How To Draw Glutamate At Ph 2, 7 And 9

Amino acid and neurotransmitter

Glutamic acid

Skeletal formula of L -glutamic acrid
Ball-and-stick model Space-filling model
Names
Systematic IUPAC name ii-Aminopentanedioic acrid
Other names 2-Aminoglutaric acrid
Identifiers
CAS Number	l isomer: 56-86-0 Y racemate: 617-65-two Y d isomer: 6893-26-1 Y
3D model (JSmol)	fifty isomer: Interactive image d isomer: Interactive image Zwitterion: Interactive image Deprotonated zwitterion: Interactive paradigm
3DMet	l isomer: B00007
Beilstein Reference	1723801 (L) 1723799 (rac) 1723800 (D)
ChEBI	50 isomer: CHEBI:16015 Y racemate: CHEBI:18237 d isomer: CHEBI:15966
ChEMBL	l isomer: ChEMBL575060 Y
ChemSpider	l isomer: 591 Y
DrugBank	l isomer: DB00142 d isomer: DB02517
ECHA InfoCard	100.009.567
EC Number	l isomer: 200-293-7
Eastward number	E620 (flavour enhancer)
Gmelin Reference	3502 (L) 101971 (rac) 202289 (D)
KEGG	50 isomer: C00025 Due north d isomer: C00217
PubChem CID	50 isomer: 33032 d isomer: 23327
UNII	l isomer: 3KX376GY7L Y racemate: 61LJO5I15S Y d isomer: Q479989WEA Y
CompTox Dashboard (EPA)	50 isomer: DTXSID0046987
InChI InChI=1S/C5H9NO4/c6-3(5(9)10)1-ii-4(7)eight/h3H,1-two,6H2,(H,7,viii)(H,9,x) Y Key: WHUUTDBJXJRKMK-UHFFFAOYSA-N Y l isomer: InChI=ane/C5H9NO4/c6-3(5(9)10)1-2-4(7)8/h3H,1-2,6H2,(H,7,viii)(H,9,x) Primal: WHUUTDBJXJRKMK-UHFFFAOYAD
SMILES l isomer: C(CC(=O)O)[C@@H](C(=O)O)N d isomer: C(CC(=O)O)[C@H](C(=O)O)Northward Zwitterion: C(CC(=O)O)C(C(=O)[O-])[NH3+] Deprotonated zwitterion: C(CC(=O)[O-])C(C(=O)[O-])[NH3+]
Backdrop
Chemical formula	C 5 H 9 Due north O 4
Molar mass	147.130 g·mol−ane
Advent	white crystalline powder
Density	1.4601 (20 °C)
Melting bespeak	199 °C (390 °F; 472 K) decomposes
Solubility in water	seven.v thou/Fifty (20 °C)[1]
Solubility	0.00035 g/100 g ethanol (25 °C)[2]
Acidity (pThou a)	2.ten, iv.07, 9.47[three]
Magnetic susceptibility (χ)	−78.v·10−6 cmiii/mol
Hazards
GHS labelling:
Pictograms
Signal give-and-take	Warning
Chance statements	H315, H319, H335
Precautionary statements	P261, P264, P271, P280, P302+P352, P304+P340, P305+P351+P338, P312, P321, P332+P313, P337+P313, P362, P403+P233, P405, P501
NFPA 704 (burn diamond)	2 1 0
Supplementary information page
Glutamic acid (data page)
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
Yverify (what is Y N  ?)
Infobox references

Chemic compound

Glutamic acid (symbol Glu or Due east;^[4] the ionic form is known every bit glutamate) is an α-amino acid that is used by almost all living beings in the biosynthesis of proteins. It is not-essential in humans, meaning that the torso tin synthesize it. Information technology is also an excitatory neurotransmitter, in fact the most abundant ane, in the vertebrate nervous system. It serves as the forerunner for the synthesis of the inhibitory gamma-aminobutyric acid (GABA) in GABA-ergic neurons.

