Die Famiele der berberine bridge enzyme-ähnlichen Proteine aus Arabidopsis thaliana: The family of berberine bridge enzyme-like proteins from Arabidopsis thaliana

Bastian Daniel, Peter Macheroux, Silvia Wallner, Barbara Steiner, Karl Gruber, Tea Pavkov-Keller

Publikation: Konferenzbeitrag(Altdaten) Vortrag oder PräsentationForschungBegutachtung

Abstract

Flavoproteins are a diverse protein class employing an isoalloxazine ring for catalysis in form of the flavin mononucleotide (FMN) or the flavin adenine dinucleotide (FAD). Among them, there is the berberine bridge enzyme-like (BBE-like) protein family (pfam 08031) that was named after the berberine bridge enzyme (EcBBE) from California poppy (Eschscholzia californica). BBE-like proteins form a multigene family in plants and the number of members varies from one in the moss Physcomitrella patens to 57 in the Western Balsam Poplar (Populus trichocarpa). Despite of the frequent occurrence of these proteins their function is largely unknown. Therefore, we chose to investigate the BBE-like proteins occurring in Arabidopsis thalina to broaden our understanding of this protein family. The genome of A. thaliana harbours 28 genes for BBE-like proteins that can be divided into seven phylogenetic groups. Presented are the structural and biochemical characterization of AtBBE-like protein 15 and AtBBE-like protein 28. There are four frequently occurring active site types from AtBBE-like proteins. AtBBE-like 15 is a representative of the most abundant type, which occurs predominantly in dicots. The type found in AtBBE-like 28 is restricted to the plant family Brassicaceae. Additionally, the potential of AtBBE-like protein 15 as biocatalyst was elucidated. This enzyme was identified as a monolignol dehydrogenase, i.e. the enzyme inhibits the reaction between the reduced flavin and oxygen. The enzyme was rationally engineered towards higher oxygen reactivity and the potential of the enzyme as biocatalyst for oxidative reactions was tested. The pH- and temperature optimum (pH 7, 50°C) was determined. The enzyme shows enhanced activity in the presence of various organic solvents and accepts various allylic and benzylic alcohols as substrates. Secondary allylic alcohols were converted with good to excellent enantioselectivity (E>34 to E>200).
Titel in ÜbersetzungDie Famiele der berberine bridge enzyme-ähnlichen Proteine aus Arabidopsis thaliana
Originalspracheenglisch
PublikationsstatusVeröffentlicht - 5 Jul 2016
VeranstaltungOxiZymes2016 - Hof van Wageningen, Wageningen, Niederlande
Dauer: 3 Jul 20166 Jul 2016

Konferenz

KonferenzOxiZymes2016
LandNiederlande
OrtWageningen
Zeitraum3/07/166/07/16

Dies zitieren

The family of berberine bridge enzyme-like proteins from Arabidopsis thaliana : The family of berberine bridge enzyme-like proteins from Arabidopsis thaliana. / Daniel, Bastian; Macheroux, Peter; Wallner, Silvia; Steiner, Barbara; Gruber, Karl; Pavkov-Keller, Tea.

2016. OxiZymes2016, Wageningen, Niederlande.

Publikation: Konferenzbeitrag(Altdaten) Vortrag oder PräsentationForschungBegutachtung

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abstract = "Flavoproteins are a diverse protein class employing an isoalloxazine ring for catalysis in form of the flavin mononucleotide (FMN) or the flavin adenine dinucleotide (FAD). Among them, there is the berberine bridge enzyme-like (BBE-like) protein family (pfam 08031) that was named after the berberine bridge enzyme (EcBBE) from California poppy (Eschscholzia californica). BBE-like proteins form a multigene family in plants and the number of members varies from one in the moss Physcomitrella patens to 57 in the Western Balsam Poplar (Populus trichocarpa). Despite of the frequent occurrence of these proteins their function is largely unknown. Therefore, we chose to investigate the BBE-like proteins occurring in Arabidopsis thalina to broaden our understanding of this protein family. The genome of A. thaliana harbours 28 genes for BBE-like proteins that can be divided into seven phylogenetic groups. Presented are the structural and biochemical characterization of AtBBE-like protein 15 and AtBBE-like protein 28. There are four frequently occurring active site types from AtBBE-like proteins. AtBBE-like 15 is a representative of the most abundant type, which occurs predominantly in dicots. The type found in AtBBE-like 28 is restricted to the plant family Brassicaceae. Additionally, the potential of AtBBE-like protein 15 as biocatalyst was elucidated. This enzyme was identified as a monolignol dehydrogenase, i.e. the enzyme inhibits the reaction between the reduced flavin and oxygen. The enzyme was rationally engineered towards higher oxygen reactivity and the potential of the enzyme as biocatalyst for oxidative reactions was tested. The pH- and temperature optimum (pH 7, 50°C) was determined. The enzyme shows enhanced activity in the presence of various organic solvents and accepts various allylic and benzylic alcohols as substrates. Secondary allylic alcohols were converted with good to excellent enantioselectivity (E>34 to E>200).",
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T2 - The family of berberine bridge enzyme-like proteins from Arabidopsis thaliana

