Fungal and Plant Phenylalanine Ammonia-lyase
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منابع مشابه
Fungal 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 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 کاملInduction of phenylalanine ammonia-lyase and 4-coumarate:CoA ligase mRNAs in cultured plant cells by UV light or fungal elicitor.
The mRNAs encoding two enzymes of phenylpropanoid metabolism, phenylalanine ammonia-lyase (PAL; EC 4.3.1.5) and 4-coumarate:CoA ligase (4CL; EC 6.2.1.12), were induced in cultured parsley cells (Petroselinum hortense) either by irradiation with UV light or by treatment with elicitor, a cell-wall fraction of the fungus Phytophthora megasperma f. sp. glycinea. Two-dimensional gel electrophoresis ...
متن کاملConcomitant induction of phenylalanine ammonia-lyase and flavanone synthase mRNAs in irradiated plant cells.
Irradiation of previously dark-grown cell suspension cultures from parsley (Petroselinum hortense Hoffm.) with ultraviolet light caused large, concomitant increases in mRNA activities for two characteristic enzymes of phenylpropanoid metabolism, phenylalanine ammonia-lyase, and flavanone synthase. The rates of enzyme synthesis both in vitro in a reticulocyte lysate and in vivo were quantitated ...
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: Mycobiology
سال: 2011
ISSN: 1229-8093,2092-9323
DOI: 10.5941/myco.2011.39.4.257