Its molecular formula is C
_five H
₉ NO
_four . Glutamic acid exists in three optically isomeric forms; the dextrorotatory L -class is ordinarily obtained by hydrolysis of gluten or from the waste waters of beet-sugar manufacture or by fermentation.^[5] Its molecular structure could be idealized as HOOC−CH(NH
_two )−(CH
_two )₂−COOH, with two carboxyl groups −COOH and one amino group −NH
₂ . Notwithstanding, in the solid state and mildly acidic water solutions, the molecule assumes an electrically neutral zwitterion structure ⁻OOC−CH(NH ⁺
₃ )−(CH
₂ )₂−COOH. It is encoded by the codons GAA or GAG.

The acid tin lose i proton from its second carboxyl grouping to form the conjugate base, the singly-negative anion glutamate ⁻OOC−CH(NH ⁺
_three )−(CH
_two )₂−COO⁻. This class of the compound is prevalent in neutral solutions. The glutamate neurotransmitter plays the principal role in neural activation.^[6] This anion creates the savory umami flavor of foods and is found in glutamate flavorings such as MSG. In Europe it is classified as nutrient additive E620. In highly alkaline metal solutions the doubly negative anion ⁻OOC−CH(NH
₂ )−(CH
_ii )₂−COO⁻ prevails. The radical corresponding to glutamate is chosen glutamyl.

Chemistry [edit]

Ionization [edit]

When glutamic acid is dissolved in water, the amino grouping (−NH
_two ) may proceeds a proton (H ⁺
), and/or the carboxyl groups may lose protons, depending on the acidity of the medium.

In sufficiently acidic environments, the amino group gains a proton and the molecule becomes a cation with a unmarried positive accuse, HOOC−CH(NH ⁺
_iii )−(CH
_two )_ii−COOH.^[7]

At pH values betwixt virtually 2.v and 4.i,^[7] the carboxylic acrid closer to the amine generally loses a proton, and the acrid becomes the neutral zwitterion ⁻OOC−CH(NH ⁺
_three )−(CH
₂ )₂−COOH. This is likewise the form of the chemical compound in the crystalline solid state.^{[8] [ix]} The change in protonation country is gradual; the two forms are in equal concentrations at pH 2.ten.^[10]

At fifty-fifty college pH, the other carboxylic acid grouping loses its proton and the acid exists nearly entirely as the glutamate anion ⁻OOC−CH(NH ⁺
₃ )−(CH
₂ )₂−COO⁻, with a single negative accuse overall. The change in protonation state occurs at pH iv.07.^[10] This form with both carboxylates lacking protons is dominant in the physiological pH range (vii.35–7.45).

At fifty-fifty higher pH, the amino grouping loses the extra proton, and the prevalent species is the doubly-negative anion ⁻OOC−CH(NH
_ii )−(CH
_ii )₂−COO⁻. The alter in protonation state occurs at pH 9.47.^[10]

Optical isomerism [edit]

The carbon atom adjacent to the amino group is chiral (connected to 4 distinct groups). Glutamic acrid can exist in 3^[5] optical isomers, including the dextrorotatory L -form,^[five] d(−), and 50(+). The l form is the ane most widely occurring in nature, only the d class occurs in some special contexts, such every bit the cell walls of the leaner (which tin can manufacture it from the l form with the enzyme glutamate racemase) and the liver of mammals.^{[11] [12]}

History [edit]

Although they occur naturally in many foods, the flavor contributions fabricated by glutamic acrid and other amino acids were only scientifically identified early in the 20th century. The substance was discovered and identified in the year 1866 by the German chemist Karl Heinrich Ritthausen, who treated wheat gluten (for which information technology was named) with sulfuric acid.^[13] In 1908, Japanese researcher Kikunae Ikeda of the Tokyo Imperial Academy 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 common salt of glutamic acid, monosodium glutamate.^{[14] [15]}

Synthesis [edit]

Biosynthesis [edit]

Reactants	Products	Enzymes
Glutamine + H2O	→ Glu + NHthree	GLS, GLS2
NAcGlu + H2O	→ Glu + Acetate	N-acetyl-glutamate synthase
α-ketoglutarate + NADPH + NH4 +	→ Glu + NADP+ + H2O	GLUD1, GLUD2[16]
α-ketoglutarate + α-amino acrid	→ 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

Industrial synthesis [edit]

