62561-76-6Relevant articles and documents
METHOD FOR PREPARING THIENYL ALANINE HAVING OPTICAL ACTIVITY
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Paragraph 0073, (2018/10/30)
This invention relates to a method of preparing optically active β-2-thienyl-alanine, and more particularly to a method of preparing optically active β-2-thienyl-L-alanine or optically active β-2-thienyl-D-alanine through an optical resolution reaction using chiral dibenzoyl tartaric acid or a derivative thereof as an optical resolving agent.
Bisepoxide cross-linked enzyme aggregates - New immobilized biocatalysts for selective biotransformations
Weiser, Diana,Varga, Andrea,Kovacs, Klaudia,Nagy, Flora,Szilagyi, Andras,Vertessy, Beata G.,Paizs, Csaba,Poppe, Laszlo
, p. 1463 - 1469 (2014/05/20)
Glycerol diglycidyl ether (GDE) is a convenient and inexpensive bisepoxide cross-linker as demonstrated by the preparation of cross-linked enzyme aggregates (CLEAs) from two enzyme classes. The GDE CLEAs of lipase from Pseudomonas fluorescens (AK), lipase from Burkholderia cepacia (PS), and lipase B from Candida antarctica (CaL B) as well as of phenylalanine ammonia-lyase (PAL) from Petroselinum crispum demonstrated improved properties as compared with their glutaraldehyde (GA) cross-linked counterparts. Ultrasonication studies indicated that the GDE CLEAs of lipase PS and PAL were mechanically more stable than the GA CLEAs. In the kinetic resolution of rac-1-phenylethanol, the catalytic activity of the GDE-lipase CLEAs (U=69.6, 134.8, and 127.4 U g -1 for AK, CaL B, and PS prepared at 22 °C, respectively) surpassed that of the corresponding GA-lipase CLEAs (U=24.4, 131.0, and 119.2 U g-1 for AK, CaL B, and PS prepared at 22 °C, respectively). The GDE co-CLEAs from PAL and bovine serum albumin (BSA) could be recycled at least three times if used for the stereoselective ammonia addition in 6 M ammonia to (E)-3-(thiophen-2-yl)acrylic acid, whereas the recycling of the conventional GA-PAL CLEAs from this medium failed. The missing linker: Glycerol diglycidyl ether is applied as a cross-linker for cross-linked enzyme aggregates (CLEAs) of various enzymes such as lipases and phenylalanine ammonia lyases. The bisepoxide CLEAs prove to be efficient and robust biocatalysts surpassing the performance of the glutaraldehyde CLEAs.
The interaction of heteroaryl-acrylates and alanines with phenylalanine ammonia-lyase from parsley
Paizs, Csaba,Katona, Adrian,Retey, Janos
, p. 2739 - 2744 (2008/02/03)
Acrylic acids and alanines substituted with heteroaryl groups at the β-position were synthesized and spectroscopically characterized (UV, HRMS, 1H NMR, and 13C NMR spectroscopy). The heteroaryl groups were furanyl, thiophenyl, benzofuranyl, and benzothiophenyl and contained the alanyl side chains either at the 2- or 3-positions. While the former are good substrates for phenylalanine ammonia lyase (PAL), the latter compounds are inhibitors. Exceptions are thiophen-3-yl-alanine, a moderate substrate and furan-3-yl-alanine, which is inert. Possible reasons for these exceptions are discussed. Starting from racemic het eroaryl-2-alanines their D-enantiomers were prepared by using a stereodestructive procedure. From the heteroaryl-2- acrylates, the L-enantiomers of the heteroaryl-2-alanines were prepared at high ammonia concentration. These results can be best explained by a Friedel - Crafts-type electrophilic attack at the aromatic part of the substrates as the initial step of the PAL reaction.