WordNet

street name for lysergic acid diethylamide (同)back breaker, battery-acid, dose, dot, Elvis, loony toons, Lucy in the sky with diamonds, pane, superman, window pane, Zen
any of various water-soluble compounds having a sour taste and capable of turning litmus red and reacting with a base to form a salt
having the characteristics of an acid; "an acid reaction"

PrepTutorEJDIC

酸性の / 酸味のある,すっぱい(sour) / (言葉・態度などが)厳しい,しんらつな / 酸 / すっぱいもの / 《俗》=LSD

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/06/13 00:36:17」(JST)

wiki ja

グルタミン酸（グルタミンさん、glutamic acid, glutamate）は、アミノ酸のひとつで、2-アミノペンタン二酸のこと。2-アミノグルタル酸とも呼ばれる。Glu あるいは E の略号で表される。小麦グルテンの加水分解物から初めて発見されたことからこの名がついた。英語に準じ、グルタメートと呼ぶこともある。

酸性極性側鎖アミノ酸に分類される。タンパク質構成アミノ酸のひとつで、非必須アミノ酸。動物の体内では神経伝達物質としても機能しており、グルタミン酸受容体を介して神経伝達が行われる、興奮性の神経伝達物質である。

グルタミン酸がたくさんつながると、納豆の粘性物質であるポリグルタミン酸になる。

致死量はLD50=20g/kgである。

生合成

クエン酸回路の一員である2-オキソグルタル酸が、グルタミン酸トランスフェラーゼの作用により他のアミノ酸からアミノ基転移を受けることで合成される。

あるいは、グルタミン酸デヒドロゲナーゼ (EC 1.4.1.3) による、グルタミン酸の2-オキソグルタル酸とアンモニアへの分解反応の逆反応により合成される。

L-glutamate + H₂O + NAD(P)⁺ → 2-oxoglutarate + NH₃ + NAD(P)H + H⁺

存在

コンブ、チーズ、緑茶などに大量に含まれるほか、シイタケ、トマト、魚介類などにも比較的多く含まれていることが知られている。

利用

主に、食品添加物であるL-グルタミン酸ナトリウム（グルタミン酸ソーダ、mono sodium glutamate、MSGあるいはグル曹とも呼ばれる）の中間原料として製造、利用される。グルタミン酸そのものは酸味を持つため、そのナトリウム塩であるグルタミン酸ナトリウムが調味料（うま味調味料）として利用されている。L-グルタミン酸ナトリウムを主成分とする調味料として、日本では味の素などがよく知られている。

製法

グルタミン酸の製造は、現在では微生物のアミノ酸発酵により、主に糖蜜またはコメ、コーンスターチなどと塩化アンモニウムを原料として、生産されている。詳細はアミノ酸発酵を参照のこと。その他の方法として、下記がある。

加水分解法

グルテン、大豆蛋白などの植物性タンパク質に、塩酸を加えて高温のもとで加水分解すると、グルタミン酸の塩酸塩が得られる。かつては小麦粉グルテンを使っての製造が行われていたが、現在は用いられない。

抽出法

テンサイから甜菜糖を作る過程で出る廃糖蜜には、約3%程度の遊離グルタミン酸が含まれるので、ステファン法によって抽出すれば利用可能であり、1930年代には工業化されたが、コストが高いことと、廃棄物が多く出ることから、現在は用いられない。

化学合成法

アクリロニトリルを原料に、カルボキシル化、シアノアミン化、加水分解を行うと、DL-グルタミン酸が得られる。これからL-グルタミン酸を分離すればよいが、約同量のD-グルタミン酸ができるので、効率が悪く、現在は用いられない。

酵素促進合成法

生合成にも使われているグルタミン酸デヒドロゲナーゼや、アミノトランスフェラーゼ、グルタミン酸合成酵素などの酵素と補酵素の作用によって、それぞれ異なる原料から製造する方法もある。

