eng URI http://hdl.handle.net/10795/2672 ένζυμο βιοχημεία βιοτεχνολογία Glutathione transferases (EC 2.5.1.18, GSTs) catalyze the nucleophilic attack of glutathione (GSH) on the electrophilic centre of a number of electrophilic compounds helping to detoxify a diverse array of toxic xenobiotics including carcinogenic, and pharmacologically active compounds. In this review, detailed descriptions are given on the structure and catalytic properties of human glutathione transferase P1-1 (hGSTP1-1) an enzyme that ubiquitously expressed in human tissues and exhibits many biological functions and multiple roles. The detoxification properties of hGSTP1-1 have been a primary research focus for the last years. However, now it has become apparent that the noncatalytic functions of GSTP1-1 have expanded the biological roles of this enzyme in cell survival, cell death and stress signalling mechanism. 11 pp. LOMv1.0 creator LOMv1.0 publisher LOMv1.0 Project Final Beneficiary LOMv1.0 Project Executing Organisation 2013-02 Digital Library of the Operational Programme "Education and Lifelong Learning" abstract types Text Glutathione transferases Cellular detoxification GTs Catalytic properties Structure Isoenzyme 977195 application/pdf http://repository.edulll.gr/edulll/bitstream/10795/2672/2/2672_Paper%206.pdf URI http://hdl.handle.net/10795/2672 LOMv1.0creator 2016-04-15T08:38:52Z LOMv1.0validator 2016-04-15T08:38:52Z LOMv1.0 gre no no Copyright EYD-EPEDBM (Operational Programme "Education and Lifelong Learning")