2,6-dioxo-6-phenylhexa-3-enoate hydrolase
| 2,6-dioxo-6-phenylhexa-3-enoate hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.7.1.8 | ||||||||
| CAS no. | 102925-38-2 | ||||||||
| 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 2,6-dioxo-6-phenylhexa-3-enoate hydrolase (EC 3.7.1.8) is an enzyme that catalyzes the chemical reaction
- 2,6-dioxo-6-phenylhexa-3-enoate + H2O benzoate + 2-oxopent-4-enoate
Thus, the two substrates of this enzyme are 2,6-dioxo-6-phenylhexa-3-enoate and H2O, whereas its two products are benzoate and 2-oxopent-4-enoate.
This enzyme belongs to the family of hydrolases, specifically those acting on carbon-carbon bonds in ketonic substances. The systematic name of this enzyme class is 2,6-dioxo-6-phenylhexa-3-enoate benzoylhydrolase. This enzyme is also called HOHPDA hydrolase. This enzyme participates in biphenyl degradation and fluorene degradation.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1C4X, 1J1I, and 2OG1.
References
- Omori T, Sugimura K, Ishigooka H, Minoda Y (1986). "Purification and some properties of a 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid hydrolyzing enzyme from Pseudomonas cruciviae S93 B1 involved in the degradation of biphenyl". Agric. Biol. Chem. 50 (4): 931–937. doi:10.1271/bbb1961.50.931.
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