神経伝達物質と興奮毒

グルタミン酸は、神経系では、興奮性神経伝達物質の一つであり、記憶・学習などの脳高次機能に重要な役割を果たしている。他方、グルタミン酸は、神経系では、内因性興奮毒としての性質を持ち、細胞死、パーキンソン病、抑うつなどの神経症に関わっている^[1]。大脳皮質でグルタミン酸は脳虚血などの病的状態においては神経毒として作用し、神経細胞の壊死を起こすことが知られている^[2]。ニューロン周囲のグルタミン酸濃度が危険な濃度にまで達すると、ニューロンはアポトーシスと呼ばれるプロセスによって自己を殺す。このプロセス全体は、グルタミン酸塩が通常は低い濃度においては興奮性の神経伝達物質として作用することから興奮毒性と呼ばれている^[3]。さらにこの作用はNMDA型グルタミン酸受容体が活性化されてグルタミン酸とともにCaイオンの過剰流入を引き起こすことによって生じると推定されている^[2]。NMDA（N-メチル-D-アスパラギン酸）型グルタミン酸受容体は通常不活性な性質を持つ。これは、細胞外からのマグネシウムイオンがこの受容体の活動を阻害（マグネシウム・ブロック）しているためである^[4]。マグネシウム欠乏下ではNMDA型グルタミン酸受容体の抑えが効かなくなり、グルタミン酸の神経毒性によりうつ病が引き起こされているのではないかという仮説がある^[5]。最近、トリプトファン代謝産物であるキヌレン酸が脊髄においてNMDA型グルタミン酸受容体に作用しグルタミン酸に拮抗することが報告されており、脳内でグルタミン酸の興奮毒性の抑制に重要な機能的役割を担っていることが想定される^[2]。なお、グルタミン酸は、血液脳関門を透過しないので、循環系から脳に供給されることはない^[1]。

出典

^ ^a ^b 痛みと鎮痛の基礎知識 - Pain Relief - 伝達物質
^ ^a ^b ^c グルタミン酸の興奮毒性に拮抗する内因性アミノ酸の存在様式と機能的役割
^ 神経毒
^ NMDA型グルタミン酸受容体
^ マグネシウム

外部リンク

グルタミン酸 - 「健康食品」の安全性・有効性情報（国立健康・栄養研究所）

wiki en

[Wiki en表示]

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. 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.^[4]

1 Chemistry
2 History
3 Biosynthesis
4 Function and uses
- 4.1 Metabolism
- 4.2 Neurotransmitter
- 4.3 Brain nonsynaptic glutamatergic signaling circuits
  - 4.3.1 GABA precursor
- 4.4 Flavor enhancer
- 4.5 Nutrient
- 4.6 Plant growth
- 4.7 NMR spectroscopy
5 Production
6 Pharmacology
7 See also
8 References
9 External links
10 Further reading

Chemistry

The side chain carboxylic acid functional group has a pK_a 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.

History

Although they occur naturally in many foods, the flavor 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 Ritthausen who treated wheat gluten (for which it was named) with sulfuric acid.^[5] 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 flavor he detected in many foods, most especially in seaweed. Professor Ikeda termed this flavor umami. He then patented a method of mass-producing a crystalline salt of glutamic acid, monosodium glutamate.^[6]^[7]

Biosynthesis

Reactants	Products	Enzymes
Glutamine + H₂O	→ Glu + NH₃	GLS, GLS2
NAcGlu + H₂O	→ Glu + Acetate	N-acetyl-glutamate synthase
α-ketoglutarate + NADPH + NH₄⁺	→ Glu + NADP⁺ + H₂O	GLUD1, GLUD2^[8]
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

Metabolism

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,^[8] 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

Glutamate is the most abundant excitatory neurotransmitter in the vertebrate nervous system.^[9] 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 or the AMPA 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.^[10] 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.^[11] In addition, glutamate plays important roles in the regulation of growth cones and synaptogenesis during brain development as originally described by Mark Mattson.

Glutamate transporters^[12] 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

Damage to mitochondria from excessively high intracellular Ca²⁺^[13]

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,^[4] autism, some forms of intellectual disability, and diseases like amyotrophic lateral sclerosis, lathyrism, and Alzheimer's disease.^[4]^[14] In contrast, decreased glutamate release is observed under conditions of classical phenylketonuria^[15] leading to developmental disruption of glutamate receptor expression.^[16]

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.^[17] 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.^[18] 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.^[19] 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.^[20] These receptors have also been described in arthropods, such as Drosophila melanogaster^[21] and Lepeophtheirus salmonis.^[22] 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.

