Aspartic acid: Difference between revisions

Aspartic acid
	; Skeletal formula of L-aspartic acid
Ball-and-stick model	Space-filling model
Names
	IUPAC name Trivial: Aspartic acid; Systematic: 2-Aminobutanedioic acid;
	Other names Aminosuccinic acid; Asparagic acid; Asparaginic acid;
Identifiers
CAS Number	L: 56-84-8 ; D/L: 617-45-8 ; D: 1783-96-6 ;
3D model (JSmol)	L: Interactive image; D: Interactive image; L Zwitterion: Interactive image; L Deprotonated zwitterion (aspartate): Interactive image;
ChEBI	L: CHEBI:17053 ; D/L: CHEBI:22660 ; D: CHEBI:17364 ;
ChEMBL	L: ChEMBL274323 ;
ChemSpider	L: 5745 ; D/L: 411 ; D: 75697 ;
DrugBank	L: DB00128 ;
ECHA InfoCard	100.000.265
EC Number	L: 200-291-6;
KEGG	D/L: C16433 ;
PubChem CID	L: 5960; D/L: 424; D: 83887;
UNII	L: 30KYC7MIAI ; D/L: 28XF4669EP ; D: 4SR0Q8YD1X ;
CompTox Dashboard (EPA)	L: DTXSID7022621 ;
	InChI InChI=1S/C4H7NO4/c5-2(4(8)9)1-3(6)7/h2H,1,5H2,(H,6,7)(H,8,9)/t2-/m0/s1 Key: CKLJMWTZIZZHCS-REOHCLBHSA-N ; D/L: Key: CKLJMWTZIZZHCS-UHFFFAOYSA-N; D: Key: CKLJMWTZIZZHCS-UWTATZPHSA-N;
	SMILES L: C([C@@H](C(=O)O)N)C(=O)O; D/L: C(C(C(=O)O)N)C(=O)O; D: C([C@H](C(=O)O)N)C(=O)O; L Zwitterion: C(C(C(=O)[O-])[NH3+])C(=O)O; L Deprotonated zwitterion (aspartate): C(C(C(=O)[O-])[NH3+])C(=O)[O-];
Properties
Chemical formula	C4H7NO4
Molar mass	133.103 g·mol−1
Appearance	colourless crystals
Density	1.7 g/cm3
Melting point	270 °C (518 °F; 543 K)
Boiling point	324 °C (615 °F; 597 K) (decomposes)
Solubility in water	4.5 g/L
Acidity (pKa)	1.99 (α-carboxyl; H2O); 3.90 (side chain; H2O); 9.90 (amino; H2O);
Conjugate base	Aspartate
Magnetic susceptibility (χ)	-64.2·10−6 cm3/mol
Hazards
NFPA 704 (fire diamond)	1 1 0
Supplementary data page
	Aspartic acid (data page)
	Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). Infobox references

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Aspartic acid (symbol Asp or D;^[4] the ionic form is known as aspartate), is an α-amino acid that is used in the biosynthesis of proteins.^[5] The L-isomer of aspartic acid is one of the 22 proteinogenic amino acids, i.e., the building blocks of proteins. D-aspartic acid is one of two D-amino acids commonly found in mammals.^[6]^[7] Apart from a few rare exceptions, D-aspartic acid is not used for protein synthesis but is incorporated into some peptides and plays a role as a neurotransmitter/neuromodulator.^[6]

Like all other amino acids, aspartic acid contains an amino group and a carboxylic acid. Its α-amino group is in the protonated –NH⁺
₃ form under physiological conditions, while its α-carboxylic acid group is deprotonated −COO⁻ under physiological conditions. Aspartic acid has an acidic side chain (CH₂COOH) which reacts with other amino acids, enzymes and proteins in the body.^[5] Under physiological conditions (pH 7.4) in proteins the side chain usually occurs as the negatively charged aspartate form, −COO⁻.^[5] It is a non-essential amino acid in humans, meaning the body can synthesize it as needed. It is encoded by the codons GAU and GAC.

In proteins aspartate sidechains are often hydrogen bonded to form asx turns or asx motifs, which frequently occur at the N-termini of alpha helices.

Aspartic acid, like glutamic acid, is classified as an acidic amino acid, with a pK_a of 3.9; however, in a peptide this is highly dependent on the local environment, and could be as high as 14.

The one-letter code D for aspartate was assigned arbitrarily,^[8] with the proposed mnemonic asparDic acid.^[9]

Discovery

Aspartic acid was first discovered in 1827 by Auguste-Arthur Plisson and Étienne Ossian Henry^[10]^[11] by hydrolysis of asparagine, which had been isolated from asparagus juice in 1806.^[12] Their original method used lead hydroxide, but various other acids or bases are now more commonly used instead.^{[citation needed]}

Forms and nomenclature

There are two forms or enantiomers of aspartic acid. The name "aspartic acid" can refer to either enantiomer or a mixture of two.^[13] Of these two forms, only one, "L-aspartic acid", is directly incorporated into proteins. The biological roles of its counterpart, "D-aspartic acid" are more limited. Where enzymatic synthesis will produce one or the other, most chemical syntheses will produce both forms, "DL-aspartic acid", known as a racemic mixture.^{[citation needed]}

Synthesis

Biosynthesis

In the human body, aspartate is most frequently synthesized through the transamination of oxaloacetate. The biosynthesis of aspartate is facilitated by an aminotransferase enzyme: the transfer of an amine group from another molecule such as alanine or glutamine yields aspartate and an alpha-keto acid.^[5]

Chemical synthesis

Industrially, aspartate is produced by amination of fumarate catalyzed by L-aspartate ammonia-lyase.^[14]

Racemic aspartic acid can be synthesized from diethyl sodium phthalimidomalonate, (C₆H₄(CO)₂NC(CO₂Et)₂).^[15]

Metabolism

In plants and microorganisms, aspartate is the precursor to several amino acids, including four that are essential for humans: methionine, threonine, isoleucine, and lysine. The conversion of aspartate to these other amino acids begins with reduction of aspartate to its "semialdehyde", O₂CCH(NH₂)CH₂CHO.^[16] Asparagine is derived from aspartate via transamidation:

⁻O₂CCH(NH₂)CH₂CO₂⁻ + GC(O)NH₃⁺ → O₂CCH(NH₂)CH₂CONH₃⁺ + GC(O)O

(where GC(O)NH₂ and GC(O)OH are glutamine and glutamic acid, respectively)

Other biochemical roles

Aspartate has many other biochemical roles. It is a metabolite in the urea cycle^[17] and participates in gluconeogenesis. It carries reducing equivalents in the malate-aspartate shuttle, which utilizes the ready interconversion of aspartate and oxaloacetate, which is the oxidized (dehydrogenated) derivative of malic acid. Aspartate donates one nitrogen atom in the biosynthesis of inosine, the precursor to the purine bases. In addition, aspartic acid acts as a hydrogen acceptor in a chain of ATP synthase. Dietary L-aspartic acid has been shown to act as an inhibitor of Beta-glucuronidase, which serves to regulate enterohepatic circulation of bilirubin and bile acids.^[18]

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles.^{[§ 1]}

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|alt=Glycolysis and Gluconeogenesis edit]]

Glycolysis and Gluconeogenesis edit

^ The interactive pathway map can be edited at WikiPathways: "GlycolysisGluconeogenesis_WP534".

