Aspartic acid in the context of De novo synthesis

An essential amino acid, or indispensable amino acid, is an amino acid that cannot be synthesized from scratch by the organism fast enough to supply its demand, and must therefore come from the diet. Of the 21 amino acids common to all life forms, the nine amino acids humans cannot synthesize are valine, isoleucine, leucine, methionine, phenylalanine, tryptophan, threonine, histidine, and lysine.

Six other amino acids are considered conditionally essential in the human diet, meaning their synthesis can be limited under special pathophysiological conditions, such as prematurity in the infant or individuals in severe catabolic distress. These six are arginine, cysteine, glycine, glutamine, proline, and tyrosine. Six amino acids are non-essential (dispensable) in humans, meaning they can be synthesized in sufficient quantities in the body. These six are alanine, aspartic acid, asparagine, glutamic acid, serine, and selenocysteine (considered the 21st amino acid). Pyrrolysine (considered the 22nd amino acid), which is proteinogenic only in certain microorganisms, is not used by and therefore non-essential for most organisms, including humans.

Threonine (symbol Thr or T) is an amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH
₃ form when dissolved in water), a carboxyl group (which is in the deprotonated −COO form when dissolved in water), and a side chain containing a hydroxyl group, making it a polar, uncharged amino acid. It is essential in humans, meaning the body cannot synthesize it: it must be obtained from the diet. Threonine is synthesized from aspartate in bacteria such as E. coli. It is encoded by all the codons starting AC (ACU, ACC, ACA, and ACG).

Threonine sidechains are often hydrogen bonded; the most common small motifs formed are based on interactions with serine: ST turns, ST motifs (often at the beginning of alpha helices) and ST staples (usually at the middle of alpha helices).

In organic chemistry, a dicarboxylic acid is an organic compound containing two carboxyl groups (−COOH). The general molecular formula for dicarboxylic acids can be written as HO₂C−R−CO₂H, where R can be aliphatic or aromatic. In general, dicarboxylic acids show similar chemical behavior and reactivity to monocarboxylic acids. Dicarboxylic acids are usually colorless solids. A wide variety of dicarboxylic acids are used in industry. Adipic acid, for example, is a precursor to certain kinds of nylon. A wide variety of dicarboxylic acids are found in nature. Aspartic acid and glutamic acid are two amino acids found in all life. Succinic and fumaric acids are essential for metabolism. A large inventory of derivatives are known including many mono- and diesters, amides, etc.

Aspartame is an artificial, non-saccharide sweetener commonly used as a sugar substitute in foods and beverages. It is 200 times sweeter than sucrose, and is a methyl ester of the aspartic acid/phenylalanine dipeptide with brand names NutraSweet, Equal, and Canderel. Discovered in 1965, aspartame was approved by the US Food and Drug Administration (FDA) in 1974 and re-approved in 1981 after its initial approval was briefly revoked.

Aspartame is one of the most studied food additives in the human food supply. Reviews by over 100 governmental regulatory bodies found the ingredient safe for consumption at the normal acceptable daily intake limit.

A phosphoprotein is a protein that is posttranslationally modified by the attachment of either a single phosphate group, or a complex molecule such as 5'-phospho-DNA, through a phosphate group. The target amino acid is most often serine, threonine, or tyrosine residues (mostly in eukaryotes), or aspartic acid or histidine residues (mostly in prokaryotes).