Glutamate dehydrogenase (GDH) is one of themost extensively studied enzymes, describedby hundreds of articles spanning more thanfive decades of research. The enzyme catalysesthe reversible oxidative deamination reactionof L-glutamate to 2-oxoglutarate. All livingorganisms express this enzyme and key catalyticresidues have remained unchangedthrough the epochs. However, animal GDHexhibits complex allosteric regulation by a widearray of metabolites compared to GDH fromthe other kingdoms. Recent studies have demonstratedthat the loss of some of this allostericregulation causes hypersecretion of insulin,suggesting that animal GDH is not just importantfor amino acid oxidation. Discussed hereare the atomic details of animal GDH regulationand why these features may have evolved.What is also emerging from these studies isthat GDH is a highly dynamic enzyme andregulators act by controlling this movement atkey junctions. These details have led to thedevelopment of a number of novel inhibitorsthat may find use in treating a number of GDHrelateddisorders. It is very clear that we areonly beginning to understand the ingeniousversatility of this very old enzyme.
|Original language||English (US)|
|Title of host publication||Amino Acids in Human Nutrition and Health|
|Number of pages||23|
|State||Published - Nov 24 2011|
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Agricultural and Biological Sciences(all)