Expression and characterization of the novel human epoxide hydrolases EH 3 and EH 4

نویسندگان

  • Martina Marion Elisabeth Decker
  • Thierry Hennet
چکیده

s for posters:Experimental Biology 2008, San Diego, April 2008IDENTIFICATION OF A NEW POTENTIAL HUMAN EPOXIDE HYDROLASE(NEH2)Martina Decker, Magdalena Adamska, Michael Arand. Leopoldina Symposium of Lipid Signaling, Frankfurt, September 2008CHARACTERIZATION OF A NOVEL HUMAN EPOXIDE HYDROLASE (EH3)CAPABLE OF CONVERTING EPOXYEICOSATRIENOIC ACIDS (EETS)Martina Decker, Magdalena Adamska, Michael Arand. 11th International Winter Eicosanoid Conference, Baltimore, March 2009ACTIVITY OF A NOVEL EPOXIDE HYDROLASE 3 (EH3) TOWARDSARACHIDONIC ACID DERIVED SUBSTRATES IS AFFECTED BY AUDA APOTENT SOLUBLE EPOXIDE HYDROLASE INHIBITORMartina Decker, Magdalena Adamska, Annette Cronin and Michael Arand Presentations:XERR 9th Annual Meeting, 2008, ZurichCHARACTERIZATION AND INHIBITORY PROFILING OF NOVEL EPOXIDEHYDROLASE EH3 16. Toxikologisches und Pathologisches Kolloquium, 2009, BaselEPOXIDE HYDROLASES XENOBIOTIC METABOLIZERS OR PHYSIOLOGICALREGULATORS? Grants:SST, Swiss Society of Toxicology: Travel Grant 2009

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Enhancement of Soluble Expression and Biochemical Characterization of Two Epoxide Hydrolases from Bacillus

Background: Enantiopure epoxides are important intermediates in the synthesis of high-value chiral chemicals. Epoxide hydrolases have been exploited in biocatalysis for kinetic resolution of racemic epoxides to produce enantiopure epoxides and vicinal diols. It is necessary to obtain sufficient stable epoxide hydrolases with high enantioselectivity to meet the requirements of i...

متن کامل

Characterization of an epoxide hydrolase from the Florida red tide dinoflagellate, Karenia brevis.

Epoxide hydrolases (EH, EC 3.3.2.3) have been proposed to be key enzymes in the biosynthesis of polyether (PE) ladder compounds such as the brevetoxins which are produced by the dinoflagellate Karenia brevis. These enzymes have the potential to catalyze kinetically disfavored endo-tet cyclization reactions. Data mining of K. brevis transcriptome libraries revealed two classes of epoxide hydrola...

متن کامل

Multiple epoxide hydrolases in Alternaria alternata f. sp. lycopersici and their relationship to medium composition and host-specific toxin production.

The production of Alternaria alternata f. sp. lycopersici host-specific toxins (AAL toxins) and epoxide hydrolase (EH) activity were studied during the growth of this plant-pathogenic fungus in stationary liquid cultures. Media containing pectin as the primary carbon source displayed peaks of EH activity at day 4 and at day 12. When pectin was replaced by glucose, there was a single peak of EH ...

متن کامل

Microsomal and cytosolic epoxide hydrolases in rhesus monkey liver, and in normal and neoplastic human liver.

The cytosolic epoxide hydrolase (EH-LC) was observed in rhesus monkey liver cytosol, and in both normal and neoplastic human liver. Microsomal epoxide hydrolase (EH-LM) was detected not only in the microsomes of normal and neoplastic human liver and normal rhesus monkey liver, but also in the cytosol of these tissues. No apparent differences were observed between the EH-LM in liver cytosol and ...

متن کامل

Sequence and structure of epoxide hydrolases: a systematic analysis.

Epoxide hydrolases (EC 3.3.2.3) are ubiquitous enzymes that catalyze the hydrolysis of epoxides to the corresponding vicinal diols. More than 100 epoxide hydrolases (EH) have been identified or predicted, and 3 structures are available. Although they catalyze the same chemical reaction, sequence similarity is low. To identify conserved regions, all EHs were aligned. Phylogenetic analysis identi...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2017