This article is an overview of the current knowledge of insect glutathione transferases. Three
major topics are discussed: the glutathione transferase contributions to insecticide …

S-Nitrosylation, the selective and reversible addition of nitric oxide (NO) moiety to cysteine
(Cys) sulfur in proteins, regulates numerous cellular processes. In recent years, proteomic …

Dehydroascorbate reductase (DHAR) is a key enzyme in the ascorbate–glutathione cycle
that maintains reduced pools of ascorbic acid and serves as an important antioxidant. In this …

BACKGROUND: Glutathione transferase (GST) catalyzes glutathione conjugation, a major
detoxification pathway for xenobiotics and endogenous substances. Here, we determined …

Glutathione transferases (GSTs) are a superfamily of dimeric proteins associated with the
detoxification of various reactive electrophiles and responsive to a multitude of stressors. We …

GST (glutathione transferase) is a dimeric enzyme recognized for biotransformation of
xenobiotics and endogenous toxic compounds. In the present study, residues forming the …

Cytosolic glutathione transferases (GSTs) are major detoxification enzymes in aerobes.
Each subunit has two distinct domains and an active site consisting of a G-site for binding …

Key message The relative position of domains is critical for enzymatic properties of tau class
glutathione S-transferases, and altering the position of linker far away from the active center …

We report four new crystal structures for Delta class glutathione transferases from insects.
We compare these new structures as well as several previously reported structures to …

Cytosolic class pi glutathione transferase P1-1 (GSTP1-1) is associated with drug resistance
and proliferative pathways because of its catalytic detoxification properties and ability to bind …