Aspartic acid

From Wikipedia, the free encyclopedia
Jump to: navigation, search
Aspartic acid
D-Aspartate (DMA)
Names
IUPAC names
Trivial: Aspartic acid
Systematic: 2-Aminobutanedioic acid
Other names
Aminosuccinic acid, asparagic acid, asparaginic acid[1]
Identifiers
617-45-8 YesY
56-84-8 (L-isomer) N
1783-96-6 (D-isomer) N
3D model (Jmol) Interactive image
Interactive image
ChEBI CHEBI:22660 YesY
ChEMBL ChEMBL139661 YesY
ChemSpider 411 YesY
ECHA InfoCard 100.000.265
EC Number 200-291-6
KEGG C16433 YesY
PubChem 424
UNII 28XF4669EP YesY
Properties
C4H7NO4
Molar mass 133.10 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)
4.5 g/L[2]
Acidity (pKa) 3.9
-64.2·10−6 cm3/mol
Hazards
Safety data sheet See: data page
NFPA 704
Flammability code 1: Must be pre-heated before ignition can occur. Flash point over 93 °C (200 °F). E.g., canola oil Health code 1: Exposure would cause irritation but only minor residual injury. E.g., turpentine Reactivity code 0: Normally stable, even under fire exposure conditions, and is not reactive with water. E.g., liquid nitrogen Special hazards (white): no codeNFPA 704 four-colored diamond
Supplementary data page
Refractive index (n),
Dielectric constantr), etc.
Thermodynamic
data
Phase behaviour
solid–liquid–gas
UV, IR, NMR, MS
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
N verify (what is YesYN ?)
Infobox references

Aspartic acid (abbreviated as Asp or D; encoded by the codons [GAU and GAC]), also known as aspartate in its deprotonated form, is an α-amino acid that is used in the biosynthesis of proteins.[3] Similar to all other amino acids it 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.[3] Under physiological conditions (pH 7.4) in proteins the side chain usually occurs as the negatively charged aspartate form, −COO .[3] It is semi-essential in humans, meaning the body can synthesize it through the transfer of an amino group, or transamination, of oxaloacetate by alanine or glutamate.[3] Additionally, Aspartate is the precursor for other the synthesis of other amino acids such as: Lysine, Threonine, and Methionine.[3]

D-Aspartate is one of two D-amino acids commonly found in mammals.[3] All other amino amino acids occur in, and are used by the body in their L confirmation.

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

Asp's L-isomer is one of the 22 proteinogenic amino acids, i.e., the building blocks of proteins. Asp (and glutamic acid) is classified as acidic, with a pKa of 3.9, however in a peptide this is highly dependent on the local environment (as with all amino acids), and could be as high as 14. Asp is pervasive in biosynthesis.

Discovery[edit]

Aspartic acid was first discovered in 1827 by Auguste-Arthur Plisson and Étienne Ossian Henry,[4] derived from asparagine, which had been isolated from asparagus juice in 1806, by boiling with a base.[5] After Asparagine is boiled with a strong base it must be hydrolyzed by either acid or alkali in order to yield aspartate. [5]

Biosynthesis[edit]

Because Aspartate can be synthesized by the body it is classified as a non-essential amino acid. In the human body, aspartate is most frequently synthesized through the transamination of oxaloacetate. The biosynthesis of Aspartate is facilitated by a class of enzyme called an aminotransferase. In other words, the transfer of an amine group by this enzyme from another molecule (i.e. alanine, glutamine) yields aspartate and an alpha-keto acid.[3] However, although aspartate is most commonly synthesized from oxaloacetate, it is also a byproduct of the urea cycle.

Aspartate is also involved in the synthesis of other amino acids such as: Lysine, Threonine, and Methionine

Chemical synthesis[edit]

Racemic aspartic acid can be synthesized from diethyl sodium phthalimidomalonate, (C6H4(CO)2NC(CO2Et)2).[6]

The major disadvantage of the above technique is that equimolar amounts of each enantiomer are made. Using biotechnology it is now possible to use immobilised enzymes to create just one type of enantiomer owing to their stereospecificity.

