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Glutamic acid
Glutamic acid
General
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SMILES  ?
Molar mass  ?.?? g/mol
Appearance  ?
CAS number [?-?-?]
Properties
Density and phase  ? g/cm³, ?
Solubility in water  ? g/100 ml (?°C)
Melting point  ?°C (? K)
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Acidity (pKa)  ?
Basicity (pKb)  ?
Chiral rotation [α]D  ?°
Viscosity  ? cP at ?°C
Structure
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geometry
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Dipole moment  ? D
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MSDS External MSDS
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NFPA 704
Flash point  ?°C
R/S statement R: ?
S: ?
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Supplementary data page
Structure and
properties
n, εr, etc.
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data
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Solid, liquid, gas
Spectral data UV, IR, NMR, MS
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Except where noted otherwise, data are given for
materials in their standard state (at 25 °C, 100 kPa)
Infobox disclaimer and references


Glutamic acid (abbreviated as Glu or E) is one of the 20-22 proteinogenic amino acids, and its codons are GAA and GAG. It is a non-essential amino acid. It acts as a precursor of glutamate so the carboxylate anions and salts of glutamic acid are known as glutamates. In neuroscience, glutamate is an important neurotransmitter that plays a key role in long-term potentiation and is important for learning and memory.[1]

Glutamic acid functions as a neurotransmitter in the dorsal horns of the spinal cord and in the cerebellum[2].

EtymologyEdit

Glutamic acid arises from the Latin gluten (glue) +amine (indicating an amine + ikos (of resembling, or characterized by)


Chemistry Edit

The side chain carboxylic acid functional group has a pKa of 4.1 and therefore exists almost entirely in its negatively charged deprotonated carboxylate form at pH values greater than 4.1; therefore, it is negatively charged at physiological pH ranging from 7.35 to 7.45.

HistoryEdit

Main article: Glutamic acid (flavour)

Although they occur naturally in many foods, the flavour contributions made by glutamic acid and other amino acids were only scientifically identified early in the twentieth century. The substance was discovered and identified in the year 1866, by the German chemist Karl Heinrich Leopold Ritthausen who treated wheat gluten (for which it was named) with sulfuric acid.[3] In 1908 Japanese researcher Kikunae Ikeda of the Tokyo Imperial University identified brown crystals left behind after the evaporation of a large amount of kombu broth as glutamic acid. These crystals, when tasted, reproduced the ineffable but undeniable flavour he detected in many foods, most especially in seaweed. Professor Ikeda termed this flavour umami. He then patented a method of mass-producing a crystalline salt of glutamic acid, monosodium glutamate.[4][5]

BiosynthesisEdit

Reactants Products Enzymes
Glutamine + H2O Glu + NH3 GLS, GLS2
NAcGlu + H2O Glu + Acetate (unknown)
α-ketoglutarate + NADPH + NH4+ Glu + NADP+ + H2O GLUD1, GLUD2[6]
α-ketoglutarate + α-amino acid Glu + α-keto acid transaminase
1-Pyrroline-5-carboxylate + NAD+ + H2O Glu + NADH ALDH4A1
N-formimino-L-glutamate + FH4 Glu + 5-formimino-FH4 FTCD
NAAG Glu + NAA GCPII


Function and uses Edit

Metabolism Edit

Glutamate is a key compound in cellular metabolism. In humans, dietary proteins are broken down by digestion into amino acids, which serve as metabolic fuel for other functional roles in the body. A key process in amino acid degradation is transamination, in which the amino group of an amino acid is transferred to an α-ketoacid, typically catalysed by a transaminase. The reaction can be generalised as such:

R1-amino acid + R2-α-ketoacid R1-α-ketoacid + R2-amino acid

A very common α-keto acid is α-ketoglutarate, an intermediate in the citric acid cycle. Transamination of α-ketoglutarate gives glutamate. The resulting α-ketoacid product is often a useful one as well, which can contribute as fuel or as a substrate for further metabolism processes. Examples are as follows:

Alanine + α-ketoglutarate pyruvate + glutamate
Aspartate + α-ketoglutarate oxaloacetate + glutamate

Both pyruvate and oxaloacetate are key components of cellular metabolism, contributing as substrates or intermediates in fundamental processes such as glycolysis, gluconeogenesis, and the citric acid cycle.