Neurotransmitter

Aspartate (the conjugate base of aspartic acid) stimulates NMDA receptors, though not as strongly as the amino acid neurotransmitter L-glutamate does.^[19]

Applications & market

In 2014, the global market for aspartic acid was 39.3 thousand short tons (35.7 thousand tonnes)^[20] or about $117 million annually.^[21] The three largest market segments include the U.S., Western Europe, and China. Current applications include biodegradable polymers (polyaspartic acid), low calorie sweeteners (aspartame), scale and corrosion inhibitors, and resins.^{[citation needed]}

Superabsorbent polymers

One area of aspartic acid market growth is biodegradable superabsorbent polymers (SAP), and hydrogels.^[22] Around 75% of superabsorbent polymers are used in disposable diapers and an additional 20% is used for adult incontinence and feminine hygiene products. Polyaspartic acid, the polymerization product of aspartic acid, is a biodegradable substitute to polyacrylate.^[22]^[23]^[24]

Additional uses

In addition to SAP, aspartic acid has applications in the fertilizer industry, where polyaspartate improves water retention and nitrogen uptake.^[25]

Sources

Dietary sources

Aspartic acid is not an essential amino acid, which means that it can be synthesized from central metabolic pathway intermediates in humans, and does not need to be present in the diet. In eukaryotic cells, roughly 1 in 20 amino acids incorporated into a protein is an aspartic acid,^[26] and accordingly almost any source of dietary protein will include aspartic acid. Additionally, aspartic acid is found in:

Dietary supplements, either as aspartic acid itself or salts (such as magnesium aspartate)
The sweetener aspartame, which is made from an aspartic acid and phenylalanine

References

^ Budavari, Susan; Co, Merck (1989). "862. Aspartic acid". The Merck Index (11th ed.). Merck. p. 132. ISBN 978-0-911910-28-5.
^ "ICSC 1439 - L-ASPARTIC ACID". inchem.org.
^ Haynes, William M., ed. (2016). CRC Handbook of Chemistry and Physics (97th ed.). CRC Press. pp. 5–89. ISBN 978-1498754286.
^ "Nomenclature and Symbolism for Amino Acids and Peptides". IUPAC-IUB Joint Commission on Biochemical Nomenclature. 1983. Archived from the original on 9 October 2008. Retrieved 5 March 2018.
^ ^a ^b ^c ^d Voet, Donald; Voet, Judith G.; Pratt, Charlotte W. (2016-02-29). Fundamentals of Biochemistry: Life at the Molecular Level. John Wiley & Sons. ISBN 9781118918401. OCLC 910538334.
^ ^a ^b D'Aniello, Antimo (1 February 2007). "d-Aspartic acid: An endogenous amino acid with an important neuroendocrine role". Brain Research Reviews. 53 (2): 215–234. doi:10.1016/j.brainresrev.2006.08.005. PMID 17118457. S2CID 12709991.
^ Huang AS, Beigneux A, Weil ZM, Kim PM, Molliver ME, Blackshaw S, Nelson RJ, Young SG, Snyder SH (March 2006). "D-aspartate regulates melanocortin formation and function: behavioral alterations in D-aspartate oxidase-deficient mice". The Journal of Neuroscience. 26 (10): 2814–9. doi:10.1523/JNEUROSCI.5060-05.2006. PMC 6675153. PMID 16525061.
^ "IUPAC-IUB Commission on Biochemical Nomenclature A One-Letter Notation for Amino Acid Sequences". Journal of Biological Chemistry. 243 (13): 3557–3559. 10 July 1968. doi:10.1016/S0021-9258(19)34176-6.
^ Adoga, Godwin I; Nicholson, Bh (January 1988). "Letters to the editor". Biochemical Education. 16 (1): 49. doi:10.1016/0307-4412(88)90026-X.
^ Plisson, A. (October 1827). "Sur l'identité du malate acide d'althéine avec l'asparagine (1); et sur un acide nouveau" [On the identity of altheine acid malate with asparagine (1); and on a new acid]. Journal de Pharmacie (in French). 13 (10): 477–492.
^ Berzelius JJ, Öngren OG (1839). Traité de chimie (in French). Vol. 3. Brussels: A. Wahlen et Cie. p. 81. Retrieved 25 August 2015.
^ Plimmer R (1912) [1908]. Plimmer R, Hopkins F (eds.). The chemical composition of the proteins. Monographs on Biochemistry. Vol. Part I. Analysis (2nd ed.). London: Longmans, Green and Co. p. 112. Retrieved January 18, 2010.
^ "Nomenclature and symbolism for amino acids and peptides (IUPAC-IUB Recommendations 1983)", Pure Appl. Chem., 56 (5): 595–624, 1984, doi:10.1351/pac198456050595.
^ Drauz, Karlheinz; Grayson, Ian; Kleemann, Axel; Krimmer, Hans-Peter; Leuchtenberger, Wolfgang; Weckbecker, Christoph (2006). Ullmann's Encyclopedia of Industrial Chemistry. Weinheim: Wiley-VCH. doi:10.1002/14356007.a02_057.pub2. ISBN 978-3527306732.
^ Dunn MS, Smart BW (1950). "DL-Aspartic Acid". Organic Syntheses. 30: 7; Collected Volumes, vol. 4, p. 55..
^ Lehninger AL, Nelson DL, Cox MM (2000). Principles of Biochemistry (3rd ed.). New York: W. H. Freeman. ISBN 1-57259-153-6.
^ "Biochemistry - Biochemistry". www.varsitytutors.com. Retrieved 2022-02-18.
^ Kreamer, Bill L.; Siegel, Frank L.; Gourley, Glenn R. (Oct 2001). "A novel inhibitor of beta-glucuronidase: L-aspartic acid". Pediatric Research. 50 (4): 460–466. doi:10.1203/00006450-200110000-00007. PMID 11568288.
^ Chen PE, Geballe MT, Stansfeld PJ, Johnston AR, Yuan H, Jacob AL, Snyder JP, Traynelis SF, Wyllie DJ (May 2005). "Structural features of the glutamate binding site in recombinant NR1/NR2A N-methyl-D-aspartate receptors determined by site-directed mutagenesis and molecular modeling". Molecular Pharmacology. 67 (5): 1470–84. doi:10.1124/mol.104.008185. PMID 15703381. S2CID 13505187.
^ "Global Aspartic Acid Market By Application". Grand View Research. Retrieved November 30, 2019.
^ Evans J (2014). Commercial Amino Acids. BCC Research. pp. 101–103.
^ ^a ^b Adelnia, Hossein; Blakey, Idriss; Little, Peter J.; Ta, Hang T. (2019). "Hydrogels Based on Poly(aspartic acid): Synthesis and Applications". Frontiers in Chemistry. 7: 755. Bibcode:2019FrCh....7..755A. doi:10.3389/fchem.2019.00755. ISSN 2296-2646. PMC 6861526. PMID 31799235.
^ Adelnia, Hossein; Tran, Huong D.N.; Little, Peter J.; Blakey, Idriss; Ta, Hang T. (2021-06-14). "Poly(aspartic acid) in Biomedical Applications: From Polymerization, Modification, Properties, Degradation, and Biocompatibility to Applications". ACS Biomaterials Science & Engineering. 7 (6): 2083–2105. doi:10.1021/acsbiomaterials.1c00150. hdl:10072/404497. PMID 33797239. S2CID 232761877.
^ Alford DD, Wheeler AP, Pettigrew CA (1994). "Biodegradation of thermally synthesized polyaspartate". J Environ Polym Degr. 2 (4): 225–236. Bibcode:1994JEPD....2..225A. doi:10.1007/BF02071970.
^ Kelling K (2001). Crop Responses to Amisorb in the North Central Region. University of Wisconsin-Madison.
^ Kozlowski LP (January 2017). "Proteome-pI: proteome isoelectric point database". Nucleic Acids Research. 45 (D1): D1112–D1116. doi:10.1093/nar/gkw978. PMC 5210655. PMID 27789699.

