The family of berberine bridge enzyme-like enzymes: A treasure-trove of oxidative reactions: A treasure-trove of oxidative reactions

Bastian Daniel, Barbara Konrad, Marina Toplak, Majd Lahham, Julia Messenlehner, Andreas Winkler, Peter Macheroux

Publikation: Beitrag in einer FachzeitschriftReview eines Fachbereichs (Review article)ForschungBegutachtung

Abstract

Biological oxidations form the basis of life on earth by utilizing organic compounds as electron donors to drive the generation of metabolic energy carriers, such as ATP. Oxidative reactions are also important for the biosynthesis of complex compounds, i.e. natural products such as alkaloids that provide vital benefits for organisms in all kingdoms of life. The vitamin B2-derived cofactors flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) enable an astonishingly diverse array of oxidative reactions that is based on the versatility of the redox-active isoalloxazine ring. The family of FAD-linked oxidases can be divided into subgroups depending on specific sequence features in an otherwise very similar structural context. The sub-family of berberine bridge enzyme (BBE)-like enzymes has recently attracted a lot of attention due to the challenging chemistry catalyzed by its members and the unique and unusual bi-covalent attachment of the FAD cofactor. This family is the focus of the present review highlighting recent advancements into the structural and functional aspects of members from bacteria, fungi and plants. In view of the unprecedented reaction catalyzed by the family's namesake, BBE from the California poppy, recent studies have provided further insights into nature's treasure chest of oxidative reactions.

Originalspracheenglisch
Seiten (von - bis)88-103
Seitenumfang16
FachzeitschriftArchives of Biochemistry and Biophysics
Jahrgang632
DOIs
PublikationsstatusVeröffentlicht - 15 Okt 2017

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Flavin-Adenine Dinucleotide
Eschscholzia
Enzymes
Flavin Mononucleotide
Riboflavin
Biosynthesis
Biological Products
Fungi
Organic compounds
Alkaloids
Oxidation-Reduction
Bacteria
Oxidoreductases
Thorax
Adenosine Triphosphate
Earth (planet)
Electrons
Oxidation
reticuline oxidase

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    The family of berberine bridge enzyme-like enzymes: A treasure-trove of oxidative reactions : A treasure-trove of oxidative reactions. / Daniel, Bastian; Konrad, Barbara; Toplak, Marina; Lahham, Majd; Messenlehner, Julia; Winkler, Andreas; Macheroux, Peter.

    in: Archives of Biochemistry and Biophysics, Jahrgang 632, 15.10.2017, S. 88-103.

    Publikation: Beitrag in einer FachzeitschriftReview eines Fachbereichs (Review article)ForschungBegutachtung

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    abstract = "Biological oxidations form the basis of life on earth by utilizing organic compounds as electron donors to drive the generation of metabolic energy carriers, such as ATP. Oxidative reactions are also important for the biosynthesis of complex compounds, i.e. natural products such as alkaloids that provide vital benefits for organisms in all kingdoms of life. The vitamin B2-derived cofactors flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) enable an astonishingly diverse array of oxidative reactions that is based on the versatility of the redox-active isoalloxazine ring. The family of FAD-linked oxidases can be divided into subgroups depending on specific sequence features in an otherwise very similar structural context. The sub-family of berberine bridge enzyme (BBE)-like enzymes has recently attracted a lot of attention due to the challenging chemistry catalyzed by its members and the unique and unusual bi-covalent attachment of the FAD cofactor. This family is the focus of the present review highlighting recent advancements into the structural and functional aspects of members from bacteria, fungi and plants. In view of the unprecedented reaction catalyzed by the family's namesake, BBE from the California poppy, recent studies have provided further insights into nature's treasure chest of oxidative reactions.",
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    T2 - A treasure-trove of oxidative reactions

    AU - Daniel, Bastian

    AU - Konrad, Barbara

    AU - Toplak, Marina

    AU - Lahham, Majd

    AU - Messenlehner, Julia

    AU - Winkler, Andreas

    AU - Macheroux, Peter

    N1 - Copyright © 2017 The Authors. Published by Elsevier Inc. All rights reserved.

    PY - 2017/10/15

    Y1 - 2017/10/15

    N2 - Biological oxidations form the basis of life on earth by utilizing organic compounds as electron donors to drive the generation of metabolic energy carriers, such as ATP. Oxidative reactions are also important for the biosynthesis of complex compounds, i.e. natural products such as alkaloids that provide vital benefits for organisms in all kingdoms of life. The vitamin B2-derived cofactors flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) enable an astonishingly diverse array of oxidative reactions that is based on the versatility of the redox-active isoalloxazine ring. The family of FAD-linked oxidases can be divided into subgroups depending on specific sequence features in an otherwise very similar structural context. The sub-family of berberine bridge enzyme (BBE)-like enzymes has recently attracted a lot of attention due to the challenging chemistry catalyzed by its members and the unique and unusual bi-covalent attachment of the FAD cofactor. This family is the focus of the present review highlighting recent advancements into the structural and functional aspects of members from bacteria, fungi and plants. In view of the unprecedented reaction catalyzed by the family's namesake, BBE from the California poppy, recent studies have provided further insights into nature's treasure chest of oxidative reactions.

    AB - Biological oxidations form the basis of life on earth by utilizing organic compounds as electron donors to drive the generation of metabolic energy carriers, such as ATP. Oxidative reactions are also important for the biosynthesis of complex compounds, i.e. natural products such as alkaloids that provide vital benefits for organisms in all kingdoms of life. The vitamin B2-derived cofactors flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) enable an astonishingly diverse array of oxidative reactions that is based on the versatility of the redox-active isoalloxazine ring. The family of FAD-linked oxidases can be divided into subgroups depending on specific sequence features in an otherwise very similar structural context. The sub-family of berberine bridge enzyme (BBE)-like enzymes has recently attracted a lot of attention due to the challenging chemistry catalyzed by its members and the unique and unusual bi-covalent attachment of the FAD cofactor. This family is the focus of the present review highlighting recent advancements into the structural and functional aspects of members from bacteria, fungi and plants. In view of the unprecedented reaction catalyzed by the family's namesake, BBE from the California poppy, recent studies have provided further insights into nature's treasure chest of oxidative reactions.

    KW - Berberine

    KW - Eschscholzia

    KW - Flavin Mononucleotide

    KW - Flavin-Adenine Dinucleotide

    KW - Oxidation-Reduction

    KW - Oxidoreductases

    KW - Plant Proteins

    KW - Journal Article

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