Expression in Escherichia coli of catalytically active phenylalanine ammonia-lyase from parsley
نویسندگان
چکیده
منابع مشابه
The interaction of heteroaryl-acrylates and alanines with phenylalanine ammonia-lyase from parsley.
Acrylic acids and alanines substituted with heteroaryl groups at the beta-position were synthesized and spectroscopically characterized (UV, HRMS, (1)H NMR, and (13)C 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 ammo...
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I?henyialanine ammonia-lyase from the yeast Rhodotorula gluiinis was purified by salt fractionations and Sephadex chromatography. Density gradient centrifugation and Sephadex chromatography indicated its molecular weight to be about 275,000. Enzymatic deamination of several ring-substituted phenylalanine analogues and n-phenylalanine was studied. While cinnamic acid, a product of deamination, a...
متن کاملTruncated phenylalanine ammonia-lyase expression in tomato (Lycopersicon esculentum).
Southern blot analyses of genomic DNA fragments suggest there are five different classes of phenylalanine ammonia-lyase (PAL, EC 4.3.1.5) genomic sequence in tomato (Lycopersicon esculentum). Isolation and subsequent sequence analysis of three examples from genomic libraries reveal highly homologous coding sequences but also a surprisingly high frequency of single point mutations which would tr...
متن کاملPurification and Characterization of Phenylalanine Ammonia Lyase from Trichosporon cutaneum
Trichosporon cutaneum phenylalanine ammonia lyase was selected as a model to investigate the dual substrate activity of this family of enzymes. Sequencing of the PAL gene identified an extensive intron region at the N-terminus. Five amino acid residues differing from a prior report were identified. Highest Phe : Tyr activities (1.6 ± 0.3 : 0.4 ± 0.1 μ mol/h g wet weight) were induced by Tyr. ...
متن کاملFunctional properties of a phenylalanine ammonia-lyase promoter from Arabidopsis.
Phenylalanine ammonia-lyase (PAL) is encoded by a small family of genes in Arabidopsis. We cloned and partially characterized one of these genes, PAL1. The deduced amino acid sequence is highly similar to PAL from bean, parsley, and rice. The promoter contains sequence elements homologous to two putative regulatory elements conserved among several phenylpropanoid genes. The regulation of the PA...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1989
ISSN: 0014-5793
DOI: 10.1016/0014-5793(89)81687-4