L-Glutamate at physiological conditions

Brain nonsynaptic glutamatergic signaling circuits

Extracellular glutamate in Drosophila brains has been found to regulate postsynaptic glutamate receptor clustering, via a process involving receptor desensitization.^[23] A gene expressed in glial cells actively transports glutamate into the extracellular space,^[23] while, in the nucleus accumbens-stimulating group II metabotropic glutamate receptors, this gene was found to reduce extracellular glutamate levels.^[24] This raises the possibility that this extracellular glutamate plays an "endocrine-like" role as part of a larger homeostatic system.

GABA precursor

Glutamate also serves as the precursor for the synthesis of the inhibitory gamma-aminobutyric acid (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 has abundant GAD, a direct immunological destruction occurs in the pancreas and the patients will have diabetes mellitus.

Flavor enhancer

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 flavor enhancer in the form of its salt, known as monosodium glutamate (MSG).

Nutrient

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.^[25]

Plant growth

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

NMR spectroscopy

In recent years, there has been much research into the use of residual dipolar coupling (RDC) in nuclear magnetic resonance spectroscopy (NMR). 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.^[26]

Production

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

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.^[27] LY354740 has also been demonstrated to act on the metabotropic glutamate receptor 3 (GRM3) of human adrenocortical cells, downregulating aldosterone synthase, CYP11B1, and the production of adrenal steroids (i.e. aldosterone and cortisol).^[28] Glutamate does not easily pass the blood brain barrier, but, instead, is transported by a high-affinity transport system.^[29] It can also be converted into glutamine.

