Enzymatic preparation of both L- and D-enantiomers of phosphonic and phosphonous analogues of alanine using penicillin acylase

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

“…Therefore, our results confirmed that penicillin G acylase showed a high preference in catalysing the hydrolysis of N-phenylacetyl moiety [4,18,19].…”

“…The same stereochemical preference of penicillin G acylase was found by Zimmermann et al [20] and Solodenko et al [4,18] for phosphonic analogues of 1-N-phenylacetylated alanine, phenylalanine, and leucine, as well as H-phosphinic analogue of 1-N-phenylacetylalanine. Reactivities of the phosphonic analogues of alanine, both free acid 3b and their dimethyl esters 2c (R 2 = Me), are 2-6 orders of magnitude higher compared to that of the corresponding phosphonic analogues of phenylalanine, valine, leucine, asparagine, t-Bu-serine, and serine…”

“…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).…”

Kinetic study of penicillin acylase from Alcaligenes faecalis

“…It was recently recognized, for example, that benzylpenicillin, which was previously claimed to be the preferred substrate of the best studied penicillin acylase from E. coli [1–3], is not amongst the five most reactive substrates [18]. In contrast to aminoacylases ( N ‐acylamino acid amidohydrolases, EC 3.5.1.14), penicillin acylase from E. coli was shown to be an effective biocatalyst for the enantioselective hydrolysis of a number of non‐conventional amino acid derivatives such as N ‐acylated aminoalkylphosphonic acids [19], aminoalkylphosphonous acids [20], β‐ and γ‐amino acids [21–24]. Penicillin acylases from different origin most probably also possess much wider substrate specificity than previously imagined but appropriate kinetic and specificity studies still have to confirm this suggestion.…”

Effect of organic cosolvent on kinetic resolution of tert-leucine by penicillin G acylase from Kluyvera citrophila

“…It can hydrolyze or synthesize the amides and esters of phenylacetic acid derivatives and its role in enantioselective hydrolysis is becoming increasingly popular recently. It has been shown that PGA from E. coli can hydrolyze enantioselectively N-phenylacetyled derivatives of a-amino acids and their derivatives [5], such as b-and c-amino acids [6,7], a-amino alcohols [8], a-amino nitriles [9], 1-aminoalkyl phosphonic acid [10,11] and 1-aminoethylphosphonous acids [10]. Although E. coli PGA is commercially available, PGA from K. citrophila may have many features for industrial applications (ease of immobilization and greater stability to heat, pH and organic solvents) [12].…”