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Styrene oxide isomerase
From Proteopedia
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<StructureSection load='8PNV' size='340' side='right' caption='The cryo-EM structure of the SOI-NB complex reveals that the quaternary structure of SOI consists of a homo-trimeric assembly. Each nanobody binds at the interface of two SOI protomers. Additionally, two nanobody molecules interact with each other, resulting in the formation of a dimer of trimer assemblies within the SOI-nanobody complex.. scene=''> | <StructureSection load='8PNV' size='340' side='right' caption='The cryo-EM structure of the SOI-NB complex reveals that the quaternary structure of SOI consists of a homo-trimeric assembly. Each nanobody binds at the interface of two SOI protomers. Additionally, two nanobody molecules interact with each other, resulting in the formation of a dimer of trimer assemblies within the SOI-nanobody complex.. scene=''> | ||
| - | == Structural | + | == Structural features == |
SOI is an integral membrane protein with four transmembrane helices. It forms a novel homo-trimeric assembly with a structural fold reminiscent of ion channels. The trimeric organization, crucial for its function, is mediated by a ferric heme b prosthetic group positioned between two protomers. This ferric heme b acts as a Lewis acid, interacting with the epoxide oxygen atom of epoxide substrate, facilitating the ring-opening. | SOI is an integral membrane protein with four transmembrane helices. It forms a novel homo-trimeric assembly with a structural fold reminiscent of ion channels. The trimeric organization, crucial for its function, is mediated by a ferric heme b prosthetic group positioned between two protomers. This ferric heme b acts as a Lewis acid, interacting with the epoxide oxygen atom of epoxide substrate, facilitating the ring-opening. | ||
Current revision
Styrene oxide isomerase (SOI) is an enzyme (EC 5.3.99.7) that catalyses isomerization of styrene oxide to phenylacetaldehyde. SOI is one of the rate-limiting step enzyme in bacterial styrene degradation pathways.
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References
1. Panke S, Witholt B, Schmid A, Wubbolts MG. 1998. Towards a Biocatalyst for (S)-Styrene Oxide Production: Characterization of the Styrene Degradation Pathway of Pseudomonas sp. Strain VLB120. Appl Environ Microbiol 64:. https://doi.org/10.1128/AEM.64.6.2032-2043.1998
2. Nobuya Itch, Kunimasa Hayashi, Keisaku Okada, Takeshi Ito, Naoyuki Mizuguchi, Characterization of Styrene Oxide Isomerase, a Key Enzyme of Styrene and Styrene Oxide Metabolism in Corynehacterium sp., Bioscience, Biotechnology, and Biochemistry, Volume 61, Issue 12, 1 January 1997, Pages 2058–2062, https://doi.org/10.1271/bbb.61.2058
3. Khanppnavar, B., Choo, J.P.S., Hagedoorn, PL. et al. Structural basis of the Meinwald rearrangement catalysed by styrene oxide isomerase. Nature Chemistry. (2024) https://doi.org/10.1038/s41557-024-01523-y
