Styrene-oxide isomerase
| styrene-oxide isomerase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.3.99.7 | ||||||||
| CAS no. | 124541-89-5 | ||||||||
| 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, a styrene-oxide isomerase (EC 5.3.99.7) is an enzyme that catalyzes the chemical reaction
- styrene oxide phenylacetaldehyde
Hence, this enzyme has one substrate, styrene oxide, and one product, phenylacetaldehyde.
This enzyme belongs to the family of isomerases, specifically a class of other intramolecular oxidoreductases[1]. The systematic name of this enzyme class is styrene-oxide isomerase (epoxide-cleaving). This enzyme is also called SOI. This enzyme participates in styrene degradation and is the second step of the pathway after the epoxidation of styrene by styrene monooxygenase.
SOI is an integral membrane protein consisting of four transmembrane helices. Khanppnavar et al[2] determined the first cryo-EM structures of this protein, which show that SOI forms a novel homo-trimeric assembly, displaying a structural fold reminiscent of ion channels.
The trimeric organization of SOI is essential for its function and is guided by the ferric heme b prosthetic group positioned at the interface of its subunits. This ferric heme b acts as a Lewis acid, interacting with the epoxide oxygen atom to facilitate epoxide ring-opening of substrates.
References[edit]
- Hartmans S, Smits JP, van der Werf MJ, Volkering F, de Bont JA (1989). "Metabolism of Styrene Oxide and 2-Phenylethanol in the Styrene-Degrading Xanthobacter Strain 124X". Appl. Environ. Microbiol. 55 (11): 2850–2855. Bibcode:1989ApEnM..55.2850H. doi:10.1128/aem.55.11.2850-2855.1989. PMC 203180. PMID 16348047.
- Khanppnavar, B., Choo, J.P.S., Hagedoorn, PL. et al. Structural basis of the Meinwald rearrangement catalysed by styrene oxide isomerase. Nat. Chem. (2024). https://doi.org/10.1038/s41557-024-01523-y
- ^ Hartmans, S.; Smits, J. P.; van der Werf, M. J.; Volkering, F.; de Bont, J. A. M. (November 1989). "Metabolism of Styrene Oxide and 2-Phenylethanol in the Styrene-Degrading Xanthobacter Strain 124X". Applied and Environmental Microbiology. 55 (11): 2850–2855. Bibcode:1989ApEnM..55.2850H. doi:10.1128/aem.55.11.2850-2855.1989. ISSN 0099-2240. PMC 203180. PMID 16348047.
- ^ Khanppnavar, Basavraj; Choo, Joel P. S.; Hagedoorn, Peter-Leon; Smolentsev, Grigory; Štefanić, Saša; Kumaran, Selvapravin; Tischler, Dirk; Winkler, Fritz K.; Korkhov, Volodymyr M.; Li, Zhi; Kammerer, Richard A.; Li, Xiaodan (2024-05-14). "Structural basis of the Meinwald rearrangement catalysed by styrene oxide isomerase". Nature Chemistry: 1–9. doi:10.1038/s41557-024-01523-y. ISSN 1755-4330.