Arginine decarboxylase

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


 * L-arginine $$\rightleftharpoons$$ agmatine + CO2

Hence, this enzyme has one substrate, L-arginine, and two products, agmatine 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 L-arginine carboxy-lyase (agmatine-forming). Other names in common use include SpeA, and L-arginine carboxy-lyase. This enzyme participates in urea cycle and metabolism of amino groups and glutamate metabolism. It employs one cofactor, pyridoxal phosphate.

Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes, , , , and.