Vanillyl alcohol oxidase

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

doi:10.1016/bs.enz.2020.05.003

Vanillyl alcohol oxidase

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

^*Corresponding author for this work

Biotechnology

Research output: Chapter in Book/Report/Conference proceeding › Chapter › Academic › peer-review

26 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 language	English
Title of host publication	Flavin-Dependent Enzymes
Subtitle of host publication	Mechanisms, Structures and Applications
Editors	Pimchai Chaiyen, Fuyuhiko Tamanoi
Publisher	Elsevier
Chapter	4
Pages	87-116
Number of pages	30
Volume	47
ISBN (Print)	978-0-12-820137-4
DOIs	https://doi.org/10.1016/bs.enz.2020.05.003
Publication status	Published - 2020

Publication series

Name	The Enzymes
Publisher	Elsevier
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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title = "Vanillyl alcohol oxidase",

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.",

keywords = "Catalytic mechanism, Covalent flavinylation, Crystal structure, Enantioselectivity, Enzyme dynamics, Flavoprotein family, Lignin and phenols, Oxidase, Phylogenetics, Suicide inhibition",

author = "Ewing, {Tom A} and Gudrun Gygli and Fraaije, {Marco W} and {van Berkel}, {Willem J H}",

year = "2020",

doi = "10.1016/bs.enz.2020.05.003",

language = "English",

isbn = "978-0-12-820137-4",

volume = "47",

series = "The Enzymes",

publisher = "Elsevier",

pages = "87--116",

editor = "Pimchai Chaiyen and Fuyuhiko Tamanoi",

booktitle = "Flavin-Dependent Enzymes",

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TY - CHAP

T1 - Vanillyl alcohol oxidase

AU - Ewing, Tom A

AU - Gygli, Gudrun

AU - Fraaije, Marco W

AU - van Berkel, Willem J H

PY - 2020

Y1 - 2020

N2 - 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.

AB - 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.

KW - Catalytic mechanism

KW - Covalent flavinylation

KW - Crystal structure

KW - Enantioselectivity

KW - Enzyme dynamics

KW - Flavoprotein family

KW - Lignin and phenols

KW - Oxidase

KW - Phylogenetics

KW - Suicide inhibition

U2 - 10.1016/bs.enz.2020.05.003

DO - 10.1016/bs.enz.2020.05.003

M3 - Chapter

C2 - 32951836

SN - 978-0-12-820137-4

VL - 47

T3 - The Enzymes

SP - 87

EP - 116

BT - Flavin-Dependent Enzymes

A2 - Chaiyen, Pimchai

A2 - Tamanoi, Fuyuhiko

PB - Elsevier

ER -

Vanillyl alcohol oxidase

Abstract

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Keywords

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