Larvae of horseradish leaf beetle Phaedon cochleariae
Photo: Sindy Frick / MPI for Chemical Ecology
Max Planck scientists in Jena, Germany, have discovered an unusual regulation of enzymes that catalyze chain elongation in an important secondary metabolism, the terpenoid pathway.
In the horseradish leaf beetle Phaedon cochleariae a single enzyme can trigger the production of two completely different substances depending on whether it is regulated by cobalt, manganese or magnesium ions: iridoids, which are defensive substances the larvae use to repel predators, or juvenile hormones, which control insect’s development. Insects unlike plants do not have a large arsenal of the proteins called isoprenyl diphosphate synthases.
Experiments with larvae in which the enzyme encoding gene was silenced showed that the protein was involved in the formation of the C10 monoterpene chrysomelidial that larvae produce to defend themselves against predators. The larvae accumulate this monoterpene in special glands and release it as a defensive secretion when they are attacked by their enemies, such as ants.
However, surprising results emerged after comprehensive biochemical characterization of the enzyme. “After we had conducted an in vitro analysis of the protein, including measurements of product formation in the presence of different metal ions as co-factors, we were surprised to discover that only geranyl diphosphate (C10), a precursor for the defensive substance chrysomelidial, was produced after addition of cobalt and manganese ions. On the other hand, adding magnesium ions resulted in the formation of farnesyl diphosphate (C15), a potential precursor for juvenile hormones, which is 5 carbon atoms longer,” says the scientist. All three metals were found in larval tissue, leading to the assumption that enzyme catalysis is directed by the different metal co-factors in the larvae, whichever is predominant in amount: Towards toxin or hormone − physiologically a major difference.
Sequence comparisons cannot replace a thorough biochemical analysis
How the different metal ions modify the product range of the enzyme is still unclear. It is very likely that the varying atomic radii of the metal ions involved in the catalysis effect changes in the spatial structure of the enzyme, which prevent or allow the admission of a third C5 unit and hence result in the production of C10 or C15 molecules.“Our experiments provide two important findings,” says Wilhelm Boland, director at the Max Planck Institute. “First, the directing influence of metal ions on the product formation of isoprenyl diphosphate synthases is a novel “control element” in the regulation of the terpene metabolism which should be included in future experimental settings. And secondly: The diversity of terpenoid molecules cannot be attributed solely to the broad substrate specificity of some enzymes in the last steps of the metabolic pathway, but is in fact already inherent in early biosynthetic steps.” Nature continues to provide interesting answers to the question how organisms manage to produce tens of thousands of different secondary metabolites. [JWK/AO]
Dr. Jan-Wolfhard Kellmann | Max-Planck-Institut
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