Aminocarboxymuconate-semialdehyde decarboxylase

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aminocarboxymuconate-semialdehyde decarboxylase
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aminocarboxymuconate-semialdehyde decarboxylase dimer, Human
Identifiers
EC number4.1.1.45
CAS number37289-47-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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. This enzyme participates in tryptophan metabolism.

Nomenclature[edit]

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.

References[edit]

Further reading[edit]

  • Ichiyama A, Nakamura S, Kawai H, Honjo T, Nishizuka Y, Hayaishi O, Senoh S (February 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". The Journal of Biological Chemistry. 240: 740–9. PMID 14275130.