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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Ehlting, Jürgen Carrington, Yuriko Alber, Annette Guo, Jia |
| Description | Author Affiliation: Guo J ( From the Department of Biology and Centre for Forest Biology, University of Victoria, Victoria, British Columbia V8W 2Y2, Canada.); Carrington Y ( From the Department of Biology and Centre for Forest Biology, University of Victoria, Victoria, British Columbia V8W 2Y2, Canada.); Alber A ( From the Department of Biology and Centre for Forest Biology, University of Victoria, Victoria, British Columbia V8W 2Y2, Canada.); Ehlting J ( From the Department of Biology and Centre for Forest Biology, University of Victoria, Victoria, British Columbia V8W 2Y2, Canada je@uvic.ca.) |
| Abstract | The shikimate pathway leads to the biosynthesis of aromatic amino acids essential for protein biosynthesis and the production of a wide array of plant secondary metabolites. Among them, quinate is an astringent feeding deterrent that can be formed in a single step reaction from 3-dehydroquinate catalyzed by quinate dehydrogenase (QDH). 3-Dehydroquinate is also the substrate for shikimate biosynthesis through the sequential actions of dehydroquinate dehydratase (DQD) and shikimate dehydrogenase (SDH) contained in a single protein in plants. The reaction mechanism of QDH resembles that of SDH. The poplar genome encodes five DQD/SDH-like genes (Poptr1 to Poptr5), which have diverged into two distinct groups based on sequence analysis and protein structure prediction. In vitro biochemical assays proved that Poptr1 and -5 are true DQD/SDHs, whereas Poptr2 and -3 instead have QDH activity with only residual DQD/SDH activity. Poplar DQD/SDHs have distinct expression profiles suggesting separate roles in protein and lignin biosynthesis. Also, the QDH genes are differentially expressed. In summary, quinate (secondary metabolism) and shikimate (primary metabolism) metabolic activities are encoded by distinct members of the same gene family, each having different physiological functions. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 34 |
| Volume Number | 289 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2014-08-22 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Populus Metabolism Quinic Acid Shikimic Acid Alcohol Oxidoreductases Chemistry Amino Acid Sequence Cloning, Molecular DNA Primers Gene Expression Profiling Genes, Plant Molecular Sequence Data Polymerase Chain Reaction Genetics Sequence Homology, Amino Acid Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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