Diaminopimelate decarboxylase

In enzymology, a diaminopimelate decarboxylase is an enzyme that catalyzes the chemical reaction


 * meso-2,6-diaminoheptanedioate $$\rightleftharpoons$$ L-lysine + CO2

Hence, this enzyme has one substrate, meso-2,6-diaminoheptanedioate, and two products, L-lysine and CO2.

This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is meso-2,6-diaminoheptanedioate carboxy-lyase (L-lysine-forming). Other names in common use include diaminopimelic acid decarboxylase, meso-diaminopimelate decarboxylase, DAP-decarboxylase, and meso-2,6-diaminoheptanedioate carboxy-lyase. This enzyme participates in lysine biosynthesis. It employs one cofactor, pyridoxal phosphate.

Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes, , , , , , , and.