Vanillyl alcohol oxidase

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

*Bijbehorende auteur voor dit werk

OnderzoeksoutputAcademicpeer review

9 Citaten (Scopus)

Samenvatting

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.

Originele taal-2English
TitelFlavin-Dependent Enzymes
SubtitelMechanisms, Structures and Applications
RedacteurenPimchai Chaiyen, Fuyuhiko Tamanoi
UitgeverijElsevier
Hoofdstuk4
Pagina's87-116
Aantal pagina's30
Volume47
ISBN van geprinte versie978-0-12-820137-4
DOI's
StatusPublished - 2020

Publicatie series

NaamThe Enzymes
UitgeverijElsevier
ISSN van geprinte versie0423-2607

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