Glutamate dehydrogenase (GLDH, GDH) is an enzyme observed in both prokaryotes and eukaryotic mitochondria. The aforementioned reaction also yields ammonia, which in eukaryotes is canonically processed as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Glutamate dehydrogenase also has a very low affinity for ammonia (high Michaelis constant of about 1 mM), and therefore toxic levels of ammonia would have to be present in the body for the reverse reaction to proceed (that is, α-ketoglutarate and ammonia to glutamate and NAD(P)+). However, in brain, the NAD+/NADH ratio in brain mitochondria encourages oxidative deamination (i.e. glutamate to α-ketoglutarate and ammonia).[1] In bacteria, the ammonia is assimilated to amino acids via glutamate and aminotransferases.[2] In plants, the enzyme can work in either direction depending on environment and stress.[3][4] Transgenic plants expressing microbial GLDHs are improved in tolerance to herbicide, water deficit, and pathogen infections.[5] They are more nutritionally valuable.[6]
The enzyme represents a key link between catabolic and anabolic pathways, and is, therefore, ubiquitous in eukaryotes. In humans the relevant genes are called GLUD1 (glutamate dehydrogenase 1) and GLUD2 (glutamate dehydrogenase 2), and there are also at least 8 GLDH pseudogenes in the human genome as well, probably reflecting microbial influences on eukaryote evolution.
Glutamate
α-Ketoglutarate
^McKenna MC, Ferreira GC (2016). "Enzyme Complexes Important for the Glutamate–Glutamine Cycle". The Glutamate/GABA-Glutamine Cycle. Advances in Neurobiology. Vol. 13. pp. 59–98. doi:10.1007/978-3-319-45096-4_4. ISBN 978-3-319-45094-0. PMID 27885627.
^Lightfoot DA, Baron AJ, Wootton JC (May 1988). "Expression of the Escherichia coli glutamate dehydrogenase gene in the cyanobacterium Synechococcus PCC6301 causes ammonium tolerance". Plant Molecular Biology. 11 (3): 335–44. doi:10.1007/BF00027390. PMID 24272346. S2CID 21845538.
^Mungur R, Glass AD, Goodenow DB, Lightfoot DA (June 2005). "Metabolite fingerprinting in transgenic Nicotiana tabacum altered by the Escherichia coli glutamate dehydrogenase gene". Journal of Biomedicine & Biotechnology. 2005 (2): 198–214. doi:10.1155/JBB.2005.198. PMC 1184043. PMID 16046826.
^Cite error: The named reference Grabowska_2011 was invoked but never defined (see the help page).
^Lightfoot DA, Bernhardt K, Mungur R, Nolte S, Ameziane R, Colter A, Jones K, Iqbal MJ, Varsa E, Young B (2007). "Improved drought tolerance of transgenic Zea mays plants that express the glutamate dehydrogenase gene (gdhA) of E. coli". Euphytica. 156 (1–2): 103–116. doi:10.1007/s10681-007-9357-y. S2CID 11806853.
^Lightfoot DA (2009). "Genes for use in improving nitrogen use efficiency in crops". In Wood, Andrew, Matthew A. Jenks (eds.). Genes for Plant Abiotic Stress. Wiley-Blackwell. pp. 167–182. ISBN 978-0-8138-1502-2.
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Glutamate
α-Ketoglutarate