References

^ http://hazard.com/msds/mf/baker/baker/files/g3970.htm
^ Belitz, H.-D; Grosch, Werner; Schieberle, Peter (2009-02-27). Food Chemistry. ISBN 9783540699330.
^ http://www.cem.msu.edu/~cem252/sp97/ch24/ch24aa.html
^ ^a ^b ^c Robert Sapolsky (2005). "Biology and Human Behavior: The Neurological Origins of Individuality, 2nd edition". The Teaching Company. "see pages 19 and 20 of Guide Book"
^ R.H.A. Plimmer (1912) [1908]. R.H.A. Plimmer & F.G. Hopkins, ed. The Chemical Constitution of the Protein. Monographs on biochemistry. Part I. Analysis (2nd ed.). London: Longmans, Green and Co. p. 114. Retrieved June 3, 2012.
^ Renton, Alex (2005-07-10). "If MSG is so bad for you, why doesn't everyone in Asia have a headache?". The Guardian. Retrieved 2008-11-21.
^ "Kikunae Ikeda Sodium Glutamate". Japan Patent Office. 2002-10-07. Retrieved 2008-11-21.
^ ^a ^b Grabowska, A.; Nowicki, M.; Kwinta, J. (2011). "Glutamate dehydrogenase of the germinating triticale seeds: Gene expression, activity distribution and kinetic characteristics". Acta Physiologiae Plantarum 33 (5): 1981. doi:10.1007/s11738-011-0801-1. edit
^ Meldrum, B. S. (2000). "Glutamate as a neurotransmitter in the brain: Review of physiology and pathology". The Journal of nutrition 130 (4S Suppl): 1007S–1015S. PMID 10736372. edit
^ McEntee, W. J.; Crook, T. H. (1993). "Glutamate: Its role in learning, memory, and the aging brain". Psychopharmacology 111 (4): 391–401. doi:10.1007/BF02253527. PMID 7870979. edit
^ Okubo, Y.; Sekiya, H.; Namiki, S.; Sakamoto, H.; Iinuma, S.; Yamasaki, M.; Watanabe, M.; Hirose, K.; Iino, M. (2010). "Imaging extrasynaptic glutamate dynamics in the brain". Proceedings of the National Academy of Sciences 107 (14): 6526. doi:10.1073/pnas.0913154107. edit
^ Shigeri, Y.; Seal, R. P.; Shimamoto, K. (2004). "Molecular pharmacology of glutamate transporters, EAATs and VGLUTs". Brain Research Reviews 45 (3): 250–265. doi:10.1016/j.brainresrev.2004.04.004. PMID 15210307. edit
^ Manev, H.; Favaron, M.; Guidotti, A.; Costa, E. (1989). "Delayed increase of Ca2+ influx elicited by glutamate: Role in neuronal death". Molecular Pharmacology 36 (1): 106–112. PMID 2568579. edit
^ Hynd, M.; Scott, H. L.; Dodd, P. R. (2004). "Glutamate-mediated excitotoxicity and neurodegeneration in Alzheimer?s disease". Neurochemistry International 45 (5): 583–595. doi:10.1016/j.neuint.2004.03.007. PMID 15234100. edit
^ Glushakov, AV; Dennis, DM; Sumners, C; Seubert, CN; Martynyuk, AE (Apr 1, 2003). "L-phenylalanine selectively depresses currents at glutamatergic excitatory synapses". Journal of neuroscience research 72 (1): 116–24. doi:10.1002/jnr.10569. PMID 12645085. Cite uses deprecated parameters (help)
^ Glushakov, AV; Glushakova, O; Varshney, M; Bajpai, LK; Sumners, C; Laipis, PJ; Embury, JE; Baker, SP; Otero, DH; Dennis, DM; Seubert, CN; Martynyuk, AE (February 2005). "Long-term changes in glutamatergic synaptic transmission in phenylketonuria". Brain : a journal of neurology 128 (Pt 2): 300–7. doi:10.1093/brain/awh354. PMID 15634735. Cite uses deprecated parameters (help)
^ Okumoto, S.; Looger, L. L.; Micheva, K. D.; Reimer, R. J.; Smith, S. J.; Frommer, W. B. (2005). "Detection of glutamate release from neurons by genetically encoded surface-displayed FRET nanosensors". Proceedings of the National Academy of Sciences 102 (24): 8740. doi:10.1073/pnas.0503274102. edit
^ Ellis-Davies, G. C. R.; Matsuzaki, M.; Paukert, M.; Kasai, H.; Bergles, D. E. (2007). "4-Carboxymethoxy-5,7-Dinitroindolinyl-Glu: An Improved Caged Glutamate for Expeditious Ultraviolet and Two-Photon Photolysis in Brain Slices". Journal of Neuroscience 27 (25): 6601–6604. doi:10.1523/jneurosci.1519-07.2007. PMID 17581946. edit
^ Laughton, D. L.; Wheeler, S. V.; Lunt, G. G.; Wolstenholme, A. J. (2002). "The β-Subunit of Caenorhabditis elegans Avermectin Receptor Responds to Glycine and is Encoded by Chromosome 1". Journal of Neurochemistry 64 (5): 2354–2357. doi:10.1046/j.1471-4159.1995.64052354.x. PMID 7536811. edit
^ Cully, D. F.; Vassilatis, D. K.; Liu, K. K.; Paress, P. S.; Van Der Ploeg, L. H. T.; Schaeffer, J. M.; Arena, J. P. (1994). "Cloning of an avermectin-sensitive glutamate-gated chloride channel from Caenorhabditis elegans". Nature 371 (6499): 707–711. doi:10.1038/371707a0. PMID 7935817. edit
^ 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'
^ Tribble, N. D.; Burka, J. F.; Kibenge, F. S. B. (2007). "Identification of the genes encoding for putative gamma aminobutyric acid (GABA) and glutamate-gated chloride channel (GluCl) alpha receptor subunits in sea lice (Lepeophtheirus salmonis)". Journal of Veterinary Pharmacology and Therapeutics 30 (2): 163–167. doi:10.1111/j.1365-2885.2007.00823.x. PMID 17348903. edit
^ ^a ^b 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. doi:10.1523/JNEUROSCI.4770-06.2007. PMC 2193629. PMID 17202478.
^ 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. doi:10.1124/jpet.300.1.162. PMID 11752112.
^ Reeds, P.J., et al. (1 April 2000). "Intestinal glutamate metabolism". Journal of Nutrition 130 (4s): 978S–982S. PMID 10736365.
^ C. M. Thiele, Concepts Magn. Reson. A, 2007, 30A, 65-80
^ 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. PMID 15573025.
^ Felizola SJA, Nakamura Y, Satoh F, Morimoto R, Kikuchi K, Nakamura T, Hozawa A, Wang L, Onodera Y, Ise K, McNamara KM, Midorikawa S, Suzuki S, Sasano H (January 2014). "Glutamate receptors and the regulation of steroidogenesis in the human adrenal gland: The metabotropic pathway.". Molecular and Cellular Endocrinology 382 (1): 170–177. doi:10.1016/j.mce.2013.09.025. PMID 24080311.
^ Smith QR (April 2000). "Transport of glutamate and other amino acids at the blood–brain barrier". J. Nutr. 130 (4S Suppl): 1016S–22S. PMID 10736373.

