ausblenden:
Schlagwörter:
MONOTERPENOID INDOLE ALKALOIDS; CELL-SUSPENSION CULTURES;
ALCOHOL-DEHYDROGENASE; BIOMIMETIC SYNTHESIS; STRICTOSIDINE GLUCOSIDASE;
HETEROYOHIMBINE ALKALOIDS; OPIUM POPPY; BIOSYNTHESIS; KEY;
4,21-DEHYDROGEISSOSCHIZINEBiochemistry & Molecular Biology;
Zusammenfassung:
The extraordinary chemical diversity of the plant-derived monoterpene indole alkaloids, which include vinblastine, quinine, and strychnine, originates from a single biosynthetic intermediate, strictosidine aglycone. Here we report for the first time the cloning of a biosynthetic gene and characterization of the corresponding enzyme that acts at this crucial branchpoint. This enzyme, an alcohol dehydrogenase homolog, converts strictosidine aglycone to the heteroyohimbine-type alkaloid tetrahydroalstonine. We also demonstrate how this enzyme, which uses a highly reactive substrate, may interact with the upstream enzyme of the pathway.
