Penicillin G acylase-mediated kinetic resolution of racemic 1-(N-acylamino)alkylphosphonic and 1-(N-acylamino)alkylphosphinic acids and their esters
Extensive studies on the penicillin G acylase-mediated kinetic resolution of N-acylated 1-aminoalkylphosphonic and 1-aminoalkylphosphinic acids as well as their esters were carried out to recognise the relationships between the substrate structure, reacti
Zielińska, Katarzyna,Mazurkiewicz, Roman,Szymańska, Katarzyna,Jarz?bski, Andrzej,Magiera, Sylwia,Erfurt, Karol
p. 31 - 40
(2016/07/19)
SYNTHESIS OF DERIVATIVES OF 1-AMINOETHYLPHOSPHONIC AND 1-AMINOETHYLPHOSPHINIC ACIDS AS SUBSTRATES FOR PENICILLINACYLASES
Racemic and optically active N-phenylacetyl derivatives of 1-aminoethylphosphonic acid, 1-aminoethylphosphinic acid, and their mono- and diesters have been synthesized to study the substrate specificity of penicillinacylases.
Solodenko, V. A.,Kasheva, T. N.,Mironenko, D. A.,Kozlova, E. V.,Shvyadas, V. K.,Kukhar, V. P.
p. 1209 - 1215
(2007/10/02)
Preparation of optically active 1-aminoalkylphosphonic acids by stereoselective enzymatic hydrolysis of racemic N-acylated 1-aminoalkylphosphonic acids
N-Phenylacetylated derivatives of 1-aminoalkylphosphonic acids were synthesized and high enantioselectivity of their hydrolysis by penicillin acylase (EC 3.5.1.11) was demonstrated. Stereoselective enzymatic hydrolysis of racemic 1-(N-phenylacetylamino) alkylphosphonic acids was used for preparation of enantiomeric 1-aminoalkylphosphonic acids. The kinetic regularities of penicillin acylase catalyzed hydrolysis were established and the biocatalytic process was optimized to increase the optical purity and the yield of the optically active product.