External links

Look up glutamic acid in Wiktionary, the free dictionary.

Glutamic acid MS Spectrum

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We report a hydrothermal method to prepare reduced graphene oxide (rGO)-based hydrogel (GelrGONR), using neutral red (NR) to mediate the assembly of rGO sheets and tune the pore size of GelrGONR. A series of techniques including scanning electron microscopy (SEM), X-ray photoelectron spectroscopy (X
PMID 25129511

Effects of charge-carrying amino acids on the gelatinization and retrogradation properties of potato starch.

Chen W1, Zhou H1, Yang H2, Cui M3.
Food chemistry.Food Chem.2015 Jan 15;167:180-4. doi: 10.1016/j.foodchem.2014.06.089. Epub 2014 Jun 30.
The objective of this study was to evaluate the effects of charge-carrying amino acids (lysine (Lys), arginine (Arg), aspartic acid (Asp) and glutamic acid (Glu)) on the gelatinization and retrogradation properties of potato starch. Acidic amino acids (Asp and Glu) showed a decreasing trend in swell
PMID 25148976

Japanese Journal

Somatosensory and Visual Deprivation Each Decrease the Density of Parvalbumin Neurons and Their Synapse Terminals in the Prefrontal Cortex and Hippocampus of Mice

Ueno Hiroshi,Shoshi Chikafumi,Suemitsu Shunsuke,Usui Shinichi,Sujiura Hiroko,Okamoto Motoi
Acta Medica Okayama 67(3), 135-143, 2013-06-00
… We used a mouse model to examine the effects of sensory deprivation achieved by whisker trimming and visual deprivation achieved by dark rearing in neonatal mice on the appearance of parvalbumin (PV) neurons and the formation of glutamic acid decarboxylase 67 (GAD67)-positive puncta around pyramidal neurons in the prefrontal cortex and hippocampus. …
NAID 120005295912

きのこ類を用いた味噌の試醸とその化学成分

本間裕人,中村和夫,川村拓未,徳田宏晴,中西戴慶
日本きのこ学会誌 : mushroom science and biotechnology 21(1), 23-29, 2013-04-30
きのこ類を用いて味噌の製造を行った.味噌の製造に利用可能なきのこ類の選抜を行ったところ,11株のきのこ類において顕著な耐塩性プロテアーゼの生産性が認められた.そこでそれらの菌株を用いて実際に味噌を試醸したところ,すべての菌株において28日間の熟成で柔らかいペースト状となり,きのこ味噌を製造することができた.製造したきのこ味噌の一般食品成分分析を行ったところ,いずれも市販米甘口味噌に近い値を示した. …
NAID 110009604524

Related Pictures

★リンクテーブル★

リンク元	「グルタミン酸」「L-glutamate」「L-glutamic acid」「Glu」「D-glutamate」
拡張検索	「1-carboxyglutamic acid」「gamma-carboxyglutamic acid」「pteroylglutamic acid」「glutamic acid decarboxylase」「γ-carboxyglutamic acid」
関連記事	「glutamic」

「グルタミン酸」

Glutamic acid
	Systematic name 2-Aminopentanedioic acid
	Other names 2-Aminoglutaric acid
Identifiers
CAS number	617-65-2
ChemSpider	591
UNII	61LJO5I15S
KEGG	D04341
ChEBI	CHEBI:18237
ChEMBL	CHEMBL276389
Jmol-3D images	Image 1
	SMILES C(CC(=O)O)C(C(=O)O)N ;
	InChI InChI=1S/C5H9NO4/c6-3(5(9)10)1-2-4(7)8/h3H,1-2,6H2,(H,7,8)(H,9,10) ; Key: WHUUTDBJXJRKMK-UHFFFAOYSA-N InChI=1/C5H9NO4/c6-3(5(9)10)1-2-4(7)8/h3H,1-2,6H2,(H,7,8)(H,9,10); Key: WHUUTDBJXJRKMK-UHFFFAOYAD ;
Properties
Molecular formula	C5H9NO4
Molar mass	147.13 g mol−1
Appearance	white crystalline powder
Density	1.4601 (20 °C)
Melting point	199 °C decomp.
Solubility in water	8.64 g/l (25 °C)
Solubility	0.00035g/100g ethanol 25 degC
Acidity (pKa)	2.1, 4.07, 9.47
Hazards
MSDS	External MSDS
NFPA 704	1 2 0
Supplementary data page
Structure and; properties	n, εr, etc.
Thermodynamic; data	Phase behaviour; Solid, liquid, gas
Spectral data	UV, IR, NMR, MS
	Except where noted otherwise, data are given for materials in their standard state (at 25 °C (77 °F), 100 kPa)
	(verify) (what is: /?)
	Infobox references

