Aminocarboxymuconate-semialdehyde decarboxylase

In enzymology, an aminocarboxymuconate-semialdehyde decarboxylase is an enzyme that catalyzes the chemical reaction


 * 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate $$\rightleftharpoons$$ 2-aminomuconate semialdehyde + CO2

Hence, this enzyme has one substrate, 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate, and two products, 2-aminomuconate semialdehyde 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 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate carboxy-lyase (2-aminomuconate-semialdehyde-forming). Other names in common use include picolinic acid carboxylase, picolinic acid decarboxylase, alpha-amino-beta-carboxymuconate-epsilon-semialdehade decarboxylase, alpha-amino-beta-carboxymuconate-epsilon-semialdehyde, beta-decarboxylase, 2-amino-3-(3-oxoprop-2-enyl)but-2-enedioate carboxy-lyase, and 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate carboxy-lyase. This enzyme participates in tryptophan metabolism.

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