Glutamic acid is produced on the largest scale of whatsoever amino acid, with an estimated annual production of nearly 1.v million tons in 2006.^[17] Chemical synthesis was supplanted by the aerobic fermentation of sugars and ammonia in the 1950s, with the organism Corynebacterium glutamicum (as well known as Brevibacterium flavum) being the most widely used for production.^[xviii] Isolation and purification can be achieved past concentration and crystallization; information technology is likewise widely available as its hydrochloride table salt.^[19]

Office and uses [edit]

Metabolism [edit]

Glutamate is a key compound in cellular metabolism. In humans, dietary proteins are broken downward by digestion into amino acids, which serve as metabolic fuel for other functional roles in the torso. 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 tin can be generalised as such:

R₁-amino acid + R_ii-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 1 as well, which tin contribute equally fuel or as a substrate for further metabolism processes. Examples are equally 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 acrid bicycle.

Glutamate too plays an important role in the torso'south disposal of excess or waste nitrogen. Glutamate undergoes deamination, an oxidative reaction catalysed by glutamate dehydrogenase,^[16] as follows:

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

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

Glutamate is likewise a neurotransmitter (run into below), which makes it i of the most abundant molecules in the encephalon. Malignant brain tumors known as glioma or glioblastoma exploit this phenomenon by using glutamate as an energy source, specially when these tumors get more dependent on glutamate due to mutations in the factor IDH1.^{[20] [21]}

Neurotransmitter [edit]

Glutamate is the near abundant excitatory neurotransmitter in the vertebrate nervous system.^[22] At chemic synapses, glutamate is stored in vesicles. Nerve impulses trigger the release of glutamate from the presynaptic jail cell. Glutamate acts on ionotropic and metabotropic (G-poly peptide coupled) receptors.^[22] In the opposing postsynaptic cell, glutamate receptors, such as the NMDA receptor or the AMPA receptor, bind glutamate and are activated. Considering of its role in synaptic plasticity, glutamate is involved in cognitive functions such equally learning and memory in the brain.^[23] The grade of plasticity known as long-term potentiation takes place at glutamatergic synapses in the hippocampus, neocortex, and other parts of the encephalon. Glutamate works not only every bit 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.^[24] In addition, glutamate plays important roles in the regulation of growth cones and synaptogenesis during brain evolution equally originally described by Mark Mattson.

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.^[25] A cistron expressed in glial cells actively transports glutamate into the extracellular space,^[25] while, in the nucleus accumbens-stimulating group Two metabotropic glutamate receptors, this gene was found to reduce extracellular glutamate levels.^[26] This raises the possibility that this extracellular glutamate plays an "endocrine-like" function as part of a larger homeostatic system.

GABA precursor [edit]

Glutamate besides serves every bit the precursor for the synthesis of the inhibitory gamma-aminobutyric acid (GABA) in GABA-ergic neurons. This reaction is catalyzed past glutamate decarboxylase (GAD), which is most abundant in the cerebellum and pancreas.^{[ commendation needed ]}

Strong person syndrome is a neurologic disorder acquired by anti-GAD antibodies, leading to a subtract in GABA synthesis and, therefore, impaired motor function such as musculus stiffness and spasm. Since the pancreas has abundant GAD, a directly immunological devastation occurs in the pancreas and the patients volition accept diabetes mellitus.^{[ citation needed ]}

Flavor enhancer [edit]

Glutamic acid, existence a elective of poly peptide, is present in foods that contain protein, only it can only be tasted when information technology is present in an unbound grade. Significant amounts of gratis glutamic acid are nowadays in a wide multifariousness of foods, including cheeses and soy sauce, and glutamic acid is responsible for umami, one of the five bones tastes of the man sense of gustatory modality. Glutamic acid often is used as a food additive and flavor enhancer in the class of its sodium salt, known equally monosodium glutamate (MSG).

Nutrient [edit]

All meats, poultry, fish, eggs, dairy products, and kombu are splendid sources of glutamic acrid. Some protein-rich plant foods besides serve as sources. 30% to 35% of gluten (much of the poly peptide in wheat) is glutamic acid. Ninety-5 percent of the dietary glutamate is metabolized by intestinal cells in a showtime pass.^[27]

Institute growth [edit]

Auxigro is a institute growth preparation that contains xxx% glutamic acid.

