Aspartic acid, represented by the symbol Asp or D, is an α-amino acid essential for protein biosynthesis. Aspartic acid possesses an acidic side chain (CH2COOH) that interacts with other amino acids, enzymes, and proteins in the body. Under physiological conditions (pH 7.4) within proteins, the side chain typically occurs as the negatively charged aspartate form, −COO. Aspartate side chains in proteins often form hydrogen bonds, giving rise to asx turns or asx motifs that frequently appear at the N-termini of alpha helices. Aspartate serves various biochemical roles. It functions as a metabolite in the urea cycle and participates in gluconeogenesis. It plays a role in the malate-aspartate shuttle, where it carries reducing equivalents and readily interconverts with oxaloacetate, the oxidized form of malic acid. Aspartate contributes one nitrogen atom in the biosynthesis of inosine, which serves as a precursor to the purine bases. Additionally, aspartic acid acts as a hydrogen acceptor in the ATP synthase chain. Dietary L-aspartic acid has been shown to act as an inhibitor of Beta-glucuronidase, regulating the enterohepatic circulation of bilirubin and bile acids. Aspartic acid is encoded by the codons GAU and GAC.

Structure
CAS Number 56-84-8
Classification

Acidic (negatively charged) amino acids include

Aspartic acid

Glutamic acid

Categories

Aspartic acid and Derivatives:

Aspartic acid:

Derivatives: