54582-02-4Relevant academic research and scientific papers
Efficient chemoenzymatic synthesis of (S)-α-amino-4-fluorobenzeneacetic acid using immobilized penicillin amidase
Lin, Chao-Ping,Tang, Xiao-Ling,Zheng, Ren-Chao,Zheng, Yu-Guo
, p. 174 - 179 (2018/06/26)
An efficient chemoenzymatic route was developed for synthesis of (S)-α-amino-4-fluorobenzeneacetic acid, a valuable chiral intermediate of Aprepitant, using immobilized penicillin amidase catalyzed kinetic resolution of racemic N-phenylacetyl-4-fluorophen
HOMOCHIRAL HETEROORGANIC ANALOGS OF NATURAL COMPOUNDS. I. PREPARATIVE BIOCATALYTIC METHOD OF OBTAINING FLUORINE-CONTAINING L- AND D-PHENYLGLYCINES
Soloshonok, V. A.,Galaev, I. Yu.,Shvyadas, V. K.,Kozlova, E. V.,Kotik, N. V.,et al.
, p. 228 - 232 (2007/10/02)
A biocatalytic method of obtaining homochiral o- and p-fluorine-substituted phenylglycines by enantiomeric hydrolysis from N-phenylacetyl or N-acetyl derivatives under the action of Escherichia coli penicillin acylase or Streptoverticillium olivoreticuli aminoacylase is proposed.The L form of the amino acid and the unhydrolyzed D-enantiomer of the initial derivative are separated by extraction and chromatographic methods.The acid hydrolysis of the D-enantiomers of N-phenylacetyl derivatives of fluorine-substituted phenylglycines leads to partial (about 15percent) racemization.With a substantially higher (by two orders of magnitude) concentration of enzyme and an increase in the reaction time it is possible to use penicillinase as a catalyst for the hydrolysis of the D-enantiomer of the N-phenylacetyl derivative not accompanied by any appreciable racemization whatever.