グルタミン酸
	IUPAC名 Glutamic acid
	別称 2-Aminopentanedioic acid; 2-Aminoglutaric acid
識別情報
CAS登録番号	617-65-2 , ; 56-86-0 (L-isomer); 6893-26-1 (D-isomer)
PubChem	611
ChemSpider	591
UNII	61LJO5I15S
EINECS番号	210-522-2
KEGG	D04341
ChEMBL	CHEMBL276389
IUPHARリガンド	1369
	SMILES C(CC(=O)O)C(C(=O)O)N;
	InChI InChI=1S/C5H9NO4/c6-3(5(9)10)1-2-4(7)8/h3H,1-2,6H2,(H,7,8)(H,9,10) ; Key: WHUUTDBJXJRKMK-UHFFFAOYSA-N InChI=1/C5H9NO4/c6-3(5(9)10)1-2-4(7)8/h3H,1-2,6H2,(H,7,8)(H,9,10); Key: WHUUTDBJXJRKMK-UHFFFAOYAD;
特性
化学式	C5H9NO4
モル質量	147.13 g mol−1
外観	白色結晶性粉末
密度	1.4601 (20 °C)
融点	199 °C（分解）
水への溶解度	soluble
	特記なき場合、データは常温 (25 °C)・常圧 (100 kPa) におけるものである。

　　[★]

英: glutamate, glutamic acid, Glu, E
同: α-アミノグルタル酸 2-アミノグルタル酸 2-アミノペンタン二酸 2-aminopentanedioic acid
関: アミノ酸、D-glutamate、L-glutamate

概念

極性。酸性。
生理活性アミン。4-アミノ酪酸、GABAの材料
カルボキシル基を有する。
アラニンの側鎖に-CH2-がつき、さらにカルボキシル基がついた形をしている。

-CH2-CH2-COOH

「L-glutamate」

　　[★]

L-グルタミン酸、L-グルタミン酸塩

関: D-glutamate、glutamate、glutamic acid、L-glutamic acid

「L-glutamic acid」

　　[★]

L-グルタミン酸

関: D-glutamate、E、Glu、glutamate、glutamic、glutamic acid、L-glutamate

「Glu」

　　[★]

グルタミン酸

関: E、glutamate、glutamic、glutamic acid、L-glutamic acid

「D-glutamate」

　　[★]

D-グルタミン酸

関: glutamate、glutamic acid、L-glutamate、L-glutamic acid

「1-carboxyglutamic acid」

　　[★]

1-カルボキシグルタミン酸、γカルボキシグルタミン酸

関: gamma-carboxyglutamate、gamma-carboxyglutamic acid、Gla

「gamma-carboxyglutamic acid」

　　[★]

γカルボキシグルタミン酸

関: 1-carboxyglutamic acid、gamma-carboxyglutamate、Gla

「pteroylglutamic acid」

　　[★] 葉酸。プテロイルグルタミン酸

「glutamic acid decarboxylase」

　　[★] グルタミン酸脱炭酸酵素 GAD

「γ-carboxyglutamic acid」

　　[★] γ-カルボキシグルタミン酸

「glutamic」

　　[★]

グルタミン酸の

関: E、Glu、glutamate、glutamic acid、L-glutamic acid

[shiga-1] 痛みと鎮痛の基礎知識 - Pain Relief - 伝達物質

[kaken-2] グルタミン酸の興奮毒性に拮抗する内因性アミノ酸の存在様式と機能的役割

[3] 神経毒

[4] NMDA型グルタミン酸受容体

[5] マグネシウム

[1] ttp://hazard.com/msds/mf/baker/baker/files/g3970.htm

[2] Belitz, H.-D; Grosch, Werner; Schieberle, Peter (2009-02-27). Food Chemistry. ISBN 9783540699330.