NMR spectroscopy [edit]

In contempo years,^{[ when? ]} in that location has been much inquiry into the use of rest dipolar coupling (RDC) in nuclear magnetic resonance spectroscopy (NMR). A glutamic acrid derivative, poly-γ-benzyl-Fifty-glutamate (PBLG), is oftentimes used equally an alignment medium to command the calibration of the dipolar interactions observed.^[28]

Pharmacology [edit]

The drug phencyclidine (more commonly known as PCP or 'Angel Grit') antagonizes glutamic acid not-competitively at the NMDA receptor. For the same reasons, dextromethorphan and ketamine as well have strong dissociative and hallucinogenic furnishings. Acute infusion of the drug LY354740 (also known equally 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 per centum) in comparison to untreated command subjects.^[29] LY354740 has also been demonstrated to human activity on the metabotropic glutamate receptor 3 (GRM3) of human adrenocortical cells, downregulating aldosterone synthase, CYP11B1, and the production of adrenal steroids (i.eastward. aldosterone and cortisol).^[thirty] Glutamate does not easily pass the blood brain barrier, but, instead, is transported past a loftier-affinity transport system.^{[31] [32]} It can likewise be converted into glutamine.

See also [edit]

• Adenosine monophosphate
• Ajinomoto
• Disodium glutamate
• Disodium inosinate
• Glutamate flavoring
• Guanosine monophosphate
• Inosinic acid
• Kainic acid
• Monopotassium glutamate
• Tien Chu Ve-Tsin

References [edit]

