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Glutamine synthetase structure‐catalysis relationship—Recent advances and applications
Author(s) -
dos Santos Moreira Cátia Daniela,
Ramos Maria João Ribeiro Nunes,
Fernandes Pedro Manuel Azevedo Alexandrino
Publication year - 2018
Publication title -
wiley interdisciplinary reviews: computational molecular science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.126
H-Index - 81
eISSN - 1759-0884
pISSN - 1759-0876
DOI - 10.1002/wcms.1399
Subject(s) - glutamine synthetase , glutamine , enzyme , biochemistry , molecular mechanics , active site , biology , computational biology , chemistry , amino acid , computational chemistry , molecular dynamics
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 Mg 2+ 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