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Aspartic acid is an alpha-amino acid with two carboxyl groups, represented in a neutral structural form as $\mathrm{HOOC}-\mathrm{CH}(\mathrm{N}{\mathrm{H}}_2)-\mathrm{C}{\mathrm{H}}_2-\mathrm{COOH}$. Its molecular formula is ${\mathrm{C}}_4{\mathrm{H}}_7\mathrm{N}{\mathrm{O}}_4$. One carboxyl group belongs to the amino-acid backbone and the other terminates the side chain.^[ref]

The protein-associated L configuration and the sequence symbols Asp and D are separate naming conventions. A one-letter D in a protein sequence denotes the aspartic-acid residue; it is not a declaration of D stereochemistry.^[ref]

Loss or redistribution of protons changes the ionic form. The name aspartate commonly denotes the anionic form. For example, a form with two carboxylates carrying $-1$ each and an ammonium group carrying $+1$ has net charge $-1-1+1=-1$. This charge count must be kept distinct from the L/D configuration and from atom connectivity.

The side-chain carboxyl chemistry also matters in aspartic proteases, where appropriately positioned acidic groups participate in peptide bond hydrolysis. Presence of an aspartic-acid residue alone does not establish catalytic activity: its geometry and chemical environment matter.^[ref]

An aspartic protease is a protease whose catalytic chemistry depends on aspartic acid side chains. In common examples, their carboxyl groups position and activate a water molecule for peptide bond hydrolysis. Water supplies the attacking nucleophile, unlike a mechanism in which an enzyme side chain itself makes the initial covalent attack.^[ref]

The name concerns catalytic groups, rather than requiring an aspartic-acid residue at every substrate cleavage site. Substrate recognition and catalytic mechanism are distinct properties.

HIV-1 protease provides an experimentally characterized example. In 1989, T. D. Meek and colleagues measured apparent masses of approximately 11,000 under denaturing conditions and 22,000 under nondenaturing conditions; protein cross-linking supplied additional evidence for an active protein dimer. The ratio $22,000/11,000=2$ explains the subunit interpretation.^[ref]

The same study found pH-dependent inactivation consistent with a required unprotonated carboxyl group in the active site. Combining this chemical perturbation with cleavage activity and subunit measurements supported a catalytic classification more specifically than the enzyme's molecular mass alone.^[ref]