular localization of soluble epoxide hydrolase in the human kidney." American Journal of Physiology-Renal Physiology 286, no. 4 (2004): F720—F726. http://dx.doi.org/10.1152/ajprenal.00165.2003.

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Epoxyeicosatrienoic acids are cytochrome P-450 metabolites of arachidonic acid with multiple biological functions, including the regulation of vascular tone, renal tubular transport, cellular proliferation, and inflammation. Epoxyeicosatrienoic acids are converted by soluble epoxide hydrolase into the corresponding dihydroxyeicosatrienoic acids, and epoxyeicosatrienoic acid hydration is regarded as one mechanism whereby their biological effects are eliminated. Previous animal studies indicate that soluble epoxide hydrolase plays an important role in the regulation of renal eicosanoid levels an

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10

Otake, Shinya, Norihiro Ogawa, Yoshikazu Kitano, Keiji Hasumi, and Eriko Suzuki. "Isoprene Side-chain of SMTP is Essential for Soluble Epoxide Hydrolase Inhibition and Cellular Localization." Natural Product Communications 11, no. 2 (2016): 1934578X1601100. http://dx.doi.org/10.1177/1934578x1601100223.

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SMTPs, a family of natural small molecules that effectively treat ischemic stroke, are subject to clinical development. SMTPs enhance plasminogen activation and inhibit soluble epoxide hydrolase (sEH), leading to promotion of endogenous thrombolysis and anti-inflammation. The SMTP molecule consists of a tricyclic γ-lactam moiety, an isoprene side-chain, and an N-linked side-chain. Here, we investigate the yet-to-be-characterized function of the isoprene side-chain of SMTPs in sEH inhibition and cellular distribution. The results demonstrated that oxidative modification as well as truncation of

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11

Blée, Elizabeth, Stephan Summerer, Martine Flenet, Hélène Rogniaux, Alain Van Dorsselaer, and Francis Schuber. "Soybean Epoxide Hydrolase." Journal of Biological Chemistry 280, no. 8 (2004): 6479–87. http://dx.doi.org/10.1074/jbc.m411366200.

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12

Gupta, Nandita C., Catherine M. Davis, Jonathan W. Nelson, Jennifer M. Young, and Nabil J. Alkayed. "Soluble Epoxide Hydrolase." Arteriosclerosis, Thrombosis, and Vascular Biology 32, no. 8 (2012): 1936–42. http://dx.doi.org/10.1161/atvbaha.112.251520.

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13

Meijer, Johan, and Joseph W. Depierre. "Cytosolic epoxide hydrolase." Chemico-Biological Interactions 64, no. 3 (1988): 207–49. http://dx.doi.org/10.1016/0009-2797(88)90100-7.

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14

Sontakke, Pooja M., Suraj G. Malpani, Pooja R. Tange, MD Rayees Ahmad, and Vishweshwar M. Dharashive. "Soluble Epoxide Hydrolase." Asian Journal of Pharmaceutical Research and Development 12, no. 2 (2024): 87–95. http://dx.doi.org/10.22270/ajprd.v12i2.1369.

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Epoxyeicosatrienoic acids (EETs) have numerous cardiovascular benefits, including vasodilation, anti-inflammatory actions, and anti-migratory effects on vascular smooth muscle cells. However, sEH, an enzyme that breaks down EETs into diols, limits these benefits. The development of sEH inhibitors (sEHIs), particularly those based on 1,3-disubstituted urea, has shown promise in enhancing the therapeutic properties of EETs. These inhibitors are antihypertensive and anti-inflammatory and can protect the heart, brain, and kidneys from damage. While there are still challenges to overcome, such as i

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15

Yoshida, A., K. Murakami, H. Tsukamoto, et al. "AB0046 OMEGA-3 EPOXIDES AMELIORATE MURINE INFLAMMATORY ARTHRITIS." Annals of the Rheumatic Diseases 82, Suppl 1 (2023): 1202.1–1202. http://dx.doi.org/10.1136/annrheumdis-2023-eular.1614.

