3-carboxy-cis,cis-muconate cycloisomerase

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In enzymology, a 3-carboxy-cis,cis-muconate cycloisomerase (EC 5.5.1.2) is an enzyme that catalyzes the chemical reaction

2-carboxy-2,5-dihydro-5-oxofuran-2-acetate $\rightleftharpoons$ cis,cis-butadiene-1,2,4-tricarboxylate

Hence, this enzyme has one substrate, 2-carboxy-2,5-dihydro-5-oxofuran-2-acetate, and one product, cis,cis-butadiene-1,2,4-tricarboxylate.

This enzyme belongs to the family of isomerases, specifically intramolecular lyases. The systematic name of this enzyme class is 2-carboxy-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing). Other names in common use include beta-carboxymuconate lactonizing enzyme, and 3-carboxymuconolactone hydrolase. 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 1Q5N.

[edit] References

IUBMB entry for 5.5.1.2
BRENDA references for 5.5.1.2 (Recommended.)
PubMed references for 5.5.1.2
PubMed Central references for 5.5.1.2
Google Scholar references for 5.5.1.2
Ornston LN (1966). "The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida. II. Enzymes of the protocatechuate pathway". J. Biol. Chem. 241: 3787–94. PMID 5916392.
Ornston LN (1970). "Conversion of catechol and protocatechuate to beta-ketoadipate (Pseudomonas putida)". Methods Enzymol. 17A: 529–549.