Premium
Atypical features of a Ure2p glutathione transferase from Phanerochaete chrysosporium
Author(s) -
Thuillier Anne,
Roret Thomas,
Favier Frédérique,
Gelhaye Eric,
Jacquot Jean-Pierre,
Didierjean Claude,
Morel-Rouhier Mélanie
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.05.031
Subject(s) - phanerochaete , chrysosporium , glutathione , biochemistry , chemistry , glutathione s transferase , asparagine , context (archaeology) , gpx3 , gpx6 , enzyme , biology , glutathione peroxidase , paleontology
Glutathione transferases (GSTs) are known to transfer glutathione onto small hydrophobic molecules in detoxification reactions. The GST Ure2pB1 from Phanerochaete chrysosporium exhibits atypical features, i.e. the presence of two glutathione binding sites and a high affinity towards oxidized glutathione. Moreover, PcUre2pB1 is able to efficiently deglutathionylate GS‐phenacylacetophenone. Catalysis is not mediated by the cysteines of the protein but rather by the one of glutathione and an asparagine residue plays a key role in glutathione stabilization. Interestingly PcUre2pB1 interacts in vitro with a GST of the omega class. These properties are discussed in the physiological context of wood degrading fungi.