Abstract
The stereochemical course of the cyclisation reaction catalysed by the bacterial 1,8-cineol synthase from Streptomyces clavuligerus was investigated using stereospecifically deuterated substrates. In contrast to the well investigated plant enzyme from Salvia officinalis, the reaction proceeds via (S)-linalyl diphosphate and the (S)-terpinyl cation, while the final cyclisation reaction is in both cases a syn addition, as could be shown by incubation of (2-13C)geranyl diphosphate in deuterium oxide.
Highlights
Among all classes of natural products the climax of structural diversity and complexity is reached within the largest, the terpenoids
In contrast to the well investigated plant enzyme from Salvia officinalis, the reaction proceeds via (S)-linalyl diphosphate and the (S)-terpinyl cation, while the final cyclisation reaction is in both cases a syn addition, as could be shown by incubation of (2-13C)geranyl diphosphate in deuterium oxide
While the plant enzyme was shown to convert GPP via (R)-LPP ((R)-5) and the (R)-terpinyl cation ((R)-6) into 1 [27], the experiments described here revealed a different course for the bacterial enzyme via (S)-6
Summary
Among all classes of natural products the climax of structural diversity and complexity is reached within the largest, the terpenoids. The stereochemical course of the cyclisation reaction catalysed by the bacterial 1,8-cineol synthase from Streptomyces clavuligerus was investigated using stereospecifically deuterated substrates.
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