Herein, what does glutathione S transferase do?
Glutathione S-transferases (GSTs) are a family of Phase II detoxification enzymes that function to protect cellular macromolecules from attack by reactive electrophiles. Specifically, GSTs catalyse the conjugation of glutathione (GSH) to a wide variety of endogenous and exogenous electrophilic compounds (Figure 1).
Subsequently, question is, what is unusual about glutathione S structure? Glutathione has a peculiar bond between glutamic acid and cysteine residues. The link occurs through γ-carboxyl group of glutamate instead of the (expected) α-carboxyl group. As a consequence, common peptidases are unable to hydrolyze the bond. Few enzymes are able to break it, such as γ-glutamyltranspeptidase (GGT).
Herein, why does GST bind to glutathione?
Specifically, the function of GSTs in this role is twofold: to bind both the substrate at the enzyme's hydrophobic H-site and GSH at the adjacent, hydrophilic G-site, which together form the active site of the enzyme; and subsequently to activate the thiol group of GSH, enabling the nucleophilic attack upon the
What is GST affinity chromatography?
GST Tag Definition
Glutathione Affinity is an efficient method for single-step purification of proteins fused to a GST (glutathione S-transferase) tag. GST can be expressed as a soluble protein in the E. coli cytoplasm in high amounts and with full enzymatic activity.
