Selectivity of enzymes involved in the formation of opposite enantiomeric series of p-menthane monoterpenoids in peppermint and Japanese catnip
| Autor: | B. Markus Lange, Iris Lange, Jana K. Richter, Matthias Wüst, Narayanan Srividya |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
chemistry.chemical_classification
Limonene Lamiaceae biology Molecular Structure Stereochemistry Enantioselective synthesis Mentha piperita Stereoisomerism Plant Science General Medicine Reductase Menthone Cofactor Mixed Function Oxygenases chemistry.chemical_compound Enzyme Isopiperitenol dehydrogenase chemistry Genetics biology.protein Monoterpenes Enantiomer Oxidoreductases Agronomy and Crop Science |
| Zdroj: | Plant science : an international journal of experimental plant biology. 314 |
| ISSN: | 1873-2259 |
| Popis: | Peppermint (Mentha x piperita L.) and Japanese catnip (Schizonepeta tenuifolia (Benth.) Briq.) accumulate p-menthane monoterpenoids with identical functionalization patterns but opposite stereochemistry. In the present study, we investigate the enantioselectivity of multiple enzymes involved in monoterpenoid biosynthesis in these species. Based on kinetic assays, mint limonene synthase, limonene 3-hydroxylase, isopiperitenol dehydrogenase, isopiperitenone reductase, and menthone reductase exhibited significant enantioselectivity toward intermediates of the pathway that proceeds through (-)-4S-limonene. Limonene synthase, isopiperitenol dehydrogenase and isopiperitenone reductase of Japanese catnip preferred intermediates of the pathway that involves (+)-4R-limonene, whereas limonene 3-hydroxylase was not enantioselective, and the activities of pulegone reductase and menthone reductase were too low to acquire meaningful kinetic data. Molecular modeling studies with docked ligands generally supported the experimental data obtained with peppermint enzymes, indicating that the preferred enantiomer was aligned well with the requisite cofactor and amino acid residues implicated in catalysis. A striking example for enantioselectivity was peppermint (-)-menthone reductase, which binds (-)-menthone with exquisite affinity but was predicted to bind (+)-menthone in a non-productive orientation that positions its carbonyl functional group at considerable distance to the NADPH cofactor. The work presented here lays the groundwork for structure-function studies aimed at unraveling how enantioselectivity evolved in closely related species of the Lamiaceae and beyond. |
| Databáze: | OpenAIRE |
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