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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Ober, Dietrich Hartmann, Thomas Naumann, Claudia |
| Description | Author Affiliation: Naumann C ( Institut für Pharmazeutische Biologie der Technischen Universität Braunschweig, Mendelssohnstrasse 1, D-38106 Braunschweig, Germany.); |
| Abstract | Larvae of Tyria jacobaeae feed solely upon the pyrrolizidine alkaloid-containing plant Senecio jacobaea. Ingested pyrrolizidine alkaloids (PAs), which are toxic to unspecialized insects and vertebrates, are efficiently N-oxidized in the hemolymph of T. jacobaeae by senecionine N-oxygenase (SNO), a flavin-dependent monooxygenase (FMO) with a high substrate specificity for PAs. Peptide microsequences obtained from purified T. jacobaeae SNO were used to clone the corresponding cDNA, which was expressed in active form in Escherichia coli. T. jacobaeae SNO possesses a signal peptide characteristic of extracellular proteins, and it belongs to a large family of mainly FMO-like sequences of mostly unknown function, including two predicted Drosophila melanogaster gene products. The data indicate that the gene for T. jacobaeae SNO, highly specific for toxic pyrrolizidine alkaloids, was recruited from a preexisting insect-specific FMO gene family of hitherto unknown function. The enzyme allows the larvae to feed on PA-containing plants and to accumulate predation-deterrent PAs in the hemolymph. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 9 |
| Volume Number | 99 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2002-05-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Evolution, Molecular Flavins Metabolism Mixed Function Oxygenases Chemistry Genetics Oxygenases Pyrrolizidine Alkaloids Amino Acid Sequence Animals Cloning, Molecular DNA, Complementary Escherichia Coli Hemolymph Enzymology Models, Chemical Molecular Sequence Data Moths Phylogeny Protein Sorting Signals Protein Structure, Tertiary Recombinant Proteins Sequence Homology, Amino Acid Substrate Specificity Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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