Special Issue "Enzymes of Glutamate Metabolism in Health and Disease"
A special issue of Biology (ISSN 2079-7737).
Deadline for manuscript submissions: closed (30 June 2016).
Interests: pyridoxal 5'-phosphate enzymes; enzyme mechanisms; bioactivation mechanisms; neurochemistry; neurodegenerative diseases; chemoprevention; and 1-C; nitrogen; sulfur and selenium biochemistry; transglutaminases (protein cross linking enzymes)
Special Issues and Collections in MDPI journals
Interests: oxidative stress and neurodegenerative disorders
Glutamate is an abundant amino acid in most mammalian tissues and is centrally important in nitrogen metabolism and homeostasis. For example, the concentrations of glutamate in brain range from 10–2 to 10–1 M in the parenchyma and synaptic vesicles, respectively. In this tissue, glutamate acts as the most important excitatory neurotransmitter and therefore its extracellular concentrations are limited to 10–6 M amounts. Higher concentrations result in excitotoxicity. Thus, the brain has an extraordinary ability to maintain glutamate in the various compartments at remarkably precise concentrations. In the liver, glutamate is a major source of ammonia for urea synthesis via the glutamate dehydrogenase reaction. Coupling of glutamate-linked amino acid aminotransferases to the glutamate dehydrogenase reaction causes excess amino acid nitrogen to be excreted as urea. Glutamine is a major source of nitrogen and energy for dividing cells including cancer cells. Much of the glutamine in these cells is converted to glutamate, which in turn is a source of the TCA cycle component α-ketoglutarate. Finally, owing to its central importance in N and energy metabolism it is not surprising that many diseases (e.g., hyperammonemia, urea cycle disorders, neurodegenerative diseases) are associated with disturbance of metabolic pathways in which glutamate participates.
Prof. Dr. Arthur J. L. Cooper
Dr. Thomas M. Jeitner
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- glutamate-utilizing aminotransferases
- glutamine synthetase
- glutamate dehydrogenase