Abstract
Gamma-glutamyltransferases: exploring the complexity of a multi-functional family of enzymes
Highlights
Gamma-glutamyltransferase (γ-GT; EC 2.3.2.2) is the sole enzyme activity capable of cleaving the gamma-glutamyl bond present in the structure of glutathione (GSH), the well known antioxidant tripeptide, and is present on the outer aspect of plasma membranes of virtually all mammalian cells. γ-GT–mediated cleavage is the first step in the degradation of extracellular GSH, which proceeds by the action of dipeptidases and makes precursor aminoacids available for reuptake and re-utilization by the cell for GSH resynthesis
Γ-GT is responsible for the processing of other substrates including GSH in their structure, such as major inflammatory mediators leukotriene C4 (LTC4) and S-nitroso-glutathione (GSNO), as well as adducts of GSH with xenobiotics and metabolites formed by the action of glutathione-S-transferases
To date structural characterization of human γ-GT1 has been hampered by its heavily glycosylated structure, as well as by its association with cell membranes, and most of the knowledge regarding enzyme structure comes from investigations in bacteria
Summary
Gamma-glutamyltransferase (γ-GT; EC 2.3.2.2) is the sole enzyme activity capable of cleaving the gamma-glutamyl bond present in the structure of glutathione (GSH), the well known antioxidant tripeptide, and is present on the outer aspect of plasma membranes of virtually all mammalian cells. γ-GT–mediated cleavage is the first step in the degradation of extracellular GSH, which proceeds by the action of dipeptidases and makes precursor aminoacids (cysteine in the first place) available for reuptake and re-utilization by the cell for GSH resynthesis. A book review on Gamma-Glutamyl Transpeptidases: Structure and Function
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