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.

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谷氨酰胺合成酶的结构-催化关系—最新进展和应用

谷氨酰胺合成酶是存在于每个活生物体中的关键酶。它负责将铵盐掺入谷氨酸盐中，生成谷氨酰胺。在过去的几十年中，对该酶的研究已大大增加。通过提高分辨率的新型新型谷氨酰胺合成酶的结晶，其结构测定的最新进展极大地促进了谷氨酰胺合成酶研究从基础到更广泛的应用。在这里，我们探索谷氨酰胺合成酶的活性位点，回顾其活性位点离子Mg ²⁺的结构和催化作用。s，结合最近从专门用于揭示其催化机理的计算研究中获得的信息，以及基于实验研究在二十一世纪初提出的假说，对竞争性谷氨酰胺合成酶抑制剂的开发进行了展望，并强调了这些酶的高价值工业，即农业和医学领域。