Forms and nomenclature[edit]

There are two forms or enantiomers of aspartic acid. The name "aspartic acid" can refer to either enantiomer or a mixture of two.[7] 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.

Metabolism[edit]

Aspartate is non-essential in mammals, being produced from oxaloacetate by transamination. 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.[8] 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)

Participation in the Urea Cycle[edit]

In the Urea cycle, Aspartate and Ammnonia donate amino groups leading to the formation of Urea

Other biochemical roles[edit]

Aspartate has many biochemical roles. Aspartate is a metabolite in the urea cycle 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 hydrogen acceptor in a chain of ATP synthase.

Through recent advances in technology, aspartate has been found to play vital roles in hormone production and secretion. Additionally aspartate has been shown to play a role in the regulation of neuronal transmission.[9]

Interactive pathway map[edit]

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

[[File:
GlycolysisGluconeogenesis_WP534 go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to Entrez go to article go to article go to article go to article go to article go to WikiPathways go to article go to Entrez go to article
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
GlycolysisGluconeogenesis_WP534 go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to Entrez go to article go to article go to article go to article go to article go to WikiPathways go to article go to Entrez go to article
|{{{bSize}}}px|alt=Glycolysis and Gluconeogenesis edit]]
Glycolysis and Gluconeogenesis edit
  1. ^ The interactive pathway map can be edited at WikiPathways: "GlycolysisGluconeogenesis_WP534". 

Neurotransmitter[edit]

Aspartate (the conjugate base of aspartic acid) stimulates NMDA receptors, though not as strongly as the amino acid neurotransmitter L-glutamate does.[10]

Applications & Market[edit]

The global market for aspartic acid is $117MM annually (50-60K MT/Yr)[11] with areas of growth accounting for an addressable market of $8.78BB.[12] 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.

Nearly all aspartic acid is manufactured in China.

Superabsorbent polymers

One area of aspartic acid market growth is biodegradable superabsorbent polymers (SAP). The super absorbent polymers market is anticipated to grow at a CAGR of 5.5% from 2014 to 2019 to reach a value of $8.78BB globally.[12] Around 75% of superabsorbent polymers are used in disposable diapers and an additional 20% is used for adult incontinence and feminine hygiene products. Polyaspartate, the polymerization product of aspartic acid, is a biodegradable substitute to polyacrylate.[13] The polyaspartate market comprises a small fraction (est. < 1%) of the total SAP market.

Additional uses

In addition to SAP, aspartic acid has applications in the $19B fertilizer industry, where polyaspartate improves water retention and nitrogen uptake;[14] the $1.1B (2020) concrete floor coatings market, where polyaspartic is a low VOC, low energy alternative to traditional epoxy resins;[15] and lastly the >$5B scale and corrosion inhibitors market.[16]

  • Aspartic acid is known to have a use in the synthesis of Lorglumide.

Supplement industry[edit]

D-Aspartic acid has been shown to increase levels of Luteinizing hormone as well as testosterone in men.[17] Its effectiveness in boosting these hormones has led to its popularity in the supplement industry where it is marketed and sold as a testosterone booster. Additionally, it has been proven to increase fertility and sperm motility in men with below average levels of fertility.[17] Studies have shown that long term supplementation (30 days or greater) does not show improvement in levels of testosterone.[18] However, earlier studies have shown that short term supplementation (approximately 12 days) does in fact lead to an increase in Luteinizing hormone and testosterone with 20 out 0f 23 subjects receiving D-Aspartic acid showing statistically significant increases in both hormones.[19]

Sources[edit]

Dietary sources[edit]

Aspartic acid is not an essential amino acid, which means that it can be synthesized from central metabolic pathway intermediates in humans. Aspartic acid is found in:

See also[edit]

References[edit]

