Citation

Ewing TA, Gygli G, Fraaije MW, van Berkel WJH. The Enzymes 2020; 47: 87-116.

Copyright

(Copyright © 2020)

DOI

10.1016/bs.enz.2020.05.003

PMID

32951836

Abstract

This review presents a historical outline of the research on vanillyl alcohol oxidase (VAO) from Penicillium simplicissimum, one of the canonical members of the VAO/PCMH flavoprotein family. After describing its discovery and initial biochemical characterization, we discuss the physiological role, substrate scope, and catalytic mechanism of VAO, and review its three-dimensional structure and mechanism of covalent flavinylation. We also explain how protein engineering provided a deeper insight into the role of certain amino acid residues in determining the substrate specificity and enantioselectivity of the enzyme. Finally, we summarize recent computational studies about the migration of substrates and products through the enzyme's structure and the phylogenetic distribution of VAO and related enzymes.

Language: en

Keywords

Alcohol Oxidoreductases; Catalytic mechanism; Covalent flavinylation; Crystal structure; Enantioselectivity; Enzyme dynamics; Flavoprotein family; Fungal Proteins; Lignin and phenols; Oxidase; Penicillium; Phylogenetics; Phylogeny; Protein Conformation; Protein Engineering; Substrate Specificity; Suicide inhibition