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BackgroundEpoxy fatty acids (EpFA), cytochrome P450(CYP)-mediated metabolites of polyunsaturated fatty acids (PUFA), have anti-inflammatory effects[1]. However, EpFA is quickly converted to an inactive form by the soluble epoxide hydrolase(sEH). In recent years, the efficacy of sEH inhibitors (sEHi) has been reported in a variety of diseases[2-4]. However, compared to ω-6 epoxides, such as epoxyeicosatirienioic acids (EET) derived from arachidonic acid (AA), there are few reports on ω-3 epoxides, epoxyeicosapentaenoic acid (EEQ) from eicosapentaenoic acid (EPA) and epoxydocosapentaenoic acids

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16

Jackson, M. R., and B. Burchell. "Expression of human liver epoxide hydrolase in Saccharomyces pombe." Biochemical Journal 251, no. 3 (1988): 931–33. http://dx.doi.org/10.1042/bj2510931.

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Human liver microsomal epoxide hydrolase cDNA was inserted into the yeast expression vector pEVP11. The resulting recombinant plasmid was introduced into Saccharomyces pombe. The epoxide hydrolase protein and enzymic activity was subsequently expressed and identified in the 105,000 g pellet after centrifugal fractionation of homogenized yeast cells. This method will provide a useful source of human liver epoxide hydrolase, avoiding the problems of obtaining human tissue.

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17

Ma, Liang, Hailing Zhao, Meijie Yu, et al. "Association of Epoxide Hydrolase 2 Gene Arg287Gln with the Risk for Primary Hypertension in Chinese." International Journal of Hypertension 2020 (February 28, 2020): 1–7. http://dx.doi.org/10.1155/2020/2351547.

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Background. Epoxide hydrolase 2 (EPHX2) gene coding for soluble epoxide hydrolase is a potential candidate in the pathogenesis of hypertension. Objectives. We aimed to assess the association of a missense mutation, R287Q, in EPHX2 gene with primary hypertension risk and examine its association with enzyme activity of soluble epoxide hydrolase. Methods. This study involved 782 patients with primary hypertension and 458 healthy controls. Genotyping was done using TaqMan technique. Activity of soluble epoxide hydrolase fusion proteins was evaluated by the conversion of 11,12-EET to corresponding

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18

Shao, Huanhuan, Pan Xu, Xiang Tao, et al. "Improving Hydrolytic Activity and Enantioselectivity of Epoxide Hydrolase from Phanerochaete chrysosporium by Directed Evolution." Molecules 29, no. 20 (2024): 4864. http://dx.doi.org/10.3390/molecules29204864.

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Epoxide hydrolases (EHs) catalyze the conversion of epoxides into vicinal diols. The epoxide hydrolase gene from P. chrysosporium was previously cloned and subjected to site-directed mutation to study its enzyme activity, but the results were unsatisfactory. This study used error prone PCR and DNA shuffling to construct a PchEHA mutation library. We performed mutation-site combinations on PchEHA based on enzyme activity measurement results combined with directed evolution technology. More than 15,000 mutants were randomly selected for the preliminary screening of PchEHA enzyme activity alongsi

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19

Imig, John D. "Epoxides and Soluble Epoxide Hydrolase in Cardiovascular Physiology." Physiological Reviews 92, no. 1 (2012): 101–30. http://dx.doi.org/10.1152/physrev.00021.2011.

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Epoxyeicosatrienoic acids (EETs) are arachidonic acid metabolites that importantly contribute to vascular and cardiac physiology. The contribution of EETs to vascular and cardiac function is further influenced by soluble epoxide hydrolase (sEH) that degrades EETs to diols. Vascular actions of EETs include dilation and angiogenesis. EETs also decrease inflammation and platelet aggregation and in general act to maintain vascular homeostasis. Myocyte contraction and increased coronary blood flow are the two primary EET actions in the heart. EET cell signaling mechanisms are tissue and organ speci

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20

Mayer, Sandra F., Harald Mang, Andreas Steinreiber, Robert Saf, and Kurt Faber. "Asymmetric total synthesis of (+)-exo-brevicomin based on enantioconvergent biocatalytic hydrolysis of an alkene-functionalized 2,3-disubstituted epoxide." Canadian Journal of Chemistry 80, no. 4 (2002): 362–69. http://dx.doi.org/10.1139/v02-037.

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A short total asymmetric synthesis of (+)-exo- and ()-endo-brevicomin ((+)-exo-3 and ()-endo-3), which are components of the attracting pheromone system of several bark-beetle species belonging to the genera Dendroctonus and Dryocoetes, was accomplished via a chemoenzymatic protocol. The key step consisted of biocatalytic hydrolysis by bacterial epoxide hydrolases of cis-configured 2,3-disubstituted oxiranes bearing olefinic side chains. This reaction proceeded in an enantioconvergent fashion, by affording a single enantiomeric vic-diol from the rac-epoxide in up to 92% ee and 83% isolated y

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21

Klingler, Franca-Maria, Markus Wolf, Sandra Wittmann, Philip Gribbon, and Ewgenij Proschak. "Bacterial Expression and HTS Assessment of Soluble Epoxide Hydrolase Phosphatase." Journal of Biomolecular Screening 21, no. 7 (2016): 689–94. http://dx.doi.org/10.1177/1087057116637609.