Glutamate also plays an important role in the body's disposal of excess or waste nitrogen. Glutamate undergoes deamination, an oxidative reaction catalysed by glutamate dehydrogenase,[6] as follows:

glutamate + H2O + NADP+ → α-ketoglutarate + NADPH + NH3 + H+

Ammonia (as ammonium) is then excreted predominantly as urea, synthesised in the liver. Transamination can, thus, be linked to deamination, effectively allowing nitrogen from the amine groups of amino acids to be removed, via glutamate as an intermediate, and finally excreted from the body in the form of urea.

Neurotransmitter Edit

Glutamate is the most abundant excitatory neurotransmitter in the vertebrate nervous system.[7] At chemical synapses, glutamate is stored in vesicles. Nerve impulses trigger release of glutamate from the pre-synaptic cell. In the opposing post-synaptic cell, glutamate receptors, such as the NMDA receptor, bind glutamate and are activated. Because of its role in synaptic plasticity, glutamate is involved in cognitive functions like learning and memory in the brain.[8] The form of plasticity known as long-term potentiation takes place at glutamatergic synapses in the hippocampus, neocortex, and other parts of the brain. Glutamate works not only as a point-to-point transmitter but also through spill-over synaptic crosstalk between synapses in which summation of glutamate released from a neighboring synapse creates extrasynaptic signaling/volume transmission.[9]

Glutamate transporters[10] are found in neuronal and glial membranes. They rapidly remove glutamate from the extracellular space. In brain injury or disease, they can work in reverse, and excess glutamate can accumulate outside cells. This process causes calcium ions to enter cells via NMDA receptor channels, leading to neuronal damage and eventual cell death, and is called excitotoxicity. The mechanisms of cell death include

  • Glu/Ca2+-mediated promotion of transcription factors for pro-apoptotic genes, or downregulation of transcription factors for anti-apoptotic genes

Excitotoxicity due to excessive glutamate release and impaired uptake occurs as part of the ischemic cascade and is associated with stroke[1] and diseases like amyotrophic lateral sclerosis, lathyrism, autism, some forms of mental retardation, and Alzheimer's disease.[1][12] In contrast, decreased glutamate release is observed under conditions of classical phenylketonuria[13] leading to developmental disruption of glutamate receptor expression.[14]

Glutamic acid has been implicated in epileptic seizures. Microinjection of glutamic acid into neurons produces spontaneous depolarisations around one second apart, and this firing pattern is similar to what is known as paroxysmal depolarizing shift in epileptic attacks. This change in the resting membrane potential at seizure foci could cause spontaneous opening of voltage-activated calcium channels, leading to glutamic acid release and further depolarization [citation needed].

Experimental techniques to detect glutamate in intact cells include using a genetically engineered nanosensor.[15] The sensor is a fusion of a glutamate-binding protein and two fluorescent proteins. When glutamate binds, the fluorescence of the sensor under ultraviolet light changes by resonance between the two fluorophores. Introduction of the nanosensor into cells enables optical detection of the glutamate concentration. Synthetic analogs of glutamic acid that can be activated by ultraviolet light and two-photon excitation microscopy have also been described.[16] This method of rapidly uncaging by photostimulation is useful for mapping the connections between neurons, and understanding synapse function.

Evolution of glutamate receptors is entirely the opposite in invertebrates, in particular, arthropods and nematodes, where glutamate stimulates glutamate-gated chloride channels.[citation needed] The beta subunits of the receptor respond with very high affinity to glutamate and glycine.[17] Targeting these receptors has been the therapeutic goal of anthelmintic therapy using avermectins. Avermectins target the alpha-subunit of glutamate-gated chloride channels with high affinity.[18] These receptors have also been described in arthropods, such as Drosophila melanogaster[19] and Lepeophtheirus salmonis.[20] Irreversible activation of these receptors with avermectins results in hyperpolarization at synapses and neuromuscular junctions resulting in flaccid paralysis and death of nematodes and arthropods.

File:L-Glutamate Structural Formulae.png

Brain nonsynaptic glutamatergic signaling circuits Edit

Extracellular glutamate in Drosophila brains has been found to regulate postsynaptic glutamate receptor clustering, via a process involving receptor desensitization.[21] A gene expressed in glial cells actively transports glutamate into the extracellular space,[21] while, in the nucleus accumbens-stimulating group II metabotropic glutamate receptors, this gene was found to reduce extracellular glutamate levels.[22] This raises the possibility that this extracellular glutamate plays an "endocrine-like" role as part of a larger homeostatic system.