External links

GMD MS Spectrum
American Chemical Society (21 April 2010). "Ancestral Eve' Crystal May Explain Origin of Life's Left-Handedness". ScienceDaily. Archived from the original on 23 April 2010. Retrieved 2010-04-21.

[WikiPathways-19] The interactive pathway map can be edited at WikiPathways: "GlycolysisGluconeogenesis_WP534".

[merck-1] Budavari, Susan; Co, Merck (1989). "862. Aspartic acid". The Merck Index (11th ed.). Merck. p. 132. ISBN 978-0-911910-28-5.

[2] "ICSC 1439 - L-ASPARTIC ACID". inchem.org.

[CRC97-3] Haynes, William M., ed. (2016). CRC Handbook of Chemistry and Physics (97th ed.). CRC Press. pp. 5–89. ISBN 978-1498754286.

[4] "Nomenclature and Symbolism for Amino Acids and Peptides". IUPAC-IUB Joint Commission on Biochemical Nomenclature. 1983. Archived from the original on 9 October 2008. Retrieved 5 March 2018.

[:1-5] Voet, Donald; Voet, Judith G.; Pratt, Charlotte W. (2016-02-29). Fundamentals of Biochemistry: Life at the Molecular Level. John Wiley & Sons. ISBN 9781118918401. OCLC 910538334.

[d-aspartic-6] D'Aniello, Antimo (1 February 2007). "d-Aspartic acid: An endogenous amino acid with an important neuroendocrine role". Brain Research Reviews. 53 (2): 215–234. doi:10.1016/j.brainresrev.2006.08.005. PMID 17118457. S2CID 12709991.

[7] Huang AS, Beigneux A, Weil ZM, Kim PM, Molliver ME, Blackshaw S, Nelson RJ, Young SG, Snyder SH (March 2006). "D-aspartate regulates melanocortin formation and function: behavioral alterations in D-aspartate oxidase-deficient mice". The Journal of Neuroscience. 26 (10): 2814–9. doi:10.1523/JNEUROSCI.5060-05.2006. PMC 6675153. PMID 16525061.

[:02-8] "IUPAC-IUB Commission on Biochemical Nomenclature A One-Letter Notation for Amino Acid Sequences". Journal of Biological Chemistry. 243 (13): 3557–3559. 10 July 1968. doi:10.1016/S0021-9258(19)34176-6.

[:22-9] Adoga, Godwin I; Nicholson, Bh (January 1988). "Letters to the editor". Biochemical Education. 16 (1): 49. doi:10.1016/0307-4412(88)90026-X.

[10] Plisson, A. (October 1827). "Sur l'identité du malate acide d'althéine avec l'asparagine (1); et sur un acide nouveau" [On the identity of altheine acid malate with asparagine (1); and on a new acid]. Journal de Pharmacie (in French). 13 (10): 477–492.

[11] Berzelius JJ, Öngren OG (1839). Traité de chimie (in French). Vol. 3. Brussels: A. Wahlen et Cie. p. 81. Retrieved 25 August 2015.

[12] Plimmer R (1912) [1908]. Plimmer R, Hopkins F (eds.). The chemical composition of the proteins. Monographs on Biochemistry. Vol. Part I. Analysis (2nd ed.). London: Longmans, Green and Co. p. 112. Retrieved January 18, 2010.

[IUPAC-13] "Nomenclature and symbolism for amino acids and peptides (IUPAC-IUB Recommendations 1983)", Pure Appl. Chem., 56 (5): 595–624, 1984, doi:10.1351/pac198456050595.

[14] Drauz, Karlheinz; Grayson, Ian; Kleemann, Axel; Krimmer, Hans-Peter; Leuchtenberger, Wolfgang; Weckbecker, Christoph (2006). Ullmann's Encyclopedia of Industrial Chemistry. Weinheim: Wiley-VCH. doi:10.1002/14356007.a02_057.pub2. ISBN 978-3527306732.

[15] Dunn MS, Smart BW (1950). "DL-Aspartic Acid". Organic Syntheses. 30: 7; Collected Volumes, vol. 4, p. 55..

[16] Lehninger AL, Nelson DL, Cox MM (2000). Principles of Biochemistry (3rd ed.). New York: W. H. Freeman. ISBN 1-57259-153-6.

[17] "Biochemistry - Biochemistry". www.varsitytutors.com. Retrieved 2022-02-18.

[18] Kreamer, Bill L.; Siegel, Frank L.; Gourley, Glenn R. (Oct 2001). "A novel inhibitor of beta-glucuronidase: L-aspartic acid". Pediatric Research. 50 (4): 460–466. doi:10.1203/00006450-200110000-00007. PMID 11568288.

[20] Chen PE, Geballe MT, Stansfeld PJ, Johnston AR, Yuan H, Jacob AL, Snyder JP, Traynelis SF, Wyllie DJ (May 2005). "Structural features of the glutamate binding site in recombinant NR1/NR2A N-methyl-D-aspartate receptors determined by site-directed mutagenesis and molecular modeling". Molecular Pharmacology. 67 (5): 1470–84. doi:10.1124/mol.104.008185. PMID 15703381. S2CID 13505187.

[21] "Global Aspartic Acid Market By Application". Grand View Research. Retrieved November 30, 2019.

[22] Evans J (2014). Commercial Amino Acids. BCC Research. pp. 101–103.

[:2-23] Adelnia, Hossein; Blakey, Idriss; Little, Peter J.; Ta, Hang T. (2019). "Hydrogels Based on Poly(aspartic acid): Synthesis and Applications". Frontiers in Chemistry. 7: 755. Bibcode:2019FrCh....7..755A. doi:10.3389/fchem.2019.00755. ISSN 2296-2646. PMC 6861526. PMID 31799235.

[24] Adelnia, Hossein; Tran, Huong D.N.; Little, Peter J.; Blakey, Idriss; Ta, Hang T. (2021-06-14). "Poly(aspartic acid) in Biomedical Applications: From Polymerization, Modification, Properties, Degradation, and Biocompatibility to Applications". ACS Biomaterials Science & Engineering. 7 (6): 2083–2105. doi:10.1021/acsbiomaterials.1c00150. hdl:10072/404497. PMID 33797239. S2CID 232761877.

