Aminocarboxymuconate-semialdehyde decarboxylase

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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

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[edit]

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2F6K and 2HBV.

References[edit]

  • 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.