화학공학소재연구정보센터
Journal of the American Chemical Society, Vol.133, No.32, 12322-12325, 2011
A Dedicated Glutathione S-Transferase Mediates Carbon-Sulfur Bond Formation in Gliotoxin Biosynthesis
Gliotoxin is a virulence factor of the human pathogen Aspergillus fumigatus, the leading cause of invasive aspergillosis. Its toxicity is mediated by the unusual transannular disulfide bridge of the epidithiodiketopiperazine (ETP) scaffold. Here we disclose the critical role of a specialized glutathione S-transferase (GST), GliG, in enzymatic sulfurization. Furthermore, we show that bishydroxylation of the diketopiperazine by the oxygenase GliC is a prerequisite for glutathione adduct formation. This is the first report of the involvement of a GST in enzymatic C-S bond formation in microbial secondary metabolism.