[25] Alford DD, Wheeler AP, Pettigrew CA (1994). "Biodegradation of thermally synthesized polyaspartate". J Environ Polym Degr. 2 (4): 225–236. Bibcode:1994JEPD....2..225A. doi:10.1007/BF02071970.

[26] Kelling K (2001). Crop Responses to Amisorb in the North Central Region. University of Wisconsin-Madison.

[27] Kozlowski LP (January 2017). "Proteome-pI: proteome isoelectric point database". Nucleic Acids Research. 45 (D1): D1112–D1116. doi:10.1093/nar/gkw978. PMC 5210655. PMID 27789699.

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@@ Line 1: / Line 1: @@
-{{short description|Amino acid}}
+{{short description|Amino acid}}{{For the|the artificial sweetener|aspartame}}{{chembox
-{{chembox
 | Name = Aspartic acid
 | ImageFile1 = L-Asparaginsäure - L-Aspartic acid.svg
@@ Line 18: / Line 17: @@
  | Aminosuccinic acid
  | Asparagic acid
- | Asparaginic acid<ref name=merck>{{cite book |title= The Merck Index |chapter= 862. Aspartic acid |edition= 11th |page= [https://archive.org/details/merckindexency00buda/page/132 132] |year= 1989 |isbn= 978-0-911910-28-5 |last1= Budavari |first1= Susan |last2= Co |first2= Merck |chapter-url-access= registration |chapter-url= https://archive.org/details/merckindexency00buda |url= https://archive.org/details/merckindexency00buda/page/132 }}</ref>
+ | Asparaginic acid<ref name=merck>{{cite book |title= The Merck Index |chapter= 862. Aspartic acid |edition= 11th |page= [https://archive.org/details/merckindexency00buda/page/132 132] |year= 1989 |isbn= 978-0-911910-28-5 |last1= Budavari |first1= Susan |last2= Co |first2= Merck |publisher= Merck |chapter-url-access= registration |chapter-url= https://archive.org/details/merckindexency00buda |url= https://archive.org/details/merckindexency00buda/page/132 }}</ref>
 }}
 |Section1={{Chembox Identifiers
@@ Line 98: / Line 97: @@
  }}
 }}
-'''Aspartic acid''' (symbol '''Asp''' or '''D''';<ref>{{cite web | url = http://www.chem.qmul.ac.uk/iupac/AminoAcid/AA1n2.html | title = Nomenclature and Symbolism for Amino Acids and Peptides | publisher = IUPAC-IUB Joint Commission on Biochemical Nomenclature | year = 1983 | access-date = 5 March 2018 | archive-url = https://web.archive.org/web/20081009023202/http://www.chem.qmul.ac.uk/iupac/AminoAcid/AA1n2.html | archive-date = 9 October 2008 |url-status = dead}}</ref> the ionic form is known as '''aspartate'''), is an α-[[amino acid]] that is used in the biosynthesis of proteins.<ref name=":1">{{Cite book|title=Fundamentals of biochemistry : life at the molecular level|last1=G.|first1=Voet, Judith|last2=W.|first2=Pratt, Charlotte|isbn=9781118918401|oclc=910538334|date=2016-02-29}}</ref> Like all other amino acids, it contains an amino group and a carboxylic acid. Its α-amino group is in the protonated –NH{{su|b=3|p=+}} form under physiological conditions, while its α-carboxylic acid group is deprotonated −COO<sup>−</sup> under physiological conditions. Aspartic acid has an acidic side chain (CH<sub>2</sub>COOH) which reacts with other amino acids, enzymes and proteins in the body.<ref name=":1" /> Under physiological conditions (pH 7.4) in proteins the side chain usually occurs as the negatively charged aspartate form, −COO<sup>−</sup>.<ref name=":1" /> It is a non-[[essential amino acid]] in humans, meaning the body can [[De novo synthesis|synthesize it]] as needed. It is [[Genetic code|encoded]] by the [[codon]]s GAU and GAC.
+'''Aspartic acid''' (symbol '''Asp''' or '''D''';<ref>{{cite web | url = http://www.chem.qmul.ac.uk/iupac/AminoAcid/AA1n2.html | title = Nomenclature and Symbolism for Amino Acids and Peptides | publisher = IUPAC-IUB Joint Commission on Biochemical Nomenclature | year = 1983 | access-date = 5 March 2018 | archive-url = https://web.archive.org/web/20081009023202/http://www.chem.qmul.ac.uk/iupac/AminoAcid/AA1n2.html | archive-date = 9 October 2008 |url-status = dead}}</ref> the ionic form is known as '''aspartate'''), is an α-[[amino acid]] that is used in the biosynthesis of proteins.<ref name=":1">{{Cite book|title=Fundamentals of Biochemistry: Life at the Molecular Level|last1=Voet|first1=Donald|first2= Judith G.|last2=Voet|last3=Pratt|first3= Charlotte W.|isbn=9781118918401|oclc=910538334|date=2016-02-29|publisher=John Wiley & Sons }}</ref> The <small>L</small>-isomer of aspartic acid is one of the 22 [[proteinogenic amino acid]]s, i.e., the building blocks of [[protein]]s.
+'''<small>D</small>-aspartic acid''' is one of two <small>D</small>-amino acids commonly found in mammals.<ref name="d-aspartic">{{cite journal |last1=D'Aniello |first1=Antimo |title=d-Aspartic acid: An endogenous amino acid with an important neuroendocrine role |journal=Brain Research Reviews |date=1 February 2007 |volume=53 |issue=2 |pages=215–234 |doi=10.1016/j.brainresrev.2006.08.005|pmid=17118457 |s2cid=12709991 }}</ref><ref>{{cite journal | vauthors = Huang AS, Beigneux A, Weil ZM, Kim PM, Molliver ME, Blackshaw S, Nelson RJ, Young SG, Snyder SH | title = D-aspartate regulates melanocortin formation and function: behavioral alterations in D-aspartate oxidase-deficient mice | journal = The Journal of Neuroscience | volume = 26 | issue = 10 | pages = 2814–9 | date = March 2006 | pmid = 16525061 | doi = 10.1523/JNEUROSCI.5060-05.2006| pmc = 6675153 }}</ref> Apart from a few rare exceptions, <small>D</small>-aspartic acid is not used for protein synthesis but is incorporated into some [[peptides]] and plays a role as a [[neurotransmitter]]/[[neuromodulator]].<ref name="d-aspartic"/>
+Like all other amino acids, aspartic acid contains an amino group and a carboxylic acid. Its α-amino group is in the protonated –NH{{su|b=3|p=+}} form under physiological conditions, while its α-carboxylic acid group is deprotonated −COO<sup>−</sup> under physiological conditions. Aspartic acid has an acidic side chain (CH<sub>2</sub>COOH) which reacts with other amino acids, enzymes and proteins in the body.<ref name=":1" /> Under physiological conditions (pH 7.4) in proteins the side chain usually occurs as the negatively charged aspartate form, −COO<sup>−</sup>.<ref name=":1" /> It is a non-[[essential amino acid]] in humans, meaning the body can [[De novo synthesis|synthesize it]] as needed. It is [[Genetic code|encoded]] by the [[codon]]s GAU and GAC.
