Styrene oxide isomerase

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'''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.
'''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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<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=''>
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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 (PDB code [[8pnv]])' scene=''>
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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.

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

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