Aminocarboxymuconate-semialdehyde decarboxylase
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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 \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.

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Contents

Structural studies

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

References

External links

The CAS registry number for this enzyme class is 37289-47-7.

Gene Ontology (GO) codes

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