Aminocarboxymuconate-semialdehyde decarboxylase

aminocarboxymuconate-semialdehyde decarboxylase
Identifiers
EC number	4.1.1.45
CAS number	37289-47-7
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search PMC articles PubMed articles NCBI proteins

In enzymology, an aminocarboxymuconate-semialdehyde decarboxylase (EC 4.1.1.45) 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 2F6K and 2HBV.

References

• SENOH S; Nakamura, S; Kawai, H; Honjo, T; Nishizuka, Y; Hayaishi, O; Senoh, S (1965). "STUDIES ON THE METABOLISM OF THE BENZENE RING OF TRYPTOPHAN IN MAMMALIAN TISSUES. II. ENZYMIC FORMATION OF ALPHA-AMINOMUCONIC ACID FROM 3-HYDROXYANTHRANILIC ACID". J. Biol. Chem. 240: 740–9. PMID 14275130.