Structural and Catalytic Properties of the Four Phenylalanine Ammonia-Lyase Isoenzymes from Parsley (Petroselinum Crispum Nym.)
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چکیده
منابع مشابه
Pectate hydrolases of parsley (Petroselinum crispum) roots.
The presence of various enzyme forms with terminal action pattern on pectate was evaluated in a protein mixture obtained from parsley roots. Enzymes found in the soluble fraction of roots (juice) were purified to homogeneity according to SDS-PAGE, partially separated by preparative isoelectric focusing and characterized. Three forms with pH optima 3.6, 4.2 and 4.6 clearly preferred substrates w...
متن کاملThe 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...
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...
متن کاملYeast Phenylalanine Ammonia-lyase
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 کاملStructural basis for the catalytic mechanism of aspartate ammonia lyase.
Aspartate ammonia lyases (or aspartases) catalyze the reversible deamination of L-aspartate into fumarate and ammonia. The lack of crystal structures of complexes with substrate, product, or substrate analogues so far precluded determination of their precise mechanism of catalysis. Here, we report crystal structures of AspB, the aspartase from Bacillus sp. YM55-1, in an unliganded state and in ...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1994
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1994.00491.x