-<small>D</small>-Aspartate is one of two <small>D</small>-amino acids commonly found in mammals.[[Aspartic acid#cite note-3|<sup>[3]</sup>]]
 In proteins aspartate sidechains are often hydrogen bonded to form [[asx turn]]s or [[asx motif]]s, which frequently occur at the N-termini of [[alpha helices]].
-The <small>L</small>-isomer of Asp is one of the 22 [[proteinogenic amino acid]]s, i.e., the building blocks of [[protein]]s. Aspartic acid, like [[glutamic acid]], is classified as an acidic amino acid, with a [[PKa|pK<sub>a</sub>]] of 3.9; however, in a peptide this is highly dependent on the local environment, and could be as high as 14. Asp is pervasive in biosynthesis.
+Aspartic acid, like [[glutamic acid]], is classified as an acidic amino acid, with a [[PKa|pK<sub>a</sub>]] of 3.9; however, in a peptide this is highly dependent on the local environment, and could be as high as 14.
+The one-letter code D for aspartate was assigned arbitrarily,<ref name=":02">{{Cite journal |date=10 July 1968 |title=IUPAC-IUB Commission on Biochemical Nomenclature A One-Letter Notation for Amino Acid Sequences |url=https://www.jbc.org/article/S0021-9258(19)34176-6/pdf |journal=Journal of Biological Chemistry |language=en |volume=243 |issue=13 |pages=3557–3559 |doi=10.1016/S0021-9258(19)34176-6|doi-access=free }}</ref> with the proposed mnemonic aspar''D''ic acid.<ref name=":22">{{Cite journal |last1=Adoga |first1=Godwin I |last2=Nicholson |first2=Bh |date=January 1988 |title=Letters to the editor |url=https://onlinelibrary.wiley.com/doi/pdf/10.1016/0307-4412%2888%2990026-X |journal=Biochemical Education |language=en |volume=16 |issue=1 |pages=49 |doi=10.1016/0307-4412(88)90026-X}}</ref>
 ==Discovery==
-Aspartic acid was first discovered in 1827 by [[Auguste-Arthur Plisson]] and [[Étienne Ossian Henry]]<ref>{{cite journal |last1=Plisson |first1=A. |title=Sur l'identité du malate acide d'althéine avec l'asparagine (1); et sur un acide nouveau |journal=Journal de Pharmacie |date=October 1827 |volume=13 |issue=10 |pages=477–492 |url=https://books.google.com/books?id=7Vf4WcM8VksC&pg=PA477 |trans-title=On the identity of altheine acid malate with asparagine (1); and on a new acid |language=French}}</ref><ref>{{cite book | title = Traité de chimie | volume = 3 | author1-first = Jöns Jakob | author1-last = Berzelius | author1-link = Jöns Jacob Berzelius | author2-first = Olof Gustaf | author2-last = Öngren | name-list-style = vanc | year = 1839 | language = fr | publisher = A. Wahlen et Cie.| location = Brussels | page = 81 | url = https://books.google.com/books?id=szLPAAAAMAAJ | access-date = 25 August 2015 }}</ref> by [[hydrolysis]] of [[asparagine]], which had been isolated from [[asparagus]] juice in 1806.<ref>{{cite book | first = R.H.A. | last = Plimmer | editor-first1 = R.H.A. | editor-last1 = Plimmer | editor-first2 = F.G. | editor-last2 = Hopkins | name-list-style = vanc | title = The chemical composition of the proteins | url = https://books.google.com/books?id=7JM8AAAAIAAJ&pg=PA112  |access-date = January 18, 2010 | edition = 2nd | series =  Monographs on Biochemistry | volume = Part I. Analysis | orig-year = 1908 | year = 1912 | publisher = Longmans, Green and Co. | location = London | page = 112 }}</ref> Their original method used [[lead hydroxide]], but various other acids or bases are now more commonly used instead.{{Cn|date=January 2021}}
+Aspartic acid was first discovered in 1827 by [[Auguste-Arthur Plisson]] and [[Étienne Ossian Henry]]<ref>{{cite journal |last1=Plisson |first1=A. |title=Sur l'identité du malate acide d'althéine avec l'asparagine (1); et sur un acide nouveau |journal=Journal de Pharmacie |date=October 1827 |volume=13 |issue=10 |pages=477–492 |url=https://books.google.com/books?id=7Vf4WcM8VksC&pg=PA477 |trans-title=On the identity of altheine acid malate with asparagine (1); and on a new acid |language=French}}</ref><ref>{{cite book | title = Traité de chimie | volume = 3 | author1-first = Jöns Jakob | author1-last = Berzelius | author1-link = Jöns Jacob Berzelius | author2-first = Olof Gustaf | author2-last = Öngren | name-list-style = vanc | year = 1839 | language = fr | publisher = A. Wahlen et Cie.| location = Brussels | page = 81 | url = https://books.google.com/books?id=szLPAAAAMAAJ | access-date = 25 August 2015 }}</ref> by [[hydrolysis]] of [[asparagine]], which had been isolated from [[asparagus]] juice in 1806.<ref>{{cite book | first = R.H.A. | last = Plimmer | editor-first1 = R.H.A. | editor-last1 = Plimmer | editor-first2 = F.G. | editor-last2 = Hopkins | name-list-style = vanc | title = The chemical composition of the proteins | url = https://books.google.com/books?id=7JM8AAAAIAAJ&pg=PA112  |access-date = January 18, 2010 | edition = 2nd | series =  Monographs on Biochemistry | volume = Part I. Analysis | orig-year = 1908 | year = 1912 | publisher = Longmans, Green and Co. | location = London | page = 112 }}</ref> Their original method used [[lead hydroxide]], but various other acids or bases are now more commonly used instead.{{Citation needed|date=January 2021}}
 ==Forms and nomenclature==
-There are two forms or [[enantiomer]]s of aspartic acid. The name "aspartic acid" can refer to either enantiomer or a mixture of two.<ref name="IUPAC">{{IUPAC-IUB amino acids 1983}}.</ref> Of these two forms, only one, "<small>L</small>-aspartic acid", is directly incorporated into proteins. The biological roles of its counterpart, "<small>D</small>-aspartic acid" are more limited. Where enzymatic synthesis will produce one or the other, most chemical syntheses will produce both forms, "<small>DL</small>-aspartic acid", known as a [[racemic mixture]].{{Cn|date=January 2021}}
+There are two forms or [[enantiomer]]s of aspartic acid. The name "aspartic acid" can refer to either enantiomer or a mixture of two.<ref name="IUPAC">{{IUPAC-IUB amino acids 1983}}.</ref> Of these two forms, only one, "<small>L</small>-aspartic acid", is directly incorporated into proteins. The biological roles of its counterpart, "<small>D</small>-aspartic acid" are more limited. Where enzymatic synthesis will produce one or the other, most chemical syntheses will produce both forms, "<small>DL</small>-aspartic acid", known as a [[racemic mixture]].{{Citation needed|date=January 2021}}
