130325-37-0Relevant articles and documents
Enzymatic Preparation of Both L- and D-Enantiomers of Phosphonic and Phosphonous Analogues of Alanine Using Penicillin Acylase
Solodenko, Vladimir A.,Belik, Michail Y.,Galushko, Sergei V.,Kukhar, Valeri P.,Kozlova, Elena V.,et al.
, p. 1965 - 1968 (1993)
D-Enantiomers of N-acylated 1-aminoethylphosphonic and 1-aminoethylphosphonous acids were able to be hydrolyzed with high concentrations of penicillin acylase in a reasonable time period.This finding was used to prepare both L- and D-enantiomers of these phosphorus analogues of alanine by stepwise enzymatic hydrolysis of their racemic N-phenylacetyl derivatives using the same enzyme - penicillin acylase - by simply changing the enzyme/substrate ratio.
SYNTHESIS OF DERIVATIVES OF 1-AMINOETHYLPHOSPHONIC AND 1-AMINOETHYLPHOSPHINIC ACIDS AS SUBSTRATES FOR 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)
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.