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2. ^ Belitz, H.-D.; Grosch, Werner; Schieberle, Peter (2009-02-27). Food Chemistry. ISBN978-3540699330.
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7. ^ ^{a b} Albert Neuberger (1936), "Dissociation constants and structures of glutamic acid and its esters". Biochemical Journal, volume xxx, issue 11, article CCXCIII, pp. 2085–2094. PMC 1263308.
8. ^ Rodante, F.; Marrosu, One thousand. (1989). "Thermodynamics of the 2d proton dissociation processes of 9 α-amino-acids and the 3rd ionization processes of glutamic acid, aspartic acid and tyrosine". Thermochimica Acta. 141: 297–303. doi:x.1016/0040-6031(89)87065-0.
9. ^ Lehmann, Mogens S.; Koetzle, Thomas F.; Hamilton, Walter C. (1972). "Precision neutron diffraction construction determination of poly peptide and nucleic acid components. 8: the crystal and molecular structure of the β-form of the amino acidl-glutamic acid". Journal of Crystal and Molecular Construction. 2 (five): 225–233. doi:10.1007/BF01246639. S2CID 93590487.
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14. ^ Renton, Alex (2005-07-ten). "If MSG is so bad for y'all, why doesn't everyone in Asia have a headache?". The Guardian . Retrieved 2008-eleven-21 .
15. ^ "Kikunae Ikeda Sodium Glutamate". Japan Patent Office. 2002-10-07. Archived from the original on 2007-x-28. Retrieved 2008-xi-21 .
16. ^ ^{a b} Grabowska, A.; Nowicki, M.; Kwinta, J. (2011). "Glutamate dehydrogenase of the germinating triticale seeds: Factor expression, activity distribution and kinetic characteristics". Acta Physiologiae Plantarum. 33 (5): 1981–1990. doi:10.1007/s11738-011-0801-one.
17. ^ Alvise Perosa; Fulvio Zecchini (2007). Methods and Reagents for Green Chemistry: An Introduction. John Wiley & Sons. p. 25. ISBN978-0-470-12407-9.
18. ^ Michael C. Flickinger (2010). Encyclopedia of Industrial Biotechnology: Bioprocess, Bioseparation, and Jail cell Technology, 7 Volume Set. Wiley. pp. 215–225. ISBN978-0-471-79930-vi.
19. ^ Foley, Patrick; Kermanshahi pour, Azadeh; Embankment, Evan Southward.; Zimmerman, Julie B. (2012). "Derivation and synthesis of renewable surfactants". Chem. Soc. Rev. 41 (4): 1499–1518. doi:10.1039/C1CS15217C. ISSN 0306-0012. PMID 22006024.
20. ^ van Lith, SA; Navis, AC; Verrijp, K; Niclou, SP; Bjerkvig, R; Wesseling, P; Tops, B; Molenaar, R; van Noorden, CJ; Leenders, WP (August 2022). "Glutamate as chemotactic fuel for diffuse glioma cells: are they glutamate suckers?". Biochimica et Biophysica Acta (BBA) - Reviews on Cancer. 1846 (1): 66–74. doi:x.1016/j.bbcan.2014.04.004. PMID 24747768.
21. ^ van Lith, SA; Molenaar, R; van Noorden, CJ; Leenders, WP (December 2022). "Tumor cells in search for glutamate: an alternative explanation for increased invasiveness of IDH1 mutant gliomas". Neuro-Oncology. 16 (12): 1669–1670. doi:x.1093/neuonc/nou152. PMC4232089. PMID 25074540.
22. ^ ^{a b} Meldrum, B. S. (2000). "Glutamate equally a neurotransmitter in the brain: Review of physiology and pathology". The Journal of Diet. 130 (4S Suppl): 1007S–1015S. doi:x.1093/jn/130.4.1007s. PMID 10736372.
23. ^ McEntee, W. J.; Cheat, T. H. (1993). "Glutamate: Its role in learning, memory, and the aging brain". Psychopharmacology. 111 (4): 391–401. doi:x.1007/BF02253527. PMID 7870979. S2CID 37400348.
24. ^ Okubo, Y.; Sekiya, H.; Namiki, S.; Sakamoto, H.; Iinuma, S.; Yamasaki, K.; Watanabe, M.; Hirose, Yard.; Iino, M. (2010). "Imaging extrasynaptic glutamate dynamics in the brain". Proceedings of the National Academy of Sciences. 107 (xiv): 6526–6531. Bibcode:2010PNAS..107.6526O. doi:x.1073/pnas.0913154107. PMC2851965. PMID 20308566.
25. ^ ^{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. PMC2193629. PMID 17202478.
26. ^ Zheng 11; Bakery DA; Shen H; Carson DS; Kalivas PW (2002). "Group 2 metabotropic glutamate receptors modulate extracellular glutamate in the nucleus accumbens". Journal of Pharmacology and Experimental Therapeutics. 300 (ane): 162–171. doi:10.1124/jpet.300.1.162. PMID 11752112.
27. ^ Reeds, P.J.; et al. (ane April 2000). "Abdominal glutamate metabolism". Journal of Nutrition. 130 (4s): 978S–982S. doi:10.1093/jn/130.4.978S. PMID 10736365.
28. ^ C. One thousand. Thiele, Concepts Magn. Reson. A, 2007, 30A, 65–80
29. ^ 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 office". CNS Spectr. 6 (7): 607–612, 617. doi:10.1017/S1092852900002157. PMID 15573025. S2CID 6029856.
30. ^ Felizola SJ, Nakamura Y, Satoh F, Morimoto R, Kikuchi K, Nakamura T, Hozawa A, Wang Fifty, Onodera Y, Ise K, McNamara KM, Midorikawa S, Suzuki S, Sasano H (January 2022). "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. S2CID 3357749.
31. ^ Smith, Quentin R. (Apr 2000). "Transport of glutamate and other amino acids at the blood–brain barrier". The Journal of Diet. 130 (4S Suppl): 1016S–1022S. doi:10.1093/jn/130.four.1016S. PMID 10736373.
32. ^ Hawkins, Richard A. (September 2009). "The claret-brain bulwark and glutamate". The American Periodical of Clinical Nutrition. 90 (iii): 867S–874S. doi:10.3945/ajcn.2009.27462BB. PMC3136011. PMID 19571220. This organisation does not allow net glutamate entry to the brain; rather, it promotes the removal of glutamate and the maintenance of low glutamate concentrations in the ECF.

Further reading [edit]

• Nelson, David L.; Cox, Michael Thousand. (2005). Principles of Biochemistry (4th ed.). New York: Due west. H. Freeman. ISBN0-7167-4339-six.

External links [edit]

• Glutamic acrid MS Spectrum

Source: https://en.wikipedia.org/wiki/Glutamic_acid

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