GABA precursor Edit

Glutamate also serves as the precursor for the synthesis of the inhibitory GABA in GABA-ergic neurons. This reaction is catalyzed by glutamate decarboxylase (GAD), which is most abundant in the cerebellum and pancreas.

Stiff-man syndrome is a neurologic disorder caused by anti-GAD antibodies, leading to a decrease in GABA synthesis and, therefore, impaired motor function such as muscle stiffness and spasm. Since the pancreas is also abundant for the enzyme GAD, a direct immunological destruction occurs in the pancreas and the patients will have diabetes mellitus.

Flavor enhancer Edit

Main article: Glutamic acid (flavor)

Glutamic acid, being a constituent of protein, is present in every food that contains protein, but it can only be tasted when it is present in an unbound form. Significant amounts of free glutamic acid are present in a wide variety of foods, including cheese and soy sauce, and is responsible for umami, one of the five basic tastes of the human sense of taste. Glutamic acid is often used as a food additive and flavour enhancer in the form of its salt, known as monosodium glutamate (MSG).

Nutrient Edit

All meats, poultry, fish, eggs, dairy products, and kombu are excellent sources of glutamic acid. Some protein-rich plant foods also serve as sources. 30% to 35% of the protein in wheat is glutamic acid. Ninety-five percent of the dietary glutamate is metabolized by intestinal cells in a first pass.[23]

Plant growth Edit

Auxigro is a plant growth preparation that contains 30% glutamic acid.

NMR spectroscopy Edit

In recent years, there has been much research into the use of RDCs in NMR spectroscopy. A glutamic acid derivative, poly-γ-benzyl-L-glutamate (PBLG), is often used as an alignment medium to control the scale of the dipolar interactions observed.[24]

Production Edit

China-based Fufeng Group Limited is the largest producer of glutamic acid in the world, with capacity increasing to 300,000 tons at the end of 2006 from 180,000 tons during 2006, putting them at 25%–30% of the Chinese market. Meihua is the second-largest Chinese producer. Together, the top-five producers have roughly 50% share in China. Chinese demand is roughly 1.1 million tons per year, while global demand, including China, is 1.7 million tons per year.

Pharmacology Edit

The drug phencyclidine (more commonly known as PCP) antagonizes glutamic acid non-competitively at the NMDA receptor. For the same reasons, dextromethorphan and ketamine also have strong dissociative and hallucinogenic effects. Acute infusion of the drug LY354740 (also known as Eglumegad, an agonist of the metabotropic glutamate receptors 2 and 3) resulted in a marked diminution of yohimbine-induced stress response in bonnet macaques (Macaca radiata); chronic oral administration of LY354740 in those animals led to markedly reduced baseline cortisol levels (approximately 50 percent) in comparison to untreated control subjects.[25]. Glutamate does not easily pass the blood brain barrier, but, instead, is transported by a high-affinity transport system.[26] It can also be converted into glutamine.

