Unusual C=C bond isomerization of an α,β-unsaturated γ-butyrolactone catalysed by flavoproteins from the old yellow enzyme family
| Autor: | Katharina Durchschein, Peter Macheroux, Silvia Wallner, Klaus Zangger, Kurt Faber, Walter M. F. Fabian |
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| Rok vydání: | 2012 |
| Předmět: |
Isomerase activity
biocatalysis Stereochemistry Stereoisomerism Isomerase Flavin group Biochemistry flavins isomerases 4-Butyrolactone Organic chemistry Molecule C=C isomerization Molecular Biology Flavoproteins Molecular Structure Chemistry Hydride Organic Chemistry NADPH Dehydrogenase Full Papers oxidoreductases enzymes and coenzymes (carbohydrates) Biocatalysis Molecular Medicine Thermodynamics Isomerization Oxidation-Reduction |
| Zdroj: | Chembiochem |
| ISSN: | 1439-7633 |
| Popis: | An unexpected, redox-neutral C=C bond isomerization of a γ-butyrolactone bearing an exo-methylene unit to the thermodynamically more favoured endo isomer (k(cat) =0.076 s(-1) ) catalysed by flavoproteins from the Old Yellow Enzyme family was discovered. Theoretical calculations and kinetic data support a mechanism through which the isomerization proceeds through FMN-mediated hydride addition onto exo-Cβ, followed by hydride abstraction from endo-Cβ', which is in line with the well-established C=C bond bioreduction of OYEs. This new isomerase activity enriches the catalytic versatility of ene-reductases. |
| Databáze: | OpenAIRE |
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