What is it about?
This review describes the discovery, origin and extensive characterization of a fungal enzyme that has grown into a founding member of a new family of flavoproteins. Like VAO, most members of this family contain a covalently bound FAD as prosthetic group. Protein engineering was used to unravel the role of the covalent attachment of the flavin and the function of a wide range of active site residues.
Featured Image
Why is it important?
This review not only explains in detail the mechanism of catalysis of VAO but also gives insights into the dynamic features of the enzyme that are important for substrate access and product release. Furthermore, it is described how rational engineering and directed evolution were used to disclose and improve the biocatalytic properties of VAO and related family members.
Perspectives
The description of the mechanistic features and molecular phylogeny of VAO gives many opportunities for future studies, directed at the application of VAO and many of its uncharacterized family members in a circular bioeconomy.
Professor Willem J.H. van Berkel
Wageningen University
Read the Original
This page is a summary of: Vanillyl alcohol oxidase, January 2020, Elsevier,
DOI: 10.1016/bs.enz.2020.05.003.
You can read the full text:
Contributors
The following have contributed to this page
