The VAO/PCMH flavoprotein family

Tom A. Ewing; Marco W. Fraaije; Andrea Mattevi; Willem J.H. van Berkel

doi:10.1016/j.abb.2017.06.022

The VAO/PCMH flavoprotein family

Tom A. Ewing, Marco W. Fraaije, Andrea Mattevi, Willem J.H. van Berkel^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

44 Citations (Scopus)

Abstract

The VAO/PCMH flavoprotein family consists of structurally homologous flavin-dependent enzymes that catalyze a wide range of chemical reactions. Family members share an architecture consisting of a conserved FAD-binding domain and a more variable substrate-binding domain, which enables varying interactions with a range of substrates while maintaining the same cofactor-binding fold. Here, we provide an overview of the current state of our knowledge on the members of the VAO/PCMH family. Based on a phylogenetic analysis, we divide the family into 11 subgroups. We discuss the properties of these subgroups, focusing on recent developments in terms of the discovery of new family members and mechanistic advances. We also highlight open questions that will provide challenges for future research.

Original language	English
Pages (from-to)	104-117
Journal	Archives of Biochemistry and Biophysics
Volume	632
Early online date	2017
DOIs	https://doi.org/10.1016/j.abb.2017.06.022
Publication status	Published - 15 Oct 2017

Keywords

Enzyme mechanism
Flavoprotein
Oxidoreductase
Phylogeny
Protein family

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10.1016/j.abb.2017.06.022

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title = "The VAO/PCMH flavoprotein family",

abstract = "The VAO/PCMH flavoprotein family consists of structurally homologous flavin-dependent enzymes that catalyze a wide range of chemical reactions. Family members share an architecture consisting of a conserved FAD-binding domain and a more variable substrate-binding domain, which enables varying interactions with a range of substrates while maintaining the same cofactor-binding fold. Here, we provide an overview of the current state of our knowledge on the members of the VAO/PCMH family. Based on a phylogenetic analysis, we divide the family into 11 subgroups. We discuss the properties of these subgroups, focusing on recent developments in terms of the discovery of new family members and mechanistic advances. We also highlight open questions that will provide challenges for future research.",

keywords = "Enzyme mechanism, Flavoprotein, Oxidoreductase, Phylogeny, Protein family",

author = "Ewing, {Tom A.} and Fraaije, {Marco W.} and Andrea Mattevi and {van Berkel}, {Willem J.H.}",

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T1 - The VAO/PCMH flavoprotein family

AU - Ewing, Tom A.

AU - Fraaije, Marco W.

AU - Mattevi, Andrea

AU - van Berkel, Willem J.H.

PY - 2017/10/15

Y1 - 2017/10/15

N2 - The VAO/PCMH flavoprotein family consists of structurally homologous flavin-dependent enzymes that catalyze a wide range of chemical reactions. Family members share an architecture consisting of a conserved FAD-binding domain and a more variable substrate-binding domain, which enables varying interactions with a range of substrates while maintaining the same cofactor-binding fold. Here, we provide an overview of the current state of our knowledge on the members of the VAO/PCMH family. Based on a phylogenetic analysis, we divide the family into 11 subgroups. We discuss the properties of these subgroups, focusing on recent developments in terms of the discovery of new family members and mechanistic advances. We also highlight open questions that will provide challenges for future research.

AB - The VAO/PCMH flavoprotein family consists of structurally homologous flavin-dependent enzymes that catalyze a wide range of chemical reactions. Family members share an architecture consisting of a conserved FAD-binding domain and a more variable substrate-binding domain, which enables varying interactions with a range of substrates while maintaining the same cofactor-binding fold. Here, we provide an overview of the current state of our knowledge on the members of the VAO/PCMH family. Based on a phylogenetic analysis, we divide the family into 11 subgroups. We discuss the properties of these subgroups, focusing on recent developments in terms of the discovery of new family members and mechanistic advances. We also highlight open questions that will provide challenges for future research.

KW - Enzyme mechanism

KW - Flavoprotein

KW - Oxidoreductase

KW - Phylogeny

KW - Protein family

U2 - 10.1016/j.abb.2017.06.022

DO - 10.1016/j.abb.2017.06.022

M3 - Article

AN - SCOPUS:85023623183

SN - 0003-9861

VL - 632

SP - 104

EP - 117

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

ER -

The VAO/PCMH flavoprotein family

Abstract

Keywords

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