The enzyme 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase (EC 4.1.1.68) catalyzes the chemical reaction
| 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.1.68 | ||||||||
| 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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- 5-oxopent-3-ene-1,2,5-tricarboxylate 2-oxohept-3-enedioate + 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 5-oxopent-3-ene-1,2,5-tricarboxylate carboxy-lyase (2-oxohept-3-enedioate-forming). Other names in common use include 5-carboxymethyl-2-oxo-hex-3-ene-1,6-dioate decarboxylase, and 5-oxopent-3-ene-1,2,5-tricarboxylate carboxy-lyase. This enzyme participates in tyrosine metabolism.
Structural studies
editAs of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1I7O.
References
edit- Garrido-Peritierra A, Cooper RA (July 1981). "Identification and purification of distinct isomerase and decarboxylase enzymes involved in the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli". European Journal of Biochemistry. 117 (3): 581–4. doi:10.1111/j.1432-1033.1981.tb06377.x. PMID 7026235.