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Soluble epoxide hydrolase (sEH) is a bifunctional enzyme that possesses an epoxide hydrolase and lipid phosphatase activity (sEH-P) at two distinct catalytic domains. While the physiological role of the epoxide hydrolase domain is well understood, the consequences of the phosphatase activity remain unclear. Herein we describe the bacterial expression of the recombinant N-terminal domain of sEH-P and the development of a high-throughput screening protocol using a sensitive and commercially available substrate fluorescein diphosphate. The usability of the assay system was demonstrated and novel

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22

Oh, Young Taek, Jun Yang, Christophe Morisseau, Qiyi He, Bruce Hammock, and Jang H. Youn. "Effects of Individual Circulating FFAs on Plasma and Hepatic FFA Epoxides, Diols, and Epoxide-Diol Ratios as Indices of Soluble Epoxide Hydrolase Activity." International Journal of Molecular Sciences 24, no. 13 (2023): 10760. http://dx.doi.org/10.3390/ijms241310760.

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Oxylipins, oxidation products of unsaturated free fatty acids (FFAs), are involved in various cellular signaling systems. Among these oxylipins, FFA epoxides are associated with beneficial effects in metabolic and cardiovascular health. FFA epoxides are metabolized to diols, which are usually biologically less active, by soluble epoxide hydrolase (sEH). Plasma epoxide-diol ratios have been used as indirect measures of sEH activity. This study was designed to examine the effects of acute elevation of individual plasma FFAs on a variety of oxylipins, particularly epoxides, diols, and their ratio

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23

FUKASAWA, Kayoko M., Katsuhiko FUKASAWA, Minoru HARADA, Junzo HIROSE, Takashi IZUMI, and Takao SHIMIZU. "Aminopeptidase B is structurally related to leukotriene-A4 hydrolase but is not a bifunctional enzyme with epoxide hydrolase activity." Biochemical Journal 339, no. 3 (1999): 497–502. http://dx.doi.org/10.1042/bj3390497.

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Aminopeptidase B (Ap B; EC 3.4.11.6) is a zinc-binding protein that contains the consensus sequence HEXXHX18E (324-347), conserved among the M1 family of metallopeptidases. To determine if these putative zinc-binding residues (His324, His328 and Glu347) and the active-site Glu325 are essential for the enzyme activity, we replaced the histidines with tyrosines and the glutamic acid residues with alanines using site-directed mutagenesis. The cDNAs were expressed in Escherichia coli, and the resulting recombinant proteins, named H324Y, E325A, H328Y and E347A, were purified to apparent homogeneity

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Choi, Won Jae, and Cha Yong Choi. "Production of chiral epoxides: Epoxide hydrolase-catalyzed enantioselective hydrolysis." Biotechnology and Bioprocess Engineering 10, no. 3 (2005): 167–79. http://dx.doi.org/10.1007/bf02932009.

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Dietze, Eric C., Eiichi Kuwano, and Bruce D. Hammock. "The interaction of cytosolic epoxide hydrolase with chiral epoxides." International Journal of Biochemistry 25, no. 1 (1993): 43–52. http://dx.doi.org/10.1016/0020-711x(93)90488-z.

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Visser, Hans, Jan A. M. de Bont, and Jan C. Verdoes. "Isolation and Characterization of the Epoxide Hydrolase-Encoding Gene from Xanthophyllomyces dendrorhous." Applied and Environmental Microbiology 65, no. 12 (1999): 5459–63. http://dx.doi.org/10.1128/aem.65.12.5459-5463.1999.

