+ Site Statistics
+ Search Articles
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ PDF Full Text
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Translate
+ Recently Requested

Oxidation of Monolignols by Members of the Berberine Bridge Enzyme Family Suggests a Role in Plant Cell Wall Metabolism

Oxidation of Monolignols by Members of the Berberine Bridge Enzyme Family Suggests a Role in Plant Cell Wall Metabolism

Journal of Biological Chemistry 290(30): 18770-18781

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.

(PDF emailed within 0-6 h: $19.90)

Accession: 058488249

Download citation: RISBibTeXText

PMID: 26037923

DOI: 10.1074/jbc.M115.659631

Related references

Structure of a Berberine Bridge Enzyme-Like Enzyme with an Active Site Specific to the Plant Family Brassicaceae. Plos One 11(6): E0156892-E0156892, 2016

Studies to the role of a tericuline converting enzyme (berberine bridge enzyme) in the benzylisoquinoline metabolism of plants. 1975

Studies on the role of a reticulin converting enzyme berberine bridge enzyme in the benzyl iso quinoline metabolism of plants. Biochemie Und Physiologie Der Pflanzen (bpp)-4): 69-77, 1975

Heterologous expression of the plant proteins strictosidine synthase and berberine bridge enzyme in insect cell culture. Phytochemistry (Oxford) 35(2): 353-360, 1994

Berberine bridge enzyme catalyzes the six electron oxidation of (S)-reticuline to dehydroscoulerine. Phytochemistry 70(9): 1092-1097, 2009

Role of NaOH-extractable cell wall proteins Ccw5p, Ccw6p, Ccw7p and Ccw8p (members of the Pir protein family) in stability of the Saccharomyces cerevisiae cell wall. Yeast 15(10a): 813-820, 1999

Visualization of plant cell wall lignification using fluorescence-tagged monolignols. Plant Journal 76(3): 357-366, 2014

The family of berberine bridge enzyme-like enzymes: A treasure-trove of oxidative reactions. Archives of Biochemistry and Biophysics 632: 88-103, 2017

Biochemical evidence that berberine bridge enzyme belongs to a novel family of flavoproteins containing a bi-covalently attached FAD cofactor. Journal of Biological Chemistry 281(30): 21276-21285, 2006

Catalytic and structural role of a conserved active site histidine in berberine bridge enzyme. Biochemistry 51(31): 6139-6147, 2012

Transgenic and mutation-based suppression of a berberine bridge enzyme-like (BBL) gene family reduces alkaloid content in field-grown tobacco. Plos One 10(2): E0117273-E0117273, 2016

Purification and characterization of the berberine bridge enzyme from berberis beaniana cell cultures. Phytochemistry (Oxford) 24(11): 2577-2584, 1985

Structural and mechanistic studies reveal the functional role of bicovalent flavinylation in berberine bridge enzyme. Journal of Biological Chemistry 284(30): 19993-20001, 2009

An Arabidopsis berberine-bridge enzyme-like protein specifically oxidizes cellulose oligomers and plays a role in immunity. Plant Journal 2019, 2019

RNA-Seq analysis of global transcriptomic changes suggests a role for the MAPK pathway and carbon metabolism in cell wall maintenance in a Saccharomyces cerevisiae FKS1 mutant. Biochemical and Biophysical Research Communications: -, 2018