Enzymatic Hydrolysis of N-Acylated 1-Aminophosphonic Acids

Penicillin G acylase-mediated kinetic resolution of racemic 1-( N -acylamino)alkylphosphonic and 1-( N -acylamino)alkylphosphinic acids and their esters

“…The resolution of racemic 1-(N-acylamino)alkylphosphonic acids using porcine kidney acylase described by Telegdi et al [14,15] was not confirmed by other authors in later experiments [16]. Solodenko et al [4,[17][18][19] applied penicillin acylase from E. coli for stereoselective hydrolytic kinetic resolution of a few relatively simple N-acylated 1-aminoalkylphosphonic acids, 1-(N-phenylacetylamino)ethylphosphonous acid, as well as dimethyl and diisopropyl esters of 1-(N-phenylacetylamino)ethylphosphonic acid. Zimmermann et al described in the US Patent [20] and other analogical patents the kinetic resolution of phosphonic analogues of a few N-acylated -amino acids using lyophilised, carrier-bound penicillin G acylase (Boehringer Mannheim GmBH).…”