Université de Lorraine, IAM, UMR 1136, IFR 110 EFABA,Vandoeuvre-lès-Nancy F-54506, France.
FEBS Lett. 2013 Jul 11;587(14):2125-30. doi: 10.1016/j.febslet.2013.05.031. Epub 2013 May 24.
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.
谷胱甘肽转移酶（GSTs）是众所周知的将谷胱甘肽转移到解毒反应中小的疏水分子上。黄孢原毛平革菌中的 GST Ure2pB1 表现出非典型的特征，即存在两个谷胱甘肽结合位点和对氧化型谷胱甘肽的高亲和力。此外，PcUre2pB1 能够有效地使 GS-苯乙酰苯酮去谷胱甘肽化。催化不是通过蛋白质的半胱氨酸介导的，而是通过谷胱甘肽的一个半胱氨酸和一个天冬酰胺残基发挥关键作用来稳定谷胱甘肽。有趣的是，PcUre2pB1 在体外与 omega 类 GST 相互作用。这些特性在木质素降解真菌的生理背景下进行了讨论。
