4-carboxymuconolactone decarboxylase

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In enzymology, a 4-carboxymuconolactone decarboxylase (EC 4.1.1.44) is an enzyme that catalyzes the chemical reaction

2-carboxy-2,5-dihydro-5-oxofuran-2-acetate $\rightleftharpoons$ 4,5-dihydro-5-oxofuran-2-acetate + CO₂

Hence, this enzyme has one substrate, 2-carboxy-2,5-dihydro-5-oxofuran-2-acetate, and two products, 4,5-dihydro-5-oxofuran-2-acetate 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-carboxy-2,5-dihydro-5-oxofuran-2-acetate carboxy-lyase (4,5-dihydro-5-oxofuran-2-acetate-forming). Other names in common use include gamma-4-carboxymuconolactone decarboxylase, and 4-carboxymuconolactone carboxy-lyase. This enzyme participates in benzoate degradation via hydroxylation.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2AF7.

[edit] References

IUBMB entry for 4.1.1.44
BRENDA references for 4.1.1.44 (Recommended.)
PubMed references for 4.1.1.44
PubMed Central references for 4.1.1.44
Google Scholar references for 4.1.1.44
Ornston LN (1966). "The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida. 3. Enzymes of the catechol pathway". J. Biol. Chem. 241: 3795–9. PMID 5330966.
Ornston LN (1970). "Conversion of catechol and protocatechuate to beta-ketoadipate (Pseudomonas putida)". Methods Enzymol. 17A: 529–549.