期刊
CHEMBIOCHEM
卷 15, 期 2, 页码 213-216出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201300708
关键词
biosynthesis; crystal structures; enzyme mechanisms; hedycaryol synthases; terpenes; X-ray diffraction
资金
- Deutsche Forschungsgemeinschaft through an Emmy Noether grant [DI1536/1-3]
- Deutsche Forschungsgemeinschaft through Heisenberg grant [DI1536/4-1]
- grant Duftstoffe aus Actinomyceten [DI1536/2-1]
- Beilstein Institut zur Forderung der Chemischen Wissenschaften with a scholarship
- Stefan Schulz (Braunschweig)
- [GRK1721]
The biosynthesis of terpenes is catalysed by class I and II terpene cyclases. Here we present structural data from a class I hedycaryol synthase in complex with nerolidol, serving as a surrogate for the reaction intermediate nerolidyl diphosphate. This prefolded ligand allows mapping of the active site and hence the identification of a key carbonyl oxygen of Val179, a highly conserved helix break (G1/2) and its corresponding helix dipole. Stabilising the carbocation at the substrate's C1 position, these elements act in concert to catalyse the 1,10 ring closure, thereby exclusively generating the anti-Markovnikov product. The delineation of a general mechanistic scaffold was confirmed by site-specific mutations. This work serves as a basis for understanding carbocation chemistry in enzymatic reactions and should contribute to future application of these enzymes in organic synthesis.
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