 == Synthesis ==
@@ Line 116: / Line 119: @@
 === Chemical synthesis ===
-Industrially, aspartate is produced by amination of [[fumarate]] catalyzed by L-[[aspartate ammonia-lyase]].<ref>{{Ullmann|author=Karlheinz Drauz, Ian Grayson, Axel Kleemann, Hans-Peter Krimmer, Wolfgang Leuchtenberger, Christoph Weckbecker|year=2006|doi=10.1002/14356007.a02_057.pub2}}</ref>
+Industrially, aspartate is produced by amination of [[fumarate]] catalyzed by L-[[aspartate ammonia-lyase]].<ref>{{Ullmann|first1=Karlheinz|last1= Drauz|first2= Ian|last2= Grayson|first3= Axel|last3= Kleemann|first4= Hans-Peter|last4= Krimmer|first5= Wolfgang|last5= Leuchtenberger|first6= Christoph|last6= Weckbecker|year=2006|doi=10.1002/14356007.a02_057.pub2}}</ref>
 [[Racemic]] aspartic acid can be synthesized from diethyl sodium phthalimidomalonate,
@@ Line 123: / Line 126: @@
 ==Metabolism==
 In plants and [[microorganism]]s, aspartate is the precursor to several amino acids, including four that are essential for humans: [[methionine]], [[threonine]], [[isoleucine]], and [[lysine]]. The conversion of aspartate to these other amino acids begins with reduction of aspartate to its "semialdehyde", O<sub>2</sub>CCH(NH<sub>2</sub>)CH<sub>2</sub>CHO.<ref>{{Lehninger3rd|name-list-style = vanc }}</ref>  [[Asparagine]] is derived from aspartate via transamidation:
-:<sup>-</sup>O<sub>2</sub>CCH(NH<sub>2</sub>)CH<sub>2</sub>CO<sub>2</sub><sup>-</sup>  +  ''G''C(O)NH<sub>3</sub><sup>+</sup>  → O<sub>2</sub>CCH(NH<sub>2</sub>)CH<sub>2</sub>CONH<sub>3</sub><sup>+</sup>  +  ''G''C(O)O
+:<sup>−</sup>O<sub>2</sub>CCH(NH<sub>2</sub>)CH<sub>2</sub>CO<sub>2</sub><sup>−</sup>  +  ''G''C(O)NH<sub>3</sub><sup>+</sup>  → O<sub>2</sub>CCH(NH<sub>2</sub>)CH<sub>2</sub>CONH<sub>3</sub><sup>+</sup>  +  ''G''C(O)O
 (where ''G''C(O)NH<sub>2</sub> and ''G''C(O)OH are [[glutamine]] and [[glutamic acid]], respectively)
 ==Other biochemical roles==
-Aspartate has many other biochemical roles. It is a [[metabolite]] in the [[urea cycle]]<ref>{{Cite web|title=Biochemistry - Biochemistry|url=https://www.varsitytutors.com/biochemistry-help/biochemistry?page=75|access-date=2022-02-18|website=www.varsitytutors.com|language=en}}</ref> and participates in [[gluconeogenesis]]. It carries reducing equivalents in the [[malate-aspartate shuttle]], which utilizes the ready interconversion of aspartate and [[oxaloacetate]], which is the oxidized (dehydrogenated) derivative of [[malic acid]]. Aspartate donates one nitrogen atom in the biosynthesis of [[inosine]], the precursor to the [[purine]] bases. In addition, aspartic acid acts as a hydrogen acceptor in a chain of ATP synthase. Dietary L-aspartic acid has been shown to act as an inhibitor of [[Beta-glucuronidase]], which serves to regulate [[enterohepatic circulation]] of [[bilirubin]] and bile acids.<ref>{{Cite journal|last=Kreamer, Siegel, & Gourley|date=Oct 2001|title=A novel inhibitor of beta-glucuronidase: L-aspartic acid.|journal=Pediatric Research|volume=50|issue=4|pages=460–466|pmid=11568288|doi=10.1203/00006450-200110000-00007|doi-access=free}}</ref>
+Aspartate has many other biochemical roles. It is a [[metabolite]] in the [[urea cycle]]<ref>{{Cite web|title=Biochemistry - Biochemistry|url=https://www.varsitytutors.com/biochemistry-help/biochemistry?page=75|access-date=2022-02-18|website=www.varsitytutors.com|language=en}}</ref> and participates in [[gluconeogenesis]]. It carries reducing equivalents in the [[malate-aspartate shuttle]], which utilizes the ready interconversion of aspartate and [[oxaloacetate]], which is the oxidized (dehydrogenated) derivative of [[malic acid]]. Aspartate donates one nitrogen atom in the biosynthesis of [[inosine]], the precursor to the [[purine]] bases. In addition, aspartic acid acts as a hydrogen acceptor in a chain of ATP synthase. Dietary L-aspartic acid has been shown to act as an inhibitor of [[Beta-glucuronidase]], which serves to regulate [[enterohepatic circulation]] of [[bilirubin]] and bile acids.<ref>{{Cite journal|first1=Bill L.|last1= Kreamer|first2=Frank L.|last2=Siegel |first3=Glenn R.|last3= Gourley|date=Oct 2001|title=A novel inhibitor of beta-glucuronidase: L-aspartic acid.|journal=Pediatric Research|volume=50|issue=4|pages=460–466|pmid=11568288|doi=10.1203/00006450-200110000-00007|doi-access=free}}</ref>
 ===Interactive pathway map===
@@ Line 136: / Line 139: @@
 == Applications & market ==
-In 2014, the global market for aspartic acid was {{convert|39.3|e3short ton|e3t|abbr=off|lk=on}}<ref>{{cite web |title=Global Aspartic Acid Market By Application |url=https://www.grandviewresearch.com/press-release/global-aspartic-acid-market |publisher=Grand View Research |access-date=November 30, 2019}}</ref> or about $117 million annually<ref>{{cite book | vauthors = Evans J | title = Commercial Amino Acids | pages = 101–103 | publisher = BCC Research | year = 2014 |url= http://www.bccresearch.com/market-research/biotechnology/commercial-amino-acids-bio007k.html }}</ref> with potential areas of growth accounting for an {{clarify|text=addressable market|reason=Is this [[Total addressable market]] or [[Serviceable available market]]?|date=March 2017}} of $8.78 billion (Bn).<ref name=":0">Transparency Market Research. Superabsorbent polymers market - global industry analysis, size, share, growth, trends and forecase, 2014-2020. (2014).</ref> The three largest market segments include the U.S., Western Europe, and China. Current applications include biodegradable polymers ([[polyaspartic acid]]), low calorie sweeteners ([[aspartame]]), scale and corrosion inhibitors, and resins.{{Cn|date=January 2021}}
+In 2014, the global market for aspartic acid was {{convert|39.3|e3short ton|e3t|abbr=off|lk=on}}<ref>{{cite web |title=Global Aspartic Acid Market By Application |url=https://www.grandviewresearch.com/press-release/global-aspartic-acid-market |publisher=Grand View Research |access-date=November 30, 2019}}</ref> or about $117 million annually.<ref>{{cite book | vauthors = Evans J | title = Commercial Amino Acids | pages = 101–103 | publisher = BCC Research | year = 2014 |url= http://www.bccresearch.com/market-research/biotechnology/commercial-amino-acids-bio007k.html }}</ref> The three largest market segments include the U.S., Western Europe, and China. Current applications include biodegradable polymers ([[polyaspartic acid]]), low calorie sweeteners ([[aspartame]]), scale and corrosion inhibitors, and resins.{{Citation needed|date=January 2021}}