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ABSTRACT The epoxide hydrolase (EH)-encoding gene (EPH1) from the basidiomycetous yeast Xanthophyllomyces dendrorhous was isolated. The genomic sequence has a 1,236-bp open reading frame which is interrupted by eight introns that encode a 411-amino-acid polypeptide with a calculated molecular mass of 46.2 kDa. The amino acid sequence is similar to that of microsomal EH and belongs to the α/β hydrolase fold family. The EPH1 gene was not essential for growth of X. dendrorhous in rich medium under laboratory conditions. The Eph1-encoding cDNA was functionally expressed in Escherichia coli. A sixf

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27

Weintraub, Neal L., Xiang Fang, Terry L. Kaduce, Mike VanRollins, Papri Chatterjee, and Arthur A. Spector. "Epoxide hydrolases regulate epoxyeicosatrienoic acid incorporation into coronary endothelial phospholipids." American Journal of Physiology-Heart and Circulatory Physiology 277, no. 5 (1999): H2098—H2108. http://dx.doi.org/10.1152/ajpheart.1999.277.5.h2098.

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Cytochrome P-450-derived epoxyeicosatrienoic acids (EETs) are avidly incorporated into and released from endothelial phospholipids, a process that results in potentiation of endothelium-dependent relaxation. EETs are also rapidly converted by epoxide hydrolases to dihydroxyeicosatrienoic acid (DHETs), which are incorporated into phospholipids to a lesser extent than EETs. We hypothesized that epoxide hydrolases functionally regulate EET incorporation into endothelial phospholipids. Porcine coronary artery endothelial cells were treated with an epoxide hydrolase inhibitor, 4-phenylchalcone oxid

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Meijer, Johan, Joseph W. DePierre, and Hans Jörnvall. "Cytosolic epoxide hydrolase from liver of control and clofibrate-treated mice. Structural comparison by HPLC peptide mapping." Bioscience Reports 7, no. 11 (1987): 891–96. http://dx.doi.org/10.1007/bf01119480.

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Cytosolic epoxide hydrolases purified from livers of control and clofibrate-induced male C57B1/6 mice were compared. The proteins were reduced, alkylated and cleaved with trypsin and chymotrypsin. The digests were analyzed by HPLC and no qualitative differences were observed in the peptide mapping profiles of the two types of epoxide hydrolase preparation. The amino acid compositions and N-terminal residues of selected tryptic peptides also gave identical results for the control and clofibrate-induced mice. Both intact proteins have e-amino-blocked N-termini. The two enzyme forms are concluded

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Wojtasek, Hubert, and Glenn D. Prestwich. "An Insect Juvenile Hormone-Specific Epoxide Hydrolase Is Related to Vertebrate Microsomal Epoxide Hydrolases." Biochemical and Biophysical Research Communications 220, no. 2 (1996): 323–29. http://dx.doi.org/10.1006/bbrc.1996.0404.

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Simard, Adam, Kelli Hvorecny, Noor Taher, et al. "Allosteric and Cooperative Networks in a Homodimeric Epoxide Hydrolase." Structural Dynamics 12, no. 2_Supplement (2025): A381. https://doi.org/10.1063/4.0000687.

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Cif is a homodimeric epoxide hydrolase produced by the opportunistic pathogen Pseudomonas aeruginosa, a species of bacteria commonly found in the lungs of patients with the disease Cystic Fibrosis (CF). Cif targets cellular epoxides, exerting a bifurcated virulence pathway that causes both premature degradation of the ion channel CFTR and hyperinflammation (1,2). The convergence of these pathways exacerbates the pulmonary pathophysiological complications associated with CF. To address Cif's effects on the patient population, we investigated Cif's hydrolysis of physiological substrates identify

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Smit, M., and M. Labuschagne. "Diversity of Epoxide Hydrolase Biocatalysts." Current Organic Chemistry 10, no. 10 (2006): 1145–61. http://dx.doi.org/10.2174/138527206777698101.

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Borhan, Babak, A. Daniel Jones, Franck Pinot, David F. Grant, Mark J. Kurth, and Bruce D. Hammock. "Mechanism of Soluble Epoxide Hydrolase." Journal of Biological Chemistry 270, no. 45 (1995): 26923–30. http://dx.doi.org/10.1074/jbc.270.45.26923.

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Craft, John A., Susan Baird, Michelle Lament, and Brian Burchell. "Membrane topology of epoxide hydrolase." Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism 1046, no. 1 (1990): 32–39. http://dx.doi.org/10.1016/0005-2760(90)90091-b.

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34

Pacifici, GM, M. Franchi, C. Bencini, and A. Rane. "Valpromide inhibits human epoxide hydrolase." British Journal of Clinical Pharmacology 22, no. 3 (1986): 269–74. http://dx.doi.org/10.1111/j.1365-2125.1986.tb02886.x.