  1. ^ a b "862. Aspartic acid". The Merck Index (11th ed.). 1989. p. 132. ISBN 0-911910-28-X. 
  2. ^ "ICSC 1439 - L-ASPARTIC ACID". inchem.org. 
  3. ^ a b c d e f G.,, Voet, Judith; W.,, Pratt, Charlotte. Fundamentals of biochemistry : life at the molecular level. ISBN 9781118918401. OCLC 910538334. 
  4. ^ Berzelius JJ, Öngren OG (1839). Traité de chimie (in French). 3. Brussels: A. Wahlen et Cie. p. 81. Retrieved 25 August 2015. 
  5. ^ Plimmer R (1912) [1908]. Plimmer R, Hopkins F, eds. The chemical composition of the proteins. Monographs on Biochemistry. Part I. Analysis (2nd ed.). London: Longmans, Green and Co. p. 112. Retrieved January 18, 2010. 
  6. ^ Dunn MS, Smart BW (1950). "DL-Aspartic Acid". Org. Synth. 30: 7. ; Coll. Vol., 4, p. 55 .
  7. ^ "Nomenclature and symbolism for amino acids and peptides (IUPAC-IUB Recommendations 1983)", Pure Appl. Chem., 56 (5): 595–624, 1984, doi:10.1351/pac198456050595 .
  8. ^ Lehninger AL, Nelson DL, Cox MM (2000). Principles of Biochemistry (3rd ed.). New York: W. H. Freeman. ISBN 1-57259-153-6. 
  9. ^ Han, Hai; Miyoshi, Yurika; Koga, Reiko; Mita, Masashi; Konno, Ryuichi; Hamase, Kenji (2015-12-10). "Changes in d-aspartic acid and d-glutamic acid levels in the tissues and physiological fluids of mice with various d-aspartate oxidase activities". Journal of Pharmaceutical and Biomedical Analysis. Recent Advances on D-Amino Acid Research. 116: 47–52. doi:10.1016/j.jpba.2015.05.013. 
  10. ^ 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. 
  11. ^ Evans J (2014). Commercial Amino Acids. BCC Research. pp. 101–103. 
  12. ^ a b Transparency Market Research. Superabsorbent polymers market - global industry analysis, size, share, growth, trends and forecase, 2014-2020. (2014).
  13. ^ Alford DD, Wheeler AP, Pettigrew CA (1994). "Biodegradation of thermally synthesized polyaspartate". J Environ Polym Degr. 2: 225–236. 
  14. ^ Kelling K (2001). Crop Responses to Amisorb in the North Central Region. University of Wisconsin-Madison. 
  15. ^ Global concrete floor coatings market will be worth US$1.1 bn by 2020. Transparency Market Research (2015).
  16. ^ Corrosion inhibitors market analysis by product, by application, by end-use industry, and segment forecasts to 2020. Grand View Research (2014)
  17. ^ a b D’Aniello, Gemma; Ronsini, Salvatore; Notari, Tiziana; Grieco, Natascia; Infante, Vincenzo; D’Angel, Nicola; Mascia, Fara; Fiore, Maria Maddalena Di; Fisher, George. "D-Aspartate, a Key Element for the Improvement of Sperm Quality". Advances in Sexual Medicine. 02 (04): 45–53. doi:10.4236/asm.2012.24008. 
  18. ^ Willoughby, Darryn S.; Leutholtz, Brian. "d-Aspartic acid supplementation combined with 28 days of heavy resistance training has no effect on body composition, muscle strength, and serum hormones associated with the hypothalamo-pituitary-gonadal axis in resistance-trained men". Nutrition Research. 33 (10): 803–810. doi:10.1016/j.nutres.2013.07.010. 
  19. ^ Topo, Enza; Soricelli, Andrea; D'Aniello, Antimo; Ronsini, Salvatore; D'Aniello, Gemma (2009-01-01). "The role and molecular mechanism of D-aspartic acid in the release and synthesis of LH and testosterone in humans and rats". Reproductive Biology and Endocrinology. 7: 120. doi:10.1186/1477-7827-7-120. ISSN 1477-7827. PMC 2774316Freely accessible. PMID 19860889. 
  20. ^ Salunkhe DK, Kadam S (18 August 1995). Handbook of Fruit Science and Technology: Production, Composition, Storage, and Processing. CRC Press. pp. 368–. ISBN 978-0-8247-9643-3. 
  21. ^ Considine DM (6 December 2012). Foods and Food Production Encyclopedia. Springer Science & Business Media. pp. 114–. ISBN 978-1-4684-8511-0. 

External links[edit]