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Enzymes in Organic Chemistry, 11: [1] Hydrolase‐Catalyzed Resolution of α‐ and β‐Hydroxyphosphonates and Synthesis of Chiral, Non‐Racemic β‐Aminophosphonic Acids
Author(s) -
Woschek A.,
Lindner Wolfgang,
Hammerschmidt F.
Publication year - 2003
Publication title -
advanced synthesis and catalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.541
H-Index - 155
eISSN - 1615-4169
pISSN - 1615-4150
DOI - 10.1002/adsc.200303135
Subject(s) - chemistry , diisopropyl ether , hydrolysis , kinetic resolution , lipase , enantioselective synthesis , acylation , enantiomer , catalysis , triacylglycerol lipase , subtilisin , enzyme , organic chemistry , enantiomeric excess , stereochemistry , ether , substrate (aquarium) , oceanography , geology
Abstract The enantioselective acylation of racemic diisopropyl α‐ and β‐hydroxyphosphonates by hydrolases in t ‐butyl methyl ether with isopropenyl acetate as acyl donor is limited by the narrow substrate specificity of the enzymes. High enantiomeric excesses (up to 99%) were obtained for the acetates of ( S )‐diisopropyl 1‐hydroxy‐(2‐thienyl)methyl‐, 1‐hydroxyethyl‐ and 1‐hydroxyhexylphosphonate and ( R )‐diisopropyl 2‐hydroxypropylphosphonate. The hydrolysis of a variety of β‐chloroacetoxyphosphonates by the lipase from Candida cylindracea and protease subtilisin in a biphasic system gives ( S )‐β‐hydroxyphosphonates (ee 51–92%) enantioselectively. ( S )‐2‐Phenyl‐2‐hydroxyethyl‐ and ( S )‐3‐methyl‐2‐hydroxybutylphosphonates (ee 96% and 99%, respectively) were transformed into ( R )‐2‐aminophosphonic acids of the same ee.