IBR   13079
INSTITUTO DE BIOLOGIA MOLECULAR Y CELULAR DE ROSARIO
Unidad Ejecutora - UE
artículos
Título:
Metal-dependent inhibition of glyoxalase II: A possible mechanism to regulate the enzyme activity
Autor/es:
VALERIA A. CAMPOS-BERMUDEZ; JORGELINA MORÁN BARRIO; ANTONIO J. COSTA-FILHO; ALEJANDRO J. VILA
Revista:
JOURNAL OF INORGANIC BIOCHEMISTRY
Editorial:
ELSEVIER SCIENCE INC
Referencias:
Lugar: New York; Año: 2010 vol. 104 p. 726 - 731
ISSN:
0162-0134
Resumen:
Glyoxalase II (GLX2, EC 3.1.2.6., hydroxyacylglutathione hydrolase) is a metalloenzymeinvolved in crucial detoxification pathways. Different studies have failed in identifying the nativemetal ion of this enzyme, which is expressed with iron, zinc and/or manganese. Here we reportthat GloB, the GLX2 from Salmonella typhimurium, is differentially inhibited by glutathione (areaction product) depending on the bound metal ion, and we provide a structural model for thisinhibition mode. This metal-dependent inhibition was shown to occur in metal enriched forms ofthe enzyme, complementing the spectroscopic data. Based on the high levels of free glutathione inthe cell, we suggest that the expression of the different metal forms of GLX2 during Salmonellainfection could be exploited as a mechanism to regulate the enzyme activity.