141928-29-2Relevant articles and documents
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)
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.
Enzymes in Organic Synthesis, 11.- Enantioselective Lactonization of Methyl 3,5-Dihydroxyalkanoates. - An Access to (3R,5S,6E)-3-Hydroxy-7-phenyl-6-hepten-5-olide by Enzyme-Catalyzed Kinetic Resolution in Organic Solvents
Henkel, Birgitta,Kunath, Annamarie,Schick, Hans
, p. 809 - 812 (2007/10/02)
By enzyme-catalyzed intramolecular transesterfication methyl (+/-)-(3R*,5S*,6E)-3,5-dihydroxy-7-phenyl-6-heptenoate (rac-4) can be enantioselectively converted into the δ-lactone 5.An enantiomeric excess of 80percent was obtained by