 ===Superabsorbent polymers===
-One area of aspartic acid market growth is [[biodegradable]] [[superabsorbent polymer]]s (SAP), and hydrogels. <ref name=":2">{{Cite journal|last1=Adelnia|first1=Hossein|last2=Blakey|first2=Idriss|last3=Little|first3=Peter J.|last4=Ta|first4=Hang T.|date=2019|title=Hydrogels Based on Poly(aspartic acid): Synthesis and Applications|journal=Frontiers in Chemistry|volume=7|page=755|language=English|doi=10.3389/fchem.2019.00755|pmid=31799235|issn=2296-2646|pmc=6861526|bibcode=2019FrCh....7..755A|doi-access=free}}</ref> The superabsorbent polymers market is anticipated to grow at a [[compound annual growth rate]] of 5.5% from 2014 to 2019 to reach a value of $8.78Bn globally.<ref name=":0" /> Around 75% of superabsorbent polymers are used in disposable [[diaper]]s and an additional 20% is used for adult [[Urinary incontinence|incontinence]] and [[feminine hygiene]] products. [[Polyaspartic acid]], the polymerization product of aspartic acid, is a biodegradable substitute to [[polyacrylate]].<ref name=":2" /><ref>{{Cite journal|last1=Adelnia|first1=Hossein|last2=Tran|first2=Huong D.N.|last3=Little|first3=Peter J.|last4=Blakey|first4=Idriss|last5=Ta|first5=Hang T.|date=2021-06-14|title=Poly(aspartic acid) in Biomedical Applications: From Polymerization, Modification, Properties, Degradation, and Biocompatibility to Applications|url=https://doi.org/10.1021/acsbiomaterials.1c00150|journal=ACS Biomaterials Science & Engineering|volume=7|issue=6|pages=2083–2105|doi=10.1021/acsbiomaterials.1c00150|pmid=33797239|hdl=10072/404497 |s2cid=232761877|hdl-access=free}}</ref><ref>{{cite journal | vauthors = Alford DD, Wheeler AP, Pettigrew CA | title = Biodegradation of thermally synthesized polyaspartate | journal = J Environ Polym Degr | volume = 2 | issue = 4 | pages = 225–236 | date = 1994 | doi = 10.1007/BF02071970 }}</ref> The polyaspartate market comprises a small fraction (est. < 1%) of the total SAP market.{{Cn|date=January 2021}}
+One area of aspartic acid market growth is [[biodegradable]] [[superabsorbent polymer]]s (SAP), and hydrogels.<ref name=":2">{{Cite journal|last1=Adelnia|first1=Hossein|last2=Blakey|first2=Idriss|last3=Little|first3=Peter J.|last4=Ta|first4=Hang T.|date=2019|title=Hydrogels Based on Poly(aspartic acid): Synthesis and Applications|journal=Frontiers in Chemistry|volume=7|page=755|language=English|doi=10.3389/fchem.2019.00755|pmid=31799235|issn=2296-2646|pmc=6861526|bibcode=2019FrCh....7..755A|doi-access=free}}</ref> Around 75% of superabsorbent polymers are used in disposable [[diaper]]s and an additional 20% is used for adult [[Urinary incontinence|incontinence]] and [[feminine hygiene]] products. [[Polyaspartic acid]], the polymerization product of aspartic acid, is a biodegradable substitute to [[polyacrylate]].<ref name=":2" /><ref>{{Cite journal|last1=Adelnia|first1=Hossein|last2=Tran|first2=Huong D.N.|last3=Little|first3=Peter J.|last4=Blakey|first4=Idriss|last5=Ta|first5=Hang T.|date=2021-06-14|title=Poly(aspartic acid) in Biomedical Applications: From Polymerization, Modification, Properties, Degradation, and Biocompatibility to Applications|url=https://doi.org/10.1021/acsbiomaterials.1c00150|journal=ACS Biomaterials Science & Engineering|volume=7|issue=6|pages=2083–2105|doi=10.1021/acsbiomaterials.1c00150|pmid=33797239|hdl=10072/404497 |s2cid=232761877|hdl-access=free}}</ref><ref>{{cite journal | vauthors = Alford DD, Wheeler AP, Pettigrew CA | title = Biodegradation of thermally synthesized polyaspartate | journal = J Environ Polym Degr | volume = 2 | issue = 4 | pages = 225–236 | date = 1994 | doi = 10.1007/BF02071970 | bibcode = 1994JEPD....2..225A }}</ref>
 ===Additional uses===
+In addition to SAP, aspartic acid has applications in the [[Fertilizer|fertilizer industry]], where polyaspartate improves water retention and nitrogen uptake.<ref>{{cite book | vauthors = Kelling K | title = Crop Responses to Amisorb in the North Central Region | publisher = University of Wisconsin-Madison | date = 2001 }}</ref>
-In addition to SAP, aspartic acid has applications in the $19Bn [[Fertilizer|fertilizer industry]], where polyaspartate improves water retention and nitrogen uptake;<ref>{{cite book | vauthors = Kelling K | title = Crop Responses to Amisorb in the North Central Region | publisher = University of Wisconsin-Madison | date = 2001 }}</ref> the $1.1Bn (2020) concrete floor coatings market, where polyaspartic is a low VOC, low energy alternative to traditional epoxy resins;<ref>Global concrete floor coatings market will be worth US$1.1Bn by 2020. ''Transparency Market Research'' (2015).</ref> and lastly the >$5Bn scale and corrosion inhibitors market.<ref>Corrosion inhibitors market analysis by product, by application, by end-use industry, and segment forecasts to 2020. ''Grand View Research'' (2014)</ref>
 == Sources ==
 {{More citations needed section|date=January 2021}}
 ===Dietary sources===
 Aspartic acid is not an [[essential amino acid]], which means that it can be synthesized from central metabolic pathway intermediates in humans, and does not need to be present in the diet. In [[Eukaryote|eukaryotic]] cells, roughly 1 in 20 amino acids incorporated into a protein is an aspartic acid,<ref>{{cite journal | vauthors = Kozlowski LP | title = Proteome-pI: proteome isoelectric point database | journal = Nucleic Acids Research | volume = 45 | issue = D1 | pages = D1112–D1116 | date = January 2017 | pmid = 27789699 | pmc = 5210655 | doi = 10.1093/nar/gkw978 }}</ref> and accordingly almost any source of dietary protein will include aspartic acid. Additionally, aspartic acid is found in:
@@ Line 170: / Line 173: @@
 {{Authority control}}
-[[Category:Proteinogenic amino acids]]
+[[Category:Aspartic acids]]
 [[Category:Glucogenic amino acids]]
-[[Category:Acidic amino acids]]
-[[Category:Dicarboxylic acids]]
 [[Category:Excitatory amino acids]]
 [[Category:Urea cycle]]

