Vanillyl-alcohol oxidase, a tasteful biocatalyst
| Autor: | Willem J. H. van Berkel, Andrea Mattevi, Robert H. H. van den Heuvel, Marco W. Fraaije, Colja Laane |
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| Přispěvatelé: | Groningen Biomolecular Sciences and Biotechnology |
| Jazyk: | angličtina |
| Rok vydání: | 2001 |
| Předmět: |
Vanillyl-alcohol oxidase
biology Stereochemistry Process Chemistry and Technology Crystal structure Active site Biochemie Bioengineering Flavin group Enantioselectivity Biochemistry Catalysis Enzyme catalysis Hydroxylation chemistry.chemical_compound Covalent flavoprotein Stereospecificity chemistry Vanillin biology.protein Organic chemistry Dehydrogenation Protein engineering Coniferyl alcohol VLAG |
| Zdroj: | Journal of Molecular Catalysis. B, Enzymatic, 11, 185-188 Journal of Molecular Catalysis B: Enzymatic, 11(4). ELSEVIER SCIENCE BV Journal of Molecular Catalysis. B, Enzymatic 11 (2001) |
| ISSN: | 1381-1177 |
| Popis: | The covalent flavoenzyme vanillyl-alcohol oxidase (VAO) is a versatile biocatalyst. It converts a wide range of phenolic compounds by catalysing oxidation, deamination, demethylation, dehydrogenation and hydroxylation reactions. The production of natural vanillin, 4-hydroxybenzaldehyde, coniferyl alcohol and enantiomeric pure phenol derivatives is of interest for biotechnological applications. The hydroxylation of 4-alkylphenols is highly stereospecific for the (R)-isomer, whereas dehydrogenation of these substrates is specific for the cis- or trans-isomer. On the basis of crystallographic data, we suggest that the stereospecificity is related to the active site residue Asp170. Another important feature of VAO is the covalent flavin attachment. Studies from site-directed mutants suggest that the covalent flavin–protein interaction improves the catalytic performance as well as the long-term stability of VAO. |
| Databáze: | OpenAIRE |
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