Metal-dependent inhibition of glyoxalase II: A possible mechanism to regulate the enzyme activity

Autor(es)

Campos-Bermudez, Valeria A. ^[1] ; Moran-Barrio, Jorgelina ^[1] ; Costa-Filho, Antonio J. ^[2] ; Vila, Alejandro J. ^[1]

Afiliação do(s) autor(es)

^[1] Univ Nacl Rosario, Fac Ciencias Bioquim & Farmaceut, CONICET, IBR Inst Biol Mol & Celular Rosario, Rosario, Santa Fe - Argentina

^[2] Univ Sao Paulo, Inst Fis Sao Carlos, BR-13560 Sao Carlos - Brazil

• Tipo de documento: Artigo Científico
• Fonte: Journal of Inorganic Biochemistry; v. 104, n. 7, p. 726-731, JUL 2010.
• Citações Web of Science: 9

Resumo

Glyoxalase II (GLX2, EC 3.1.2.6., hydroxyacylglutathione hydrolase) is a metalloenzyme involved in crucial detoxification pathways. Different studies have failed in identifying the native metal ion of this enzyme, which is expressed with iron, zinc and/or manganese. Here we report that GloB, the GLX2 from Salmonella typhimurium, is differentially inhibited by glutathione (a reaction product) depending on the bound metal ion, and we provide a structural model for this inhibition mode. This metal-dependent inhibition was shown to occur in metal-enriched forms of the enzyme, complementing the spectroscopic data. Based on the high levels of free glutathione in the cell, we suggest that the expression of the different metal forms of GLX2 during Salmonella infection could be exploited as a mechanism to regulate the enzyme activity. (C) 2010 Elsevier Inc. All rights reserved. (AU)

• Processo FAPESP: 03/09859-2 - Ressonância paramagnética eletrônica em estudos estruturais de proteínas, peptídeos, biomembranas, polímeros, moléculas modelo e seus complexos com metais de transição
• Beneficiário: Otaciro Rangel Nascimento
• Modalidade de apoio: Auxílio à Pesquisa - Programa PRONEX - Temático