52794-99-7Relevant articles and documents
Telescopic one-pot condensation-hydroamination strategy for the synthesis of optically pure L-phenylalanines from benzaldehydes
Parmeggiani, Fabio,Ahmed, Syed T.,Weise, Nicholas J.,Turner, Nicholas J.
, p. 7256 - 7262 (2016/10/26)
A chemo-enzymatic telescopic approach was designed for the synthesis of L-arylalanines in high yield and optical purity, starting from commercially available and inexpensive substituted benzaldehydes. The method exploits a chemical Knoevenagel–Doebner condensation (optimised to give complete conversions in a short reaction time, employing microwave irradiation) and a biocatalytic phenylalanine ammonia lyase mediated hydroamination (for the stereoselective addition of ammonia). The two reactions can be run sequentially in one pot, bringing together the advantages of chemical and biological catalysis. The preparative applicability was demonstrated with the synthesis of five L-dihalophenylalanines (71–84% yield, 98–99% ee) of relevance as molecular probes, for medicinal chemistry and for the synthesis of pharmaceutical ingredients.
Enantioselective scavenging using homogenate of Rhodotorula graminis: a facile preparation of d-amino acid derivatives in enantiopure form
Zhang, Zizhang
body text, p. 6468 - 6470 (2009/04/06)
An enantioselective scavenger (ES) comprised homogenate of Rhodotorula graminis containing multiple enzymes can enantioselectively remove l-enantiomer in a racemic mixture of amino acid derivatives (AADs), yielding d-enantiomer in high ee. Thirteen non-proteinogenic AADs were produced in enantiopure d form. The method appears to be an efficient cleaning and preparative strategy which can be applied to the production of d-AADs in high ee by enantioselectively scavenging the 'l-contaminants'.
METABOLISM OF D,L-CHLORO-PHENYLALANINES BY PHENYLALANINE AMINOTRANSFERASE ISOZYMES PURIFIED FROM BUSHBEAN SHOOTS
Taylor, David C.,Wightman, Frank
, p. 1279 - 1288 (2007/10/02)
Key Word Index - Phaseolus vulgaris; Leguminosae; bushbean; metabolism; phenylalanine decarboxylase; phenylalanine aminotransferase; purification; substituted amino acids; D,L-chloro-phenylalanines.A series of mono-, di- and trichloro-D,L-phenylalanines was tested as substrates for both phenylalanine aminotransferase and phenylalanine decarboxylase partially purified from bushbean (Phaseolus vulgaris L.) seedling extracts by ammonium sulphate fractionation and Sephacryl S-300 gel filtration.While most of the D,L-chlorophenylalanines were transaminated at rates of 35-100percent of that observed with D,L-phenylalanine, no chloro-phenylalanine decarboxylase activity was observed.A transamination reaction is therefore likely to be the initial step in the conversion of chloro-phenylalanines to their corresponding chloro-phenylacetic acids via a reaction pathway similar to the known route for the metabolism of L-phenylalanine to phenylacetic acid.The highest specific activity of phenylalanine aminotransferase was found in both root and shoot tissues of bushbean at the 10-day stage of seedling growth.Partially purified extracts of these tissues were able to transaminate most of the mono- and dichloro-phenylalanines at ca 20-40percent of the rate observed with D,L-phenylalanine, while the trichloro-phenylalanines (assayed at lower concentrations due to solubility) were transaminated at rates equal to those observed with D,L-phenylalanine.The 4-chloro derivative was the best substrate tested showing rates of transamination that were 25percent higher than those observed with D,L-phenylalanine.Further purification of shoot fractions by DEAE-Sephacel chromatography resolved the phenylalanine aminotransferase activity into two peaks (enzymes I and II) which on further purification, were found to behave differently during hydrophobic chromatography and PAGE.These results indicated the presence of two isozymic forms of phenylalanine aminotransferase in bushbean shoots and both were found to catalyse transamination of the monochloro-phenylalanines examined in this study.
