| α-Pinene-oxide decyclase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.5.1.10 | ||||||||
| CAS no. | 112692-50-9 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, an α-pinene-oxide decyclase (EC 5.5.1.10) is an enzyme that catalyzes the chemical reaction
- α-pinene oxide (Z)-2-methyl-5-isopropylhexa-2,5-dienal
Hence, this enzyme has one substrate, α-pinene oxide, and one product, (Z)-2-methyl-5-isopropylhexa-2,5-dienal.
This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is α-pinene-oxide lyase (decyclizing). This enzyme is also called α-pinene oxide lyase. This enzyme participates in limonene and pinene degradation.
References
- Griffiths ET, Harries PC, Jeffcoat R, Trudgill PW (1987). "Purification and properties of alpha-pinene oxide lyase from Nocardia sp. strain P18.3". J. Bacteriol. 169 (11): 4980–3. PMC 213896. PMID 3667522.
This page was last edited on 26 August 2023, at 13:07