Table of Contents
Which of the following is an inhibitor of glutamate dehydrogenase?
1 Answer. Allosteric inhibitor of glutamate dehydrogenase is ATP.
What is glutamate dehydrogenase activated by?
GDH is activated when amino acids (protein) are ingested to promote insulin secretion and appropriate anabolic effects on peripheral tissues; in the glucose-fed state, GDH is inhibited in pancreas perhaps to redirect amino acids into glutamine synthesis in order to amplify insulin release.
Why is glutamate dehydrogenase important in the urea cycle?
Glutamate dehydrogenase (GLDH) is a mitochondrial enzyme that reversibly converts glutamate to alpha-ketoglutarate as part of the urea cycle. GLDH activity increases with liver injury and the magnitude of elevation may be higher and longer lasting when compared to ALT [31].
Is glutamate dehydrogenase in the liver?
The liver is rich in glutamate dehydrogenase (GDH) that catalyzes the reversible oxidative deamination of glutamate to α-ketoglutarate and ammonia, thus bridging amino acid–to–glucose pathways.
Why is glutamate important in metabolism?
Glutamate plays a critical role in the central metabolism of many organisms, including nitrogen assimilation, amino acid biosynthesis, and cofactor production. It is also involved in the production of secondary metabolites such as antibiotics.
What is the role of glutamic acid and glutamate dehydrogenase in ammonia metabolism?
Abstract. Glutamate dehydrogenase (GDH) catalyzes the reversible inter-conversion of glutamate to α-ketoglutarate and ammonia. High levels of GDH activity is found in mammalian liver, kidney, brain, and pancreas.
Is glutamate dehydrogenase present in kidney?
Glutamate dehydrogenase (GDH) catalyzes the reversible inter-conversion of glutamate to α-ketoglutarate and ammonia. High levels of GDH activity is found in mammalian liver, kidney, brain, and pancreas.