Abstract
The class II diterpene cyclase (DTC) from pleuromutilin biosynthesis uniquely mediates 'A' ring contraction of the initially formed decalin bicycle, yielding mutildienyl diphosphate (MPP). Catalysis requires a divalent metal cation co-factor. Intriguingly, selectively with magnesium, this DTC catalyzes ring expansion/contraction between MPP and halimadienyl diphosphate, providing some catalytic insight.
Highlights
The class II diterpene cyclase (DTC) from pleuromutilin biosynthesis uniquely mediates ‘A’ ring contraction of the initially formed decalin bicycle, yielding mutildienyl diphosphate (MPP)
As identified by comparison to an authentic standard,[7] isotuberculosinol/nosyberkol (5) was observed (Fig. S2†). This is derived from addition of water to the tertiary carbocation formed by lysis of the allylic diphosphate ester bond in 3, consistent with the known class I activity of Clitopilus passeckeranis (CpPS)
3 is not a precursor to 4 and, CpPS:D649L does not seem to produce 3 directly from 1. This suggests that the CpPS DTC active site seems be able to produce 3 from its usual product 2, albeit this ring expansion reaction is clearly much less efficient than that catalysed by its class I active site
Summary
Magnesium-specific ring expansion/contraction catalysed by the class II diterpene cyclase from pleuromutilin biosynthesis† The class II diterpene cyclase (DTC) from pleuromutilin biosynthesis uniquely mediates ‘A’ ring contraction of the initially formed decalin bicycle, yielding mutildienyl diphosphate (MPP). Selectively with magnesium, this DTC catalyzes ring expansion/contraction between MPP and halimadienyl diphosphate, providing some catalytic insight.
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