Styrene-oxide isomerase - Misplaced Pages

This enzyme belongs to the family of isomerases, specifically a class of other intramolecular oxidoreductases. 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. 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

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. PMC 11374702.

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

v t e Isomerases: intramolecular oxidoreductases (EC 5.3)
5.3.1: Aldoses/Ketoses	Triosephosphate isomerase Ribose-5-phosphate isomerase Mannose phosphate isomerase Glucose isomerase
5.3.2: Keto/Enol	Phenylpyruvate tautomerase Oxaloacetate tautomerase 4-Oxalocrotonate tautomerase
5.3.3: C = C	Steroid D-isomerase Isopentenyl-diphosphate delta isomerase Vinylacetyl-CoA D-isomerase Muconolactone D-isomerase Cholestenol Delta-isomerase (EBP) Methylitaconate D-isomerase Aconitate Delta-isomerase Enoyl CoA isomerase Prostaglandin-A1 Delta-isomerase 5-carboxymethyl-2-hydroxymuconate D-isomerase Isopiperitenone D-isomerase L-dopachrome isomerase Polyenoic fatty acid isomerase
5.3.4: S-S	Protein disulfide-isomerase (PDIA3)
5.3.99: other	Prostaglandin D2 synthase/Prostaglandin-D synthase Prostaglandin E synthase Prostacyclin synthase Thromboxane-A synthase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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