Aspartic acid (symbol Asp or D;
Like all other amino acids, aspartic acid contains an amino group and a carboxylic acid. Its α-amino group is in the protonated –NH 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.
In proteins aspartate sidechains are often hydrogen bonded to form or , which frequently occur at the N-termini of alpha helices.
Aspartic acid, like glutamic acid, is classified as an acidic amino acid, with a PKa 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,
Discovery
Aspartic acid was first discovered in 1827 by Auguste-Arthur Plisson and Étienne Ossian Henry
by
hydrolysis of
asparagine, which had been isolated from
asparagus juice in 1806.
Their original method used
lead hydroxide, but various other acids or bases are now more commonly used instead.
Forms and nomenclature
There are two forms or
of aspartic acid. The name "aspartic acid" can refer to either enantiomer or a mixture of two.
[.] 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.
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.
Chemical synthesis
Industrially, aspartate is produced by amination of
fumarate catalyzed by L-aspartate ammonia-lyase.
Racemic aspartic acid can be synthesized from diethyl sodium phthalimidomalonate,
(C6H4(CO)2NC(CO2Et)2).[.]
Metabolism
In plants and
, 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
2CCH(NH
2)CH
2CHO.
is derived from aspartate via transamidation:
- −O2CCH(NH2)CH2CO2− + GC(O)NH3+ → O2CCH(NH2)CH2CONH3+ + GC(O)O
(where
GC(O)NH
2 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 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.
Interactive pathway map
Neurotransmitter
Aspartate (the
conjugate base of aspartic acid) stimulates
, though not as strongly as the amino acid neurotransmitter
glutamic acid does.
Applications & market
In 2014, the global market for aspartic acid was
or about $117 million annually
with potential areas of growth accounting for an of $8.78 billion (Bn).
[Transparency Market Research. Superabsorbent polymers market - global industry analysis, size, share, growth, trends and forecase, 2014-2020. (2014).] 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.
Superabsorbent polymers
One area of aspartic acid market growth is
biodegradable superabsorbent polymers (SAP), and hydrogels.
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.
Around 75% of superabsorbent polymers are used in disposable
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.
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 $19Bn
Fertilizer, where polyaspartate improves water retention and nitrogen uptake;
the $1.1Bn (2020) concrete floor coatings market, where polyaspartic is a low VOC, low energy alternative to traditional epoxy resins;
[Global concrete floor coatings market will be worth US$1.1Bn by 2020. Transparency Market Research (2015).] and lastly the >$5Bn scale and corrosion inhibitors market.
[Corrosion inhibitors market analysis by product, by application, by end-use industry, and segment forecasts to 2020. Grand View Research (2014)]
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
Eukaryote cells, roughly 1 in 20 amino acids incorporated into a protein is an aspartic acid,
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
See also
-
Aspartate transaminase
-
Polyaspartic acid
-
Sodium polyaspartate, a synthetic polyamide
External links
