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Epoxide Hydrolases: Multipotential Biocatalysts. [PDF]

open access: yesInt J Mol Sci, 2023
Epoxide hydrolases are attractive and industrially important biocatalysts. They can catalyze the enantioselective hydrolysis of epoxides to the corresponding diols as chiral building blocks for bioactive compounds and drugs. In this review article, we discuss the state of the art and development potential of epoxide hydrolases as biocatalysts based on ...
Bučko M   +4 more
europepmc   +3 more sources

Role of epoxide hydrolases in lipid metabolism. [PDF]

open access: yesBiochimie, 2013
Epoxide hydrolases (EH), enzymes present in all living organisms, transform epoxide-containing lipids to 1,2-diols by the addition of a molecule of water. Many of these oxygenated lipid substrates have potent biological activities: host defense, control of development, regulation of blood pressure, inflammation, and pain. In general, the bioactivity of
Morisseau C.
europepmc   +5 more sources

Soluble Epoxide Hydrolase in Atherosclerosis [PDF]

open access: yesCurrent Atherosclerosis Reports, 2010
Like many eicosanoids, epoxyeicosatrienoic acids (EETs) have multiple biological functions, including reduction of blood pressure, inflammation, and atherosclerosis in multiple species. Hydration of EETs by the soluble epoxide hydrolase (sEH) is the major route of their degradation to the less bioactive diols.
Wang, Yi-Xin Jim   +3 more
openaire   +5 more sources

The crystal structure of mycobacterial epoxide hydrolase A [PDF]

open access: yesScientific Reports, 2020
AbstractThe human pathogen Mycobacterium tuberculosis is the causative agent of tuberculosis resulting in over 1 million fatalities every year, despite decades of research into the development of new anti-TB compounds. Unlike most other organisms M. tuberculosis has six putative genes for epoxide hydrolases (EH) of the α/β-hydrolase family with little ...
Boris Krichel   +9 more
openaire   +5 more sources

Cholesterol epoxide hydrolase and cancer

open access: yesCurrent Opinion in Pharmacology, 2012
Cholesterol epoxide hydrolase (ChEH) catalyzes the hydration of cholesterol-5,6-epoxides (5,6-EC) into cholestane-3β,5α,6β-triol. ChEH is a hetero-oligomeric complex called the anti-estrogen binding site (AEBS) comprising 3β-hydroxysterol-Δ(8)-Δ(7)-isomerase (D8D7I) and 3β-hydroxysterol-Δ(7)-reductase (DHCR7).
Silvente-Poirot, Sandrine, Poirot, Marc
openaire   +4 more sources

Microsomal epoxide hydrolase polymorphisms

open access: yesMolecular Medicine Reports, 2010
Microsomal epoxide hydrolase plays a dual role in the activation and detoxification of carcinogenic compounds. Two polymorphic sites have been described in exons 3 and 4 of the microsomal epoxide hydrolase gene that change tyrosine residue 113 to histidine (Tyr113His) and histidine 139 to arginine (His139Arg), respectively.
Pinarbasi, Hatice   +2 more
openaire   +6 more sources

Epoxides and Soluble Epoxide Hydrolase in Cardiovascular Physiology [PDF]

open access: yesPhysiological Reviews, 2012
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.
openaire   +3 more sources

Visualization of a Covalent Intermediate between Microsomal Epoxide Hydrolase, but not Cholesterol Epoxide Hydrolase, and their Substrates [PDF]

open access: yesEuropean Journal of Biochemistry, 1997
Mammalian soluble and microsomal epoxide hydrolases have been proposed to belong to the family of αlβ‐hydrolase‐fold enzymes. These enzymes hydrolyse their substrates by a catalytic triad, with the first step of the enzymatic reaction being the formation of a covalent enzyme‐substrate ester. In the present paper, we describe the direct visualization of
Müller, F   +10 more
openaire   +3 more sources

Catalysis of potato epoxide hydrolase, StEH1 [PDF]

open access: yesBiochemical Journal, 2005
The kinetic mechanism of epoxide hydrolase (EC 3.3.2.3) from potato, StEH1 (Solanum tuberosum epoxide hydrolase 1), was studied by presteady-state and steady-state kinetics as well as by pH dependence of activity. The specific activities towards the different enantiomers of TSO (trans-stilbene oxide) as substrate were 43 and 3 μmol·min−1·mg−1 with the ...
Mikael Widersten, Lisa T. Elfström
openaire   +3 more sources

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