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Wang, Yi-Xin Jim, Arzu Ulu, Le-Ning Zhang, and Bruce Hammock. "Soluble Epoxide Hydrolase in Atherosclerosis." Current Atherosclerosis Reports 12, no. 3 (2010): 174–83. http://dx.doi.org/10.1007/s11883-010-0108-5.

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Silvente-Poirot, Sandrine, and Marc Poirot. "Cholesterol epoxide hydrolase and cancer." Current Opinion in Pharmacology 12, no. 6 (2012): 696–703. http://dx.doi.org/10.1016/j.coph.2012.07.007.

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37

Wang, Jisheng, Mengying Zhang, Hongtuo Fu, et al. "Regulation Roles of Juvenile Hormone Epoxide Hydrolase Gene 2 in the Female River Prawn Macrobrachium nipponense Reproductive Process." Current Issues in Molecular Biology 46, no. 12 (2024): 13456–70. http://dx.doi.org/10.3390/cimb46120803.

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In this study, we investigated the regulatory roles of the juvenile hormone epoxide hydrolase (JHEH) gene in the reproductive process of female Macrobrachium nipponense. Its total cDNA length was 1848 bp, encoding for 460 amino acids. It contained conserved domains typical of epoxide hydrolases, such as the Abhydrolase family domain, the EHN epoxide hydrolase superfamily domain, and the “WWG” and “HGWP” motifs. The qPCR results showed that the expression of Mn-JHEH was the highest in hepatopancreas. Mn-JHEH was expressed at all stages of the embryonic and larval stages. The expression of Mn-JH

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Doderer, Kai, Sabine Lutz-Wahl, Bernhard Hauer, and Rolf D. Schmid. "Spectrophotometric assay for epoxide hydrolase activity toward any epoxide." Analytical Biochemistry 321, no. 1 (2003): 131–34. http://dx.doi.org/10.1016/s0003-2697(03)00399-3.

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39

Haeggström, Jesper Z., Anders Wetterholm, Bert L. Vallee, and Bengt Samuelsson. "Leukotriene A4 hydrolase: An epoxide hydrolase with peptidase activity." Biochemical and Biophysical Research Communications 173, no. 1 (1990): 431–37. http://dx.doi.org/10.1016/s0006-291x(05)81076-9.

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Nelson, Jonathan W., Rishi M. Subrahmanyan, Sol A. Summers, Xiangshu Xiao, and Nabil J. Alkayed. "Soluble Epoxide Hydrolase Dimerization Is Required for Hydrolase Activity." Journal of Biological Chemistry 288, no. 11 (2013): 7697–703. http://dx.doi.org/10.1074/jbc.m112.429258.

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Hu, Die, Xun-Cheng Zong, Feng Xue, Chuang Li, Bo-Chun Hu, and Min-Chen Wu. "Manipulating regioselectivity of an epoxide hydrolase for single enzymatic synthesis of (R)-1,2-diols from racemic epoxides." Chemical Communications 56, no. 18 (2020): 2799–802. http://dx.doi.org/10.1039/d0cc00283f.

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Friedberg, T., B. Löllmann, R. Becker, R. Holler, and F. Oesch. "The microsomal epoxide hydrolase has a single membrane signal anchor sequence which is dispensable for the catalytic activity of this protein." Biochemical Journal 303, no. 3 (1994): 967–72. http://dx.doi.org/10.1042/bj3030967.

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The microsomal epoxide hydrolase (mEH) catalyses the hydrolysis of reactive epoxides which are formed by the action of cytochromes P-450 from xenobiotics. In addition it has been suggested that mEH might mediate the transport of bile acids. For the mEH it has been shown that it is co-translationally inserted into the endoplasmic reticulum. Here we demonstrate that the N-terminal 20 amino acid residues of this protein serve as its single membrane anchor signal sequence and that the function of this sequence can also be supplied by a cytochrome P-450 (CYP2B1) anchor signal sequence. The evidence

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He, Xin, Wen-Yu Zhao, Bo Shao, et al. "Natural soluble epoxide hydrolase inhibitors from Inula helenium and their interactions with soluble epoxide hydrolase." International Journal of Biological Macromolecules 158 (September 2020): 1362–68. http://dx.doi.org/10.1016/j.ijbiomac.2020.04.227.

