glutamine synthetase

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glutamine synthetase

[′glüd·ə‚mēn ′sin·thə‚tās]
(biochemistry)
An enzyme which catalyzes the formation of glutamine from glutamic acid and ammonia, using adenosine triphosphate as a source of energy.
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Excessive ROS production mediated by the necrosome occurs through the following mechanisms: (a) RIP3 can allosterically activate glutamate-ammonia ligase or glutamine synthetase (GLUL) and glutamate dehydrogenase (GLUD1) enzymes.
Second, GLUL expression is highly correlated with Wnt/[beta]-catenin activation, demonstrating its faithfulness as a Wnt target gene.
Furthermore, level of glutamate-ammonia ligase (glutamine synthetase (GLUL)), an enzyme involved in metabolism of glutamine and gamma aminobutyric acid (GABA), was increased in the livers, HCCs, and HCAs of both PB-treated [Ogg1.sup.-/-] and [Ogg1.sup.+/+] mice (Table 2).
As shown in Figure 2, the Glul regulated the glutamate metabolism, the nitrogen metabolism, and peptidoglycan biosynthesis.
A genetic variant in the region of the GLUL gene was identified that is associated with an increased risk of CHD in type 2 diabetics.
Several proteins were differentially expressed, which included karyopherin alpha 4 (KPNA4) overexpressed only in paralytic rabies, calcium calmodulin dependent kinase 2 alpha (CAMK2A) which was upregulated in paralytic rabies, and glutamate ammonia ligase (GLUL) which was overexpressed both in paralytic and encephalitic rabies.