See alsoEdit

References Edit

  1. 1.0 1.1 1.2 includeonly>Robert Sapolsky. "Biology and Human Behavior: The Neurological Origins of Individuality, 2nd edition", 'The Teaching Company'. “see pages 19 and 20 of Guide Book”
  2. Coleman,A F (2006). Oxford Dictionary of Psychology, 2nd ed. Oxford:OUP.
  3. R.H.A. Plimmer [1908] (1912). R.H.A. Plimmer & F.G. Hopkins The chemical composition of the proteins, 2nd, London: Longmans, Green and Co.. URL accessed June 3, 2012.
  4. includeonly>Renton, Alex. "If MSG is so bad for you, why doesn't everyone in Asia have a headache?", 'The Guardian', 2005-07-10. Retrieved on 2008-11-21.
  5. Kikunae Ikeda Sodium Glutamate. Japan Patent Office. URL accessed on 2008-11-21.
  6. PMID 10736372 (PMID 10736372)
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  7. DOI:10.1007/BF02253527
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  8. DOI:10.1073/pnas.0913154107
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  9. DOI:10.1016/j.brainresrev.2004.04.004
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  10. PMID 2568579 (PMID 2568579)
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  11. DOI:10.1016/j.neuint.2004.03.007
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  12. Glushakov, AV, Dennis, DM; Sumners, C; Seubert, CN; Martynyuk, AE (2003 Apr 1). L-phenylalanine selectively depresses currents at glutamatergic excitatory synapses. Journal of neuroscience research 72 (1): 116–24.
  13. Glushakov, AV, Glushakova, O; Varshney, M; Bajpai, LK; Sumners, C; Laipis, PJ; Embury, JE; Baker, SP; Otero, DH; Dennis, DM; Seubert, CN; Martynyuk, AE (2005 Feb). Long-term changes in glutamatergic synaptic transmission in phenylketonuria. Brain : a journal of neurology 128 (Pt 2): 300–7.
  14. DOI:10.1073/pnas.0503274102
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  15. DOI:10.1523/jneurosci.1519-07.2007
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  16. DOI:10.1046/j.1471-4159.1995.64052354.x
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  17. DOI:10.1038/371707a0
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  18. Cully, D.F., Paress, P.S., Liu, K.K., Schaeffer, J.M. and Arena, J.P. 1996. "Identification of a Drosophila melanogaster glutamate-gated chloride channel sensitive to the antiparasitic agent avermectin". J. Biol. Chem. '271, 20187-20191'
  19. DOI:10.1111/j.1365-2885.2007.00823.x
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  20. 21.0 21.1 Augustin H, Grosjean Y, Chen K, Sheng Q, Featherstone DE (2007). Nonvesicular Release of Glutamate by Glial xCT Transporters Suppresses Glutamate Receptor Clustering In Vivo. Journal of Neuroscience 27 (1): 111–123.
  21. Zheng Xi, Baker DA, Shen H, Carson DS, Kalivas PW (2002). Group II metabotropic glutamate receptors modulate extracellular glutamate in the nucleus accumbens. Journal of Pharmacology and Experimental Therapeutics 300 (1): 162–171.
  22. Reeds, P.J., et al. (1 April 2000). Intestinal glutamate metabolism. Journal of Nutrition 130 (4s): 978S–982S.
  23. C. M. Thiele, Concepts Magn. Reson. A, 2007, 30A, 65-80
  24. Coplan JD, Mathew SJ, Smith EL, Trost RC, Scharf BA, Martinez J, Gorman JM, Monn JA, Schoepp DD, Rosenblum LA (July 2001). Effects of LY354740, a novel glutamatergic metabotropic agonist, on nonhuman primate hypothalamic-pituitary-adrenal axis and noradrenergic function.. CNS Spectr. 6 (7): 607-12, 617.
  25. Smith QR (April 2000). Transport of glutamate and other amino acids at the blood–brain barrier. J. Nutr. 130 (4S Suppl): 1016S–22S.

Further readingEdit

Key textsEdit

BooksEdit

PapersEdit

  1. Nelson DL and Cox MM. Lehninger Principles of Biochemistry, 4th edition.
  2. a 
Free text Okumoto, S., et al. (2005).  Detection of glutamate release from neurons by genetically encoded surface-displayed FRET nanosensors. Proceedings of the National Academy of Sciences U.S.A 102 (24): 8740-8745. PMID 15939876. Free text
  1. a 
Molecular pharmacology of glutamate transporters, EAATs and VGLUTs. Brain Res Brain Res Rev. 2004 Jul; 45(3):250-65. PMID 15210307
  1. a 
Delayed increase of Ca2+ influx elicited by glutamate: role in neuronal death. Mol Pharmacol. 1989 Jul;36(1):106-12; PMID 2568579
  1. a 
Free text Reeds, P.J., et al. (2000).  Intestinal glutamate metabolism. Journal of Nutrition 130 (4s): 978S-982S. PMID 10736365.. Free text
  1.  
Free text Corrie, J.E., et al. (1993).  Postsynaptic activation at the squid giant synapse by photolytic release of L-glutamate from a 'caged' L-glutamate. Journal of Physiology 465 (Jun): 1-8. PMID 7901400. Free text 
  1.  
Augustin H, Grosjean Y, Chen K, Sheng Q, Featherstone DE (2007).  Nonvesicular release of glutamate by glial xCT transporters suppresses glutamate receptor clustering in vivo. Journal of Neuroscience 27 (1): 111-123. PMID 17202478.
  1.  
Zheng Xi, Baker DA, Shen H, Carson DS, Kalivas PW (2002).  Group II metabotropic glutamate receptors modulate extracellular glutamate in the nucleus accumbens. Journal of Pharmacology and Experimental Therapeutics 300 (1): 162-171. PMID 11752112.

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