3-carboxy-cis,cis-muconate cycloisomerase
| 3-carboxy-cis,cis-muconate cycloisomerase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.5.1.2 | ||||||||
| CAS no. | 9075-77-8 | ||||||||
| 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 / QuickGO | ||||||||
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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 cis,cis-butadiene-1,2,4-tricarboxylate
Hence, this enzyme has one substrate, , 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.
Structural studies[]
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1Q5N.
References[]
- Ornston LN (August 1966). "The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida. II. Enzymes of the protocatechuate pathway". The Journal of Biological Chemistry. 241 (16): 3787–94. PMID 5916392.
- Ornston LN (1970). "Conversion of catechol and protocatechuate to beta-ketoadipate (Pseudomonas putida)". Methods Enzymol. 17A: 529–549. doi:10.1016/0076-6879(71)17237-0.
Categories:
- EC 5.5.1
- Enzymes of known structure
- Isomerase stubs