AU - Daniel, Bastian

AU - Macheroux, Peter

AU - Wallner, Silvia

AU - Steiner, Barbara

AU - Gruber, Karl

AU - Pavkov-Keller, Tea

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N2 - Flavoproteins are a diverse protein class employing an isoalloxazine ring for catalysis in form of the flavin mononucleotide (FMN) or the flavin adenine dinucleotide (FAD). Among them, there is the berberine bridge enzyme-like (BBE-like) protein family (pfam 08031) that was named after the berberine bridge enzyme (EcBBE) from California poppy (Eschscholzia californica). BBE-like proteins form a multigene family in plants and the number of members varies from one in the moss Physcomitrella patens to 57 in the Western Balsam Poplar (Populus trichocarpa). Despite of the frequent occurrence of these proteins their function is largely unknown. Therefore, we chose to investigate the BBE-like proteins occurring in Arabidopsis thalina to broaden our understanding of this protein family. The genome of A. thaliana harbours 28 genes for BBE-like proteins that can be divided into seven phylogenetic groups. Presented are the structural and biochemical characterization of AtBBE-like protein 15 and AtBBE-like protein 28. There are four frequently occurring active site types from AtBBE-like proteins. AtBBE-like 15 is a representative of the most abundant type, which occurs predominantly in dicots. The type found in AtBBE-like 28 is restricted to the plant family Brassicaceae. Additionally, the potential of AtBBE-like protein 15 as biocatalyst was elucidated. This enzyme was identified as a monolignol dehydrogenase, i.e. the enzyme inhibits the reaction between the reduced flavin and oxygen. The enzyme was rationally engineered towards higher oxygen reactivity and the potential of the enzyme as biocatalyst for oxidative reactions was tested. The pH- and temperature optimum (pH 7, 50°C) was determined. The enzyme shows enhanced activity in the presence of various organic solvents and accepts various allylic and benzylic alcohols as substrates. Secondary allylic alcohols were converted with good to excellent enantioselectivity (E>34 to E>200).

AB - Flavoproteins are a diverse protein class employing an isoalloxazine ring for catalysis in form of the flavin mononucleotide (FMN) or the flavin adenine dinucleotide (FAD). Among them, there is the berberine bridge enzyme-like (BBE-like) protein family (pfam 08031) that was named after the berberine bridge enzyme (EcBBE) from California poppy (Eschscholzia californica). BBE-like proteins form a multigene family in plants and the number of members varies from one in the moss Physcomitrella patens to 57 in the Western Balsam Poplar (Populus trichocarpa). Despite of the frequent occurrence of these proteins their function is largely unknown. Therefore, we chose to investigate the BBE-like proteins occurring in Arabidopsis thalina to broaden our understanding of this protein family. The genome of A. thaliana harbours 28 genes for BBE-like proteins that can be divided into seven phylogenetic groups. Presented are the structural and biochemical characterization of AtBBE-like protein 15 and AtBBE-like protein 28. There are four frequently occurring active site types from AtBBE-like proteins. AtBBE-like 15 is a representative of the most abundant type, which occurs predominantly in dicots. The type found in AtBBE-like 28 is restricted to the plant family Brassicaceae. Additionally, the potential of AtBBE-like protein 15 as biocatalyst was elucidated. This enzyme was identified as a monolignol dehydrogenase, i.e. the enzyme inhibits the reaction between the reduced flavin and oxygen. The enzyme was rationally engineered towards higher oxygen reactivity and the potential of the enzyme as biocatalyst for oxidative reactions was tested. The pH- and temperature optimum (pH 7, 50°C) was determined. The enzyme shows enhanced activity in the presence of various organic solvents and accepts various allylic and benzylic alcohols as substrates. Secondary allylic alcohols were converted with good to excellent enantioselectivity (E>34 to E>200).

M3 - (Old data) Lecture or Presentation

ER -