[3] ttp://www.cem.msu.edu/~cem252/sp97/ch24/ch24aa.html

[twsNovK11-4] Robert Sapolsky (2005). "Biology and Human Behavior: The Neurological Origins of Individuality, 2nd edition". The Teaching Company. "see pages 19 and 20 of Guide Book"

[5] R.H.A. Plimmer (1912) [1908]. R.H.A. Plimmer & F.G. Hopkins, ed. The Chemical Constitution of the Protein. Monographs on biochemistry. Part I. Analysis (2nd ed.). London: Longmans, Green and Co. p. 114. Retrieved June 3, 2012.

[guardian-6] Renton, Alex (2005-07-10). "If MSG is so bad for you, why doesn't everyone in Asia have a headache?". The Guardian. Retrieved 2008-11-21.

[7] "Kikunae Ikeda Sodium Glutamate". Japan Patent Office. 2002-10-07. Retrieved 2008-11-21.

[springerlink-8] Grabowska, A.; Nowicki, M.; Kwinta, J. (2011). "Glutamate dehydrogenase of the germinating triticale seeds: Gene expression, activity distribution and kinetic characteristics". Acta Physiologiae Plantarum 33 (5): 1981. doi:10.1007/s11738-011-0801-1. edit

[pmid10736372-9] Meldrum, B. S. (2000). "Glutamate as a neurotransmitter in the brain: Review of physiology and pathology". The Journal of nutrition 130 (4S Suppl): 1007S–1015S. PMID 10736372. edit

[10] McEntee, W. J.; Crook, T. H. (1993). "Glutamate: Its role in learning, memory, and the aging brain". Psychopharmacology 111 (4): 391–401. doi:10.1007/BF02253527. PMID 7870979. edit

[11] Okubo, Y.; Sekiya, H.; Namiki, S.; Sakamoto, H.; Iinuma, S.; Yamasaki, M.; Watanabe, M.; Hirose, K.; Iino, M. (2010). "Imaging extrasynaptic glutamate dynamics in the brain". Proceedings of the National Academy of Sciences 107 (14): 6526. doi:10.1073/pnas.0913154107. edit

[12] Shigeri, Y.; Seal, R. P.; Shimamoto, K. (2004). "Molecular pharmacology of glutamate transporters, EAATs and VGLUTs". Brain Research Reviews 45 (3): 250–265. doi:10.1016/j.brainresrev.2004.04.004. PMID 15210307. edit

[13] Manev, H.; Favaron, M.; Guidotti, A.; Costa, E. (1989). "Delayed increase of Ca2+ influx elicited by glutamate: Role in neuronal death". Molecular Pharmacology 36 (1): 106–112. PMID 2568579. edit

[14] Hynd, M.; Scott, H. L.; Dodd, P. R. (2004). "Glutamate-mediated excitotoxicity and neurodegeneration in Alzheimer?s disease". Neurochemistry International 45 (5): 583–595. doi:10.1016/j.neuint.2004.03.007. PMID 15234100. edit

[15] Glushakov, AV; Dennis, DM; Sumners, C; Seubert, CN; Martynyuk, AE (Apr 1, 2003). "L-phenylalanine selectively depresses currents at glutamatergic excitatory synapses". Journal of neuroscience research 72 (1): 116–24. doi:10.1002/jnr.10569. PMID 12645085. Cite uses deprecated parameters (help)

[16] Glushakov, AV; Glushakova, O; Varshney, M; Bajpai, LK; Sumners, C; Laipis, PJ; Embury, JE; Baker, SP; Otero, DH; Dennis, DM; Seubert, CN; Martynyuk, AE (February 2005). "Long-term changes in glutamatergic synaptic transmission in phenylketonuria". Brain : a journal of neurology 128 (Pt 2): 300–7. doi:10.1093/brain/awh354. PMID 15634735. Cite uses deprecated parameters (help)

[17] Okumoto, S.; Looger, L. L.; Micheva, K. D.; Reimer, R. J.; Smith, S. J.; Frommer, W. B. (2005). "Detection of glutamate release from neurons by genetically encoded surface-displayed FRET nanosensors". Proceedings of the National Academy of Sciences 102 (24): 8740. doi:10.1073/pnas.0503274102. edit

