Glutamine synthetase structure‐catalysis relationship—Recent advances and applications

Glutamine synthetase is a key enzyme that exists in every living organism. It is responsible for incorporating ammonium into glutamate, generating glutamine. Research on this enzyme has grown substantially over the last decades. The recent advances in the determination of its structure, through the crystallization of novel classes of glutamine synthetase with increased resolution, greatly contributed to a shift in the glutamine synthetase research from fundamental to more applied. Here, we explore the active sites of glutamine synthetases, review the structural and catalytic roles of their active sites' ions Mg2+s, combine the information gathered from recent computational studies dedicated to unravel their catalytic mechanisms with the hypothesis raised at the beginning of the XXI century based on experimental studies, glance at the development of competitive glutamine synthetase inhibitors, and highlight the high value of these enzymes to industry, namely in the fields of agriculture and medicine. This article is categorized under: Molecular and Statistical Mechanics > Molecular Mechanics Structure and Mechanism > Reaction Mechanisms and Catalysis The crucial enzymes glutamine synthetases are responsible for the condensation of glutamate and ammonium, at the expense of ATP cleavage, to form glutamine. This catalytic reaction is at the cornerstone of life and can be tweaked to enhance agriculture productivity or improve human health