3-carboxy-cis,cis-muconate cycloisomerase
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
| 3-carboxy-cis,cis-muconate cycloisomerase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 5.5.1.2 | ||||||||
| CAS number | 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 | ||||||||
| |||||||||
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.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1Q5N.
gollark: Apologies, my internet connection briefly incursed.
gollark: - also the cubes, I guess
gollark: Well, various possibilities exist:- add "exist again" after "exit the zzcxz" - this could take you to a new area with more doors or something- somehow add a mysterious button on the wall of one of the halls which switches the door to osmarks.net mode (somehow²)- "go in an anomalous direction" (or somehow "go up"/"go down") in the initial room- in the bee room, one series of choices could allow access to it- the "sandy ground" area after going backward
gollark: Yes, that is what I was wondering.
gollark: Hmm, where would it actually go? I guess I could repurpose one of the doors.
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.
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