Ultraviolet Light-induced Formation of Pisatin and Phenylalanine Ammonia Lyase
نویسندگان
چکیده
منابع مشابه
Induction of phenylalanine ammonia lyase and pisatin by photosensitive psoralen compounds.
The psoralen compounds, xanthotoxin and 4,5', 8-trimethylpsoralen, when activated, increased phenylalanine ammonia lyase (PAL) activity and the synthesis of pisatin in excised pea pods. Pods presoaked 1 hr with 4,5',8-trimethylpsoralen and then irradiated 4 minutes with 366 nanometer ultraviolet light had twice as much PAL activity 3 hours after irradiation and 12 times as much PAL activity 20 ...
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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 کاملFungal and Plant Phenylalanine Ammonia-lyase
L-Phenylalanine is one of the essential amino acids that cannot be synthesized in mammals in adequate amounts to meet the requirements for protein synthesis. Fungi and plants are able to synthesize phenylalanine via the shikimic acid pathway. L-Phenylalanine, derived from the shikimic acid pathway, is used directly for protein synthesis in plants or metabolized through the phenylpropanoid pathw...
متن کاملEthylene-induced Phenylalanine Ammonia-Lyase Activity in Carrot Roots.
Ethylene enhanced the activity of phenylalanine ammonialyase in carrot (Daucus carota L., var. "Nauty") root tissue. Slight increase in enzyme activity was exhibited by root discs incubated in ethylene-free air. It was probably due to the ethylene formed within the sliced tissue. Addition of ethylene to the air stream increased phenylalanine ammonia-lyase activity and the total protein content ...
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. ...
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ژورنال
عنوان ژورنال: Plant Physiology
سال: 1971
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.47.4.588