ArticleThe Journal of biological chemistry2015
Oxidation of Monolignols by Members of the Berberine Bridge Enzyme Family Suggests a Role in Plant Cell Wall Metabolism.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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52 citing papers in PubMed, 116 citations in OpenAlex.
- Functional characterization of the grape VvCAD15-like gene in enhancing cold tolerance via regulation of lignin biosynthesis.Plant cell reports · 2026Article
- Genome-Wide Identification and Functional Verification of CoreInternational journal of molecular sciences · 2026Article
- Ethylene signalling enhances mitochondrial stress tolerance independently of the transcription factor ANAC017 in Arabidopsis.Journal of experimental botany · 2026Article
- Aspartic acid residues in BBE-like enzymes fromProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Berberine bridge enzyme-like oxidases orchestrate homeostasis and signaling of oligogalacturonides in defense and upon mechanical damage.The Plant journal : for cell and molecular biology · 2025Article
- Interactive 3D Objects Enhance Scientific Communication of Structural Data.Chembiochem : a European journal of chemical biology · 2025Review
- Effects of Chlortetracycline on Lignin Biosynthesis inInternational journal of molecular sciences · 2025Article
- Exocyst subunits EXO70B1 and B2 contribute to stomatal dynamics and cell wall modifications.Frontiers in plant science · 2025Article
- Morphological and genetic characterization of the muscadine fruit abscission zone.Horticulture research · 2024Article
- Extracellular vesicles of Norway spruce contain precursors and enzymes for lignin formation and salicylic acid.Plant physiology · 2024Article
- Biosynthetic Strategies of Berberine Bridge Enzyme-like Flavoprotein Oxidases toward Structural Diversification in Natural Product Biosynthesis.Biochemistry · 2024Review
- The evolutionary origin of naturally occurring intermolecular Diels-Alderases from Morus alba.Nature communications · 2024Article
- Cacao pod transcriptome profiling of seven genotypes identifies features associated with post-penetration resistance to Phytophthora palmivora.Scientific reports · 2024Article
- Exploring the Biologically Active Metabolites Produced byMetabolites · 2023Article
- Radical cation scavenging activity of berberine bridge enzyme-like oligosaccharide oxidases acting on short cell wall fragments.Scientific reports · 2023Article
- Analysis of the apoplast fluid proteome during the induction of systemic acquired resistance inPeerJ · 2023Article
- GhTCE1-GhTCEE1 dimers regulate transcriptional reprogramming during wound-induced callus formation in cotton.The Plant cell · 2022Article
- Molecular and Physiological Responses ofInternational journal of molecular sciences · 2022Article
- A Berberine Bridge Enzyme-Like Protein,Frontiers in plant science · 2022Article
- Low temperature modifies seedling leaf anatomy and gene expression inFrontiers in plant science · 2022Article
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plant genomes contain a large number of genes encoding for berberine bridge enzyme (BBE)-like enzymes. Despite the widespread occurrence and abundance of this protein family in the plant kingdom, the biochemical function remains largely unexplored. In this study, we have expressed two members of the BBE-like enzyme family from Arabidopsis thaliana in the host organism Komagataella pastoris. The two proteins, termed AtBBE-like 13 and AtBBE-like 15, were purified, and their catalytic properties were determined. In addition, AtBBE-like 15 was crystallized and structurally characterized by x-ray crystallography. Here, we show that the enzymes catalyze the oxidation of aromatic allylic alcohols, such as coumaryl, sinapyl, and coniferyl alcohol, to the corresponding aldehydes and that AtBBE-like 15 adopts the same fold as vanillyl alcohol oxidase as reported previously for berberine bridge enzyme and other FAD-dependent oxidoreductases. Further analysis of the substrate range identified coniferin, the glycosylated storage form of coniferyl alcohol, as a substrate of the enzymes, whereas other glycosylated monolignols were rather poor substrates. A detailed analysis of the motifs present in the active sites of the BBE-like enzymes in A. thaliana suggested that 14 out of 28 members of the family might catalyze similar reactions. Based on these findings, we propose a novel role of BBE-like enzymes in monolignol metabolism that was previously not recognized for this enzyme family.
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