This enzyme belongs to the family of lyases, specifically the amine-lyases, which cleave carbon-nitrogen bonds.

4-hydroxy-tetrahydrodipicolinate synthase is the key enzyme in lysine biosynthesis via the diaminopimelate pathway of prokaryotes, some phycomycetes, and higher plants.

[5] Three other proteins are structurally related to this enzyme and probably also act via a similar catalytic mechanism.

These are Escherichia coli N-acetylneuraminate lyase (EC 4.1.3.3) (protein NanA), which catalyses the condensation of N-acetyl-D-mannosamine and pyruvate to form N-acetylneuraminate; Rhizobium meliloti (Sinorhizobium meliloti) protein MosA,[6] which is involved in the biosynthesis of the rhizopine 3-O-methyl-scyllo-inosamine; and E. coli hypothetical protein YjhH.

The structure takes the form of a homotetramer, in which 2 monomers are related by an approximate 2-fold symmetry.