Vanillyl alcohol oxidase

Tom A Ewing, Gudrun Gygli, Marco W Fraaije, Willem J H van Berkel*

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapterAcademicpeer-review

9 Citations (Scopus)

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.

Original languageEnglish
Title of host publicationFlavin-Dependent Enzymes
Subtitle of host publicationMechanisms, Structures and Applications
EditorsPimchai Chaiyen, Fuyuhiko Tamanoi
PublisherElsevier
Chapter4
Pages87-116
Number of pages30
Volume47
ISBN (Print)978-0-12-820137-4
DOIs
Publication statusPublished - 2020

Publication series

NameThe Enzymes
PublisherElsevier
ISSN (Print)0423-2607

Keywords

  • Catalytic mechanism
  • Covalent flavinylation
  • Crystal structure
  • Enantioselectivity
  • Enzyme dynamics
  • Flavoprotein family
  • Lignin and phenols
  • Oxidase
  • Phylogenetics
  • Suicide inhibition

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