[18] Ellis-Davies, G. C. R.; Matsuzaki, M.; Paukert, M.; Kasai, H.; Bergles, D. E. (2007). "4-Carboxymethoxy-5,7-Dinitroindolinyl-Glu: An Improved Caged Glutamate for Expeditious Ultraviolet and Two-Photon Photolysis in Brain Slices". Journal of Neuroscience 27 (25): 6601–6604. doi:10.1523/jneurosci.1519-07.2007. PMID 17581946. edit

[19] Laughton, D. L.; Wheeler, S. V.; Lunt, G. G.; Wolstenholme, A. J. (2002). "The β-Subunit of Caenorhabditis elegans Avermectin Receptor Responds to Glycine and is Encoded by Chromosome 1". Journal of Neurochemistry 64 (5): 2354–2357. doi:10.1046/j.1471-4159.1995.64052354.x. PMID 7536811. edit

[20] Cully, D. F.; Vassilatis, D. K.; Liu, K. K.; Paress, P. S.; Van Der Ploeg, L. H. T.; Schaeffer, J. M.; Arena, J. P. (1994). "Cloning of an avermectin-sensitive glutamate-gated chloride channel from Caenorhabditis elegans". Nature 371 (6499): 707–711. doi:10.1038/371707a0. PMID 7935817. edit

[21] 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'

[22] Tribble, N. D.; Burka, J. F.; Kibenge, F. S. B. (2007). "Identification of the genes encoding for putative gamma aminobutyric acid (GABA) and glutamate-gated chloride channel (GluCl) alpha receptor subunits in sea lice (Lepeophtheirus salmonis)". Journal of Veterinary Pharmacology and Therapeutics 30 (2): 163–167. doi:10.1111/j.1365-2885.2007.00823.x. PMID 17348903. edit

[augustin-23] 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. doi:10.1523/JNEUROSCI.4770-06.2007. PMC 2193629. PMID 17202478.

[24] 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. doi:10.1124/jpet.300.1.162. PMID 11752112.

[25] Reeds, P.J., et al. (1 April 2000). "Intestinal glutamate metabolism". Journal of Nutrition 130 (4s): 978S–982S. PMID 10736365.

[26] C. M. Thiele, Concepts Magn. Reson. A, 2007, 30A, 65-80

[27] 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. PMID 15573025.

[28] Felizola SJA, Nakamura Y, Satoh F, Morimoto R, Kikuchi K, Nakamura T, Hozawa A, Wang L, Onodera Y, Ise K, McNamara KM, Midorikawa S, Suzuki S, Sasano H (January 2014). "Glutamate receptors and the regulation of steroidogenesis in the human adrenal gland: The metabotropic pathway.". Molecular and Cellular Endocrinology 382 (1): 170–177. doi:10.1016/j.mce.2013.09.025. PMID 24080311.

[29] Smith QR (April 2000). "Transport of glutamate and other amino acids at the blood–brain barrier". J. Nutr. 130 (4S Suppl): 1016S–22S. PMID 10736373.

グルタミン酸


IUPAC名 Glutamic acid
別称 2-Aminopentanedioic acid 2-Aminoglutaric acid
識別情報
CAS登録番号	617-65-2, 56-86-0 (L-isomer) 6893-26-1 (D-isomer)
PubChem	611
ChemSpider	591
UNII	61LJO5I15S
EINECS番号	210-522-2
KEGG	D04341
ChEMBL	CHEMBL276389
IUPHARリガンド	1369
SMILES C(CC(=O)O)C(C(=O)O)N
InChI InChI=1S/C5H9NO4/c6-3(5(9)10)1-2-4(7)8/h3H,1-2,6H2,(H,7,8)(H,9,10) Key: WHUUTDBJXJRKMK-UHFFFAOYSA-N InChI=1/C5H9NO4/c6-3(5(9)10)1-2-4(7)8/h3H,1-2,6H2,(H,7,8)(H,9,10) Key: WHUUTDBJXJRKMK-UHFFFAOYAD
特性
化学式	C₅H₉NO₄
モル質量	147.13 g mol⁻¹
外観	白色結晶性粉末
密度	1.4601 (20 °C)
融点	199 °C（分解）
水への溶解度	soluble
特記なき場合、データは常温 (25 °C)・常圧 (100 kPa) におけるものである。

匿名

検索

案内

glutamic acid