v t e Ionotropic glutamate receptor modulators
AMPARTooltip α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor	Agonists: Main site agonists: 5-Fluorowillardiine Acromelic acid (acromelate) AMPA BOAA Domoic acid Glutamate Ibotenic acid Proline Quisqualic acid Willardiine; Positive allosteric modulators: Aniracetam Cyclothiazide CX-516 CX-546 CX-614 Farampator (CX-691, ORG-24448) CX-717 CX-1739 CX-1942 Diazoxide Hydrochlorothiazide (HCTZ) IDRA-21 LY-392098 LY-395153 LY-404187 LY-451646 LY-503430 Mibampator (LY-451395) Nooglutyl ORG-26576 Oxiracetam PEPA Pesampator (BIIB-104, PF-04958242) Piracetam Pramiracetam S-18986 Tulrampator (S-47445, CX-1632) Antagonists: ACEA-1011 ATPO Becampanel Caroverine CNQX Dasolampanel DNQX Fanapanel (MPQX) GAMS Kaitocephalin Kynurenic acid Kynurenine Licostinel (ACEA-1021) NBQX PNQX Selurampanel Tezampanel Theanine Topiramate YM90K Zonampanel; Negative allosteric modulators: Barbiturates (e.g., pentobarbital, sodium thiopental) Cyclopropane Enflurane Ethanol (alcohol) Evans blue GYKI-52466 GYKI-53655 Halothane Irampanel Isoflurane Perampanel Pregnenolone sulfate Sevoflurane Talampanel; Unknown/unsorted antagonists: Minocycline
KARTooltip Kainate receptor	Agonists: Main site agonists: 5-Bromowillardiine 5-Iodowillardiine Acromelic acid (acromelate) AMPA ATPA Domoic acid Glutamate Ibotenic acid Kainic acid LY-339434 Proline Quisqualic acid SYM-2081; Positive allosteric modulators: Cyclothiazide Diazoxide Enflurane Halothane Isoflurane Antagonists: ACEA-1011 CNQX Dasolampanel DNQX GAMS Kaitocephalin Kynurenic acid Licostinel (ACEA-1021) LY-382884 NBQX NS102 Selurampanel Tezampanel Theanine Topiramate UBP-302; Negative allosteric modulators: Barbiturates (e.g., pentobarbital, sodium thiopental) Enflurane Ethanol (alcohol) Evans blue NS-3763 Pregnenolone sulfate
NMDARTooltip N-Methyl-D-aspartate receptor	Agonists: Main site agonists: AMAA Aspartate Glutamate Homocysteic acid (L-HCA) Homoquinolinic acid Ibotenic acid NMDA Proline Quinolinic acid Tetrazolylglycine Theanine; Glycine site agonists: β-Fluoro-D-alanine ACBD ACC (ACPC) ACPD AK-51 Apimostinel (NRX-1074) B6B21 CCG D-Alanine D-Cycloserine D-Serine DHPG Dimethylglycine Glycine HA-966 L-687414 L-Alanine L-Serine Milacemide Neboglamine (nebostinel) Rapastinel (GLYX-13) Sarcosine; Polyamine site agonists: Neomycin Spermidine Spermine; Other positive allosteric modulators: 24S-Hydroxycholesterol DHEATooltip Dehydroepiandrosterone (prasterone) DHEA sulfate (prasterone sulfate) Epipregnanolone sulfate Plazinemdor Pregnenolone sulfate SAGE-201 SAGE-301 SAGE-718 Antagonists: Competitive antagonists: AP5 (APV) AP7 CGP-37849 CGP-39551 CGP-39653 CGP-40116 CGS-19755 CPP Kaitocephalin LY-233053 LY-235959 LY-274614 MDL-100453 Midafotel (d-CPPene) NPC-12626 NPC-17742 PBPD PEAQX Perzinfotel PPDA SDZ-220581 Selfotel; Glycine site antagonists: 4-Cl-KYN (AV-101) 5,7-DCKA 7-CKA ACC ACEA-1011 ACEA-1328 Apimostinel (NRX-1074) AV-101 Carisoprodol CGP-39653 CNQX D-Cycloserine DNQX Felbamate Gavestinel GV-196771 Harkoseride Kynurenic acid Kynurenine L-689560 L-701324 Licostinel (ACEA-1021) LU-73068 MDL-105519 Meprobamate MRZ 2/576 PNQX Rapastinel (GLYX-13) ZD-9379; Polyamine site antagonists: Arcaine Co 101676 Diaminopropane Diethylenetriamine Huperzine A Putrescine; Uncompetitive pore blockers (mostly dizocilpine site): 2-MDP 3-HO-PCP 3-MeO-PCE 3-MeO-PCMo 3-MeO-PCP 4-MeO-PCP 8A-PDHQ 18-MC α-Endopsychosin Alaproclate Alazocine (SKF-10047) Amantadine Aptiganel Argiotoxin-636 Arketamine ARL-12495 ARL-15896-AR ARL-16247 Budipine Coronaridine Delucemine (NPS-1506) Dexoxadrol Dextrallorphan Dextromethadone Dextromethorphan Dextrorphan Dieticyclidine Diphenidine Dizocilpine Ephenidine Esketamine Etoxadrol Eticyclidine Fluorolintane Gacyclidine Ibogaine Ibogamine Indantadol Ketamine Ketobemidone Lanicemine Levomethadone Levomethorphan Levomilnacipran Levorphanol Loperamide Memantine Methadone Methorphan Methoxetamine Methoxphenidine Milnacipran Morphanol NEFA Neramexane Nitromemantine Noribogaine Norketamine Orphenadrine PCPr PD-137889 Pethidine (meperidine) Phencyclamine Phencyclidine Propoxyphene Remacemide Rhynchophylline Rimantadine Rolicyclidine Sabeluzole Tabernanthine Tenocyclidine Tiletamine Tramadol; Ifenprodil (NR2B) site antagonists: Besonprodil Buphenine (nylidrin) CO-101244 (PD-174494) Eliprodil Haloperidol Isoxsuprine Radiprodil (RGH-896) Rislenemdaz (CERC-301, MK-0657) Ro 8-4304 Ro 25-6981 Safaprodil Traxoprodil (CP-101606); NR2A-selective antagonists: MPX-004 MPX-007 TCN-201 TCN-213; Cations: Hydrogen Magnesium Zinc; Alcohols/volatile anesthetics/related: Benzene Butane Chloroform Cyclopropane Desflurane Diethyl ether Enflurane Ethanol (alcohol) Halothane Hexanol Isoflurane Methoxyflurane Nitrous oxide Octanol Sevoflurane Toluene Trichloroethane Trichloroethanol Trichloroethylene Urethane Xenon Xylene; Unknown/unsorted antagonists: ARR-15896 Bumetanide Caroverine Conantokin D-αAA Dexanabinol Flufenamic acid Flupirtine FPL-12495 FR-115427 Furosemide Hodgkinsine Ipenoxazone (MLV-6976) MDL-27266 Metaphit Minocycline MPEP Niflumic acid Pentamidine Pentamidine isethionate Piretanide Psychotridine Transcrocetin (saffron) Unsorted: Allosteric modulators: AGN-241751
See also: Receptor/signaling modulators Metabotropic glutamate receptor modulators Glutamate metabolism/transport modulators