| Content Provider |
World Health Organization (WHO)-Global Index Medicus |
| Author |
Steiner, Barbara Gutmann, Alexander Gruber, Karl Pavkov-keller, Tea Daniel, Bastian Van Der Graaff, Eric Dordic, Andela Sensen, Christoph W. Macheroux, Peter Nidetzky, Bernd Wallner, Silvia |
| Description |
Author Affiliation: Daniel B ( From the Institutes of Biochemistry.); Pavkov-Keller T ( the Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria, the ACIB GmbH, 8010 Graz, Austria, and.); Steiner B ( From the Institutes of Biochemistry.); Dordic A ( the Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria, the ACIB GmbH, 8010 Graz, Austria, and.); Gutmann A ( Biotechnology and Biochemical Engineering, and.); Nidetzky B ( Biotechnology and Biochemical Engineering, and.); Sensen CW ( Molecular Biotechnology, Graz University of Technology, 8010 Graz, Austria.); van der Graaff E ( the Section for Crop Sciences, Copenhagen University, 2630 Copenhagen, Denmark.); Wallner S ( From the Institutes of Biochemistry.); Gruber K ( the Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria.); Macheroux P ( From the Institutes of Biochemistry, peter.macheroux@tugraz.at.) |
| 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. |
| ISSN |
00219258 |
| e-ISSN |
1083351X |
| Journal |
Journal of Biological Chemistry |
| Issue Number |
30 |
| Volume Number |
290 |
| Language |
English |
| Publisher |
American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date |
2015-07-24 |
| Publisher Place |
United States |
| Access Restriction |
Open |
| Subject Keyword |
Arabidopsis Proteins Chemistry Cell Wall Enzymology Lignin Metabolism Oxidoreductases, N-Demethylating Amino Acid Sequence Arabidopsis Genetics Catalysis Catalytic Domain Crystallography, X-Ray Kinetics Oxidation-Reduction Protein Structure, Tertiary Substrate Specificity Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type |
Text |
| Resource Type |
Article |
| Subject |
Cell Biology Biochemistry Molecular Biology |