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Watabe, Tadashi, Naoki Ozawa, Hiroaki Ishii, Koji Chiba, and Akira Hiratsuka. "Hepatic microsomal cholesterol epoxide hydrolase: Selective inhibition by detergents and separation from xenobiotic epoxide hydrolase." Biochemical and Biophysical Research Communications 140, no. 2 (1986): 632–37. http://dx.doi.org/10.1016/0006-291x(86)90778-3.

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Kesavan, Rushendhiran, Timo Frömel, Sven Zukunft, et al. "The Consequences of Soluble Epoxide Hydrolase Deletion on Tumorigenesis and Metastasis in a Mouse Model of Breast Cancer." International Journal of Molecular Sciences 22, no. 13 (2021): 7120. http://dx.doi.org/10.3390/ijms22137120.

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Epoxides and diols of polyunsaturated fatty acids (PUFAs) are bioactive and can influence processes such as tumor cell proliferation and angiogenesis. Studies with inhibitors of the soluble epoxide hydrolase (sEH) in animals overexpressing cytochrome P450 enzymes or following the systemic administration of specific epoxides revealed a markedly increased incidence of tumor metastases. To determine whether PUFA epoxides increased metastases in a model of spontaneous breast cancer, sEH-/- mice were crossed onto the polyoma middle T oncogene (PyMT) background. We found that the deletion of the sEH

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Yamanashi, Haruto, William E. Boeglin, Christophe Morisseau, et al. "Catalytic activities of mammalian epoxide hydrolases with cis and trans fatty acid epoxides relevant to skin barrier function." Journal of Lipid Research 59, no. 4 (2018): 684–95. http://dx.doi.org/10.1194/jlr.m082701.

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Lipoxygenase (LOX)-catalyzed oxidation of the essential fatty acid, linoleate, represents a vital step in construction of the mammalian epidermal permeability barrier. Analysis of epidermal lipids indicates that linoleate is converted to a trihydroxy derivative by hydrolysis of an epoxy-hydroxy precursor. We evaluated different epoxide hydrolase (EH) enzymes in the hydrolysis of skin-relevant fatty acid epoxides and compared the products to those of acid-catalyzed hydrolysis. In the absence of enzyme, exposure to pH 5 or pH 6 at 37°C for 30 min hydrolyzed fatty acid allylic epoxyalcohols to fo

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de Bourg, Marcus, Abhishek Mishra, Rawand S. Mohammad, et al. "Synthetic Epoxyeicosatrienoic Acid Mimics Protect Mesangial Cells from Sorafenib-Induced Cell Death." Molecules 30, no. 7 (2025): 1445. https://doi.org/10.3390/molecules30071445.

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Nineteen potential mimics of 8,9-epoxyeicosatrienoic acid (8,9-EET), a natural bioactive oxylipin, were synthesized and evaluated for their ability to protect renal mesangial cells against sorafenib-induced cell death in a water-soluble tetrazolium (WST-8) assay. All compounds were also evaluated as inhibitors of soluble epoxide hydrolase. As expected of a potent pan-kinase inhibitor the drug sorafenib caused a significant decrease in cell viability in HRMCs. Several analogs containing amide and oxamide groups in place of the epoxide showed efficacy in reducing sorafenib induced human renal me

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Lee, Eun Yeol. "Epoxide hydrolase-mediated enantioconvergent bioconversions to prepare chiral epoxides and alcohols." Biotechnology Letters 30, no. 9 (2008): 1509–14. http://dx.doi.org/10.1007/s10529-008-9727-0.

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Anita, Natasha Z., and Walter Swardfager. "Soluble Epoxide Hydrolase and Diabetes Complications." International Journal of Molecular Sciences 23, no. 11 (2022): 6232. http://dx.doi.org/10.3390/ijms23116232.

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Type 2 diabetes mellitus (T2DM) can result in microvascular complications such as neuropathy, retinopathy, nephropathy, and cerebral small vessel disease, and contribute to macrovascular complications, such as heart failure, peripheral arterial disease, and large vessel stroke. T2DM also increases the risks of depression and dementia for reasons that remain largely unclear. Perturbations in the cytochrome P450-soluble epoxide hydrolase (CYP-sEH) pathway have been implicated in each of these diabetes complications. Here we review evidence from the clinical and animal literature suggesting the i

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Bellevik, Stefan, Jiaming Zhang, and Johan Meijer. "Brassica napus soluble epoxide hydrolase (BNSEH1)." European Journal of Biochemistry 269, no. 21 (2002): 5295–302. http://dx.doi.org/10.1046/j.1432-1033.2002.03247.x.

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