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Enzymes in Organic Synthesis, 11. Enantioselective Lactonization of Methyl 3,5‐Dihydroxyalkanoates. — An Access to (3 R ,5 S ,6 E )‐3‐Hydroxy‐7‐phenyl‐6‐hepten‐5‐olide by Enzyme‐Catalyzed Kinetic Resolution in Organic Solvents
Author(s) -
Henkel Birgitta,
Kunath Annamarie,
Schick Hans
Publication year - 1992
Publication title -
liebigs annalen der chemie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 0170-2041
DOI - 10.1002/jlac.1992199201133
Subject(s) - chemistry , enantioselective synthesis , intramolecular force , transesterification , enantiomer , lipase , enzyme , enantiomeric excess , catalysis , stereochemistry , ether , lactone , kinetic resolution , organic chemistry , medicinal chemistry
By enzyme‐catalyzed intramolecular transesterification methyl (±)‐(3 R *,5 S *,6 E )‐3,5‐dihydroxy‐7‐phenyl‐6‐heptenoate ( rac ‐ 4 ) can be enantioselectively converted into the δ‐lactone 5 . An enantiomeric excess of 80% was obtained by Pancreatin in diethyl ether at ambient temperature. Repetition of the enzyme‐catalyzed lactonization with enantiomerically enriched 3,5‐dihydroxy ester 4 / ent ‐ 4 enhanced the e.e. to >99%. Lipases of Pseudomonas and Candida sp. 382 tested in eight organic solvents were less efficient. The absolute configuration of 5 , obtained as the major enantiomer in all experiments, has been determined by its conversion into the known (—)‐goniothalamin ( 6 ).