57012-11-0Relevant academic research and scientific papers
Characterisation of the broadly-specific O-methyl-transferase jerf from the late stages of jerangolid biosynthesis
Friedrich, Steffen,Hemmerling, Franziska,Lindner, Frederick,Warnke, Anna,Wunderlich, Johannes,Berkhan, Gesche,Hahn, Frank
, (2016/11/11)
We describe the characterisation of the O-methyltransferase JerF from the late stages of jerangolid biosynthesis. JerF is the first known example of an enzyme that catalyses the formation of a non-aromatic, cyclic methylenolether. The enzyme was overexpressed in E. coli and the cell-free extracts were used in bioconversion experiments. Chemical synthesis gave access to a series of substrate surrogates that covered a broad structural space. Enzymatic assays revealed a broad substrate tolerance and high regioselectivity of JerF, which makes it an attractive candidate for an application in chemoenzymatic synthesis with particular usefulness for late stage application on 4-methoxy-5,6-dihydro-2H-pyran-2-one-containing natural products.
Ring opening/fragmentation of dihydropyrones for the synthesis of homopropargyl alcohols
Tummatorn, Jumreang,Dudley, Gregory B.
, p. 5050 - 5051 (2008/10/09)
Ring-opening/C-C bond cleavage reactions induced by nucleophilic addition of methyl Grignard to 5,6-dihydro-2-pyrone (DHP) triflates 1 furnish homopropargyl alcohols (1 → 2) stereospecifically with respect to the stereochemistry of 1. Carbonyl extrusion from DHP triflates provides a unified and operationally simple strategy for preparing chiral homopropargyl alcohols. Copyright
