Styrene oxide isomerase

From Proteopedia

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.

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 (PDB code 8pnv)

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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