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Trametes versicolor glutathione transferase Xi 3, a dual Cys‐GST with catalytic specificities of both Xi and Omega classes
Author(s) -
Schwartz Mathieu,
Perrot Thomas,
Deroy Aurélie,
Roret Thomas,
MorelRouhier Mélanie,
Mulliert Guillermo,
Gelhaye Eric,
Favier Frédérique,
Didierjean Claude
Publication year - 2018
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 - 10.1002/1873-3468.13224
Subject(s) - glutathione , reductase , chemistry , cysteine , residue (chemistry) , stereochemistry , glutathione s transferase , biochemistry , enzyme
Glutathione transferases ( GST s) from the Xi and Omega classes have a catalytic cysteine residue, which gives them reductase activities. Until now, they have been assigned distinct substrates. While Xi GST s specifically reduce glutathionyl‐(hydro)quinones, Omega GST s are specialized in the reduction of glutathionyl‐acetophenones. Here, we present the biochemical and structural analysis of Tv GSTX 1 and Tv GSTX 3 isoforms from the wood‐degrading fungus Trametes versicolor . Tv GSTX 1 reduces GS ‐menadione as expected, while Tv GSTX 3 reduces both Xi and Omega substrates. An in‐depth structural analysis indicates a broader active site for Tv GSTX 3 due to specific differences in the nature of the residues situated in the C‐terminal helix α9. This feature could explain the catalytic duality of Tv GSTX 3. Based on phylogenetic analysis, we propose that this duality might exist in saprophytic fungi and ascomycetes.