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 | ||||||||
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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 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.