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Exit of products from the active site of human glutathione transferase P1-1 is promoted by valine 10

Conference Paper


Abstract


  • In search of potential residues involved in co-substrate recognition or product dissociation we have probed the electrophilic binding site (H-site) of human placental glutathione transferase (GST P1-1) by mutating two valines (Val 10 and Val 35) into glycine and alanine, respectively. The results demonstrate that Val35Ala behaves similar to wild type, whereas Val10Gly exhibits a strong decrease of kcat towards two selected co-substrates, ethacrynic acid and 1-chloro-2,4-dinitrobenzene. Kinetic, spectroscopic and crystallographic analysis of the Val10Gly mutant enzyme indicate that Val 10, located on the floor of the H-site, may orient products and help them to leave the active site. © 2001 Elsevier Science Ireland Ltd. All rights reserved.

Publication Date


  • 2001

Citation


  • Micaloni, C., Mazzetti, A. P., Nuccetelli, M., Rossjohn, J., McKinstry, W. J., Antonini, G., . . . Lo Bello, M. (2001). Exit of products from the active site of human glutathione transferase P1-1 is promoted by valine 10. In Chemico-Biological Interactions Vol. 133 (pp. 192-195).

Scopus Eid


  • 2-s2.0-0003129127

Start Page


  • 192

End Page


  • 195

Volume


  • 133

Issue


  • 1-3

Abstract


  • In search of potential residues involved in co-substrate recognition or product dissociation we have probed the electrophilic binding site (H-site) of human placental glutathione transferase (GST P1-1) by mutating two valines (Val 10 and Val 35) into glycine and alanine, respectively. The results demonstrate that Val35Ala behaves similar to wild type, whereas Val10Gly exhibits a strong decrease of kcat towards two selected co-substrates, ethacrynic acid and 1-chloro-2,4-dinitrobenzene. Kinetic, spectroscopic and crystallographic analysis of the Val10Gly mutant enzyme indicate that Val 10, located on the floor of the H-site, may orient products and help them to leave the active site. © 2001 Elsevier Science Ireland Ltd. All rights reserved.

Publication Date


  • 2001

Citation


  • Micaloni, C., Mazzetti, A. P., Nuccetelli, M., Rossjohn, J., McKinstry, W. J., Antonini, G., . . . Lo Bello, M. (2001). Exit of products from the active site of human glutathione transferase P1-1 is promoted by valine 10. In Chemico-Biological Interactions Vol. 133 (pp. 192-195).

Scopus Eid


  • 2-s2.0-0003129127

Start Page


  • 192

End Page


  • 195

Volume


  • 133

Issue


  • 1-3