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Glutamine synthetase (GS, EC 6.3.1.4.) is a key multimeric enzyme in nitrogen metabolism. GS is indispensable for the adequate growth and development of wheat plants, and extremely important for proper grain gilling process. There are two isoforms of GS in wheat leaves: the cytoplasmic GS1 and the chloroplast localized GS2, where GS2 is the predominant isoform. The GS2 takes place at the carbon-nitrogen metabolic branch point. We studied the kinetic properties of GS2 of wheat (Triticum aestivum L. cv. Jubilejnaja-50), its substrate consumption under various conditions and its magnesia and manganese binding capabilities. We showed kinetic evidence, that at the connection of carbon and nitrogen pathways GS is a fine regulator, and its enzymatic activity is regulated in a negatively cooperative allosteric manner. This allosteric negative cooperativity is driven by the regulatory substrate which has been identified as glutamic acid. To describe this regulation, we have created a new, approximate mathematical model, which can be associated with our newly introduced mechanistic model of GS2. We also showed that supraoptimal ATP concentration inhibits the activity of GS2 in vitro. In case of wheat GS2 half of the bound Mg2+ can be displaced by Mn2+, presumably this change occurs at the n2 metal binding sites, which have lower Mg2+ affinity.

A búza (Triticum aestivum L.) kloroplasztisz lokalizált glutamin-szintetáz enzim allosztérikus szabályozása, a szubsztrátumszintű működés tanulmányozása