Dihydrodipicolinate synthase

In enzymology, a dihydrodipicolinate synthase is an enzyme that catalyzes the chemical reaction


 * L-aspartate 4-semialdehyde + pyruvate $$\rightleftharpoons$$ (S)-2,3-dihydropyridine-2,6-dicarboxylate + 2 H2O

Thus, the two substrates of this enzyme are L-aspartate 4-semialdehyde and pyruvate, whereas its two products are (S)-2,3-dihydropyridine-2,6-dicarboxylate and H2O.

This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is L-aspartate-4-semialdehyde hydro-lyase [adding pyruvate and cyclizing; (S)-2,3-dihydropyridine-2,6-dicarboxylate-forming]. Other names in common use include dihydropicolinate synthetase, dihydrodipicolinic acid synthase, L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and, and cyclizing). This enzyme participates in lysine biosynthesis.

Structural studies
As of late 2007, 16 structures have been solved for this class of enzymes, with PDB accession codes, , , , , , , , , , , , , , , and.