alexa Characterization Of The Pesticide Detoxifying Enzyme CdGSTM1-1 By Kinetic Analysis And Differential Scanning Fluorimetry
ISSN: 2150-3494

Chemical Sciences Journal
Open Access

OMICS International organises 3000+ Global Conferenceseries Events every year across USA, Europe & Asia with support from 1000 more scientific Societies and Publishes 700+ Open Access Journals which contains over 50000 eminent personalities, reputed scientists as editorial board members.

Open Access Journals gaining more Readers and Citations

700 Journals and 15,000,000 Readers Each Journal is getting 25,000+ Readers

This Readership is 10 times more when compared to other Subscription Journals (Source: Google Analytics)

Share This Page

Additional Info

Loading Please wait..

4th European Chemistry Congress
May 11-13, 2017 Barcelona, Spain

Fereniki Perperopoulou, Farid Ataya and Nikolaos E Labrou
Agricultural University of Athens, Greece
College of Science King Saud University, Saudi Arabia
Posters & Accepted Abstracts: Chem Sci J
DOI: 10.4172/2150-3494-C1-009
Glutathione transferases (GSTs, EC. form a large group of multifunctional enzymes, best known for their involvement in the metabolism and inactivation of a wide range of xenobiotic compounds. GSTs catalyze the nucleophilic attack of the reduced form of glutathione (γ-L-Glu-L-Cys-Gly, GSH) on the electrophilic center of a variety of compounds such as pesticides, herbicides etc. The conjugation of GSH to such molecules results in the increase of their solubility and the reduction of their toxicity. GSTs are useful tools with a variety of biotechnological applications in many fields. The natural ability of the GSTs to interact with xenobiotic compounds gives the opportunity to develop enzyme biosensors for the simple and direct monitoring of environmental pollutants. In the present work we report the cloning, kinetic and structural characterization of the GSTM1-1 from camel (Camelus dromedarius) as well as a screening method to identify ligands that bind the protein. The CdGSΤM1-1 enzyme was expressed in E. coli and purified by affinity chromatography. The ligandin function of the enzyme was evaluated by measuring the ability of forty seven xenobiotic compounds to bind and inhibit enzyme activity. The inhibition potency was measured with the CDNB/GSH assay system. The IC50 value and the kinetic analysis of the compound that showed the highest inhibition were determined. The results showed that the enzyme exhibits high selectivity towards the fungicide zoxium zoxamide. The thermodynamic stability of CdGSTM1-1 and the influence of zoxium zoxamide were investigated using the differential scanning fluorimetry (DSF). The results are explored for the development of an optical biosensor for the determination of zoxium zoxamide in environmental samples.

Fereniki Perperopoulou studied Agricultural Biotechnology at the Agricultural University of Athens. She remained at the Agricultural Biotechnology Department of the Agricultural University of Athens, where she earned a master's degree on "Bioactive Protein Products & Technology". From 2014 to date she is a PhD candidate at the Department of Biotechnology (Agricultural University of Athens), working on the subject "Protein engineering and molecular study of transferase glutathione", for which she has been awarded a scholarship under the scheme research projects for excellence iky/siemens.

Email: [email protected]

image PDF   |   image HTML

Relevant Topics

Peer Reviewed Journals
Make the best use of Scientific Research and information from our 700 + peer reviewed, Open Access Journals
International Conferences 2017-18
Meet Inspiring Speakers and Experts at our 3000+ Global Annual Meetings

Contact Us

© 2008-2017 OMICS International - Open Access Publisher. Best viewed in Mozilla Firefox | Google Chrome | Above IE 7.0 version