Purification and Characterization of Anabaena flos-aquae Phenylalanine Ammonia-Lyase as a Novel Approach for Myristicin Biotransformation
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چکیده
منابع مشابه
Purification 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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Calves, rats, ducks, and goldfish given lethal oral doses of bacteria-free lyophilized cell suspensions of toxic Anabaena flos-aquae died as a result of respiratory arrest. Experiments with selected animals and pharmacological preparations showed that the main effect of the toxin was production of a sustained postsynaptic depolarizing neuromuscular blockade.
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...
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The toxicity of 7 herbicides to the three cyanobacteria was tested in this work. The results indicated that: (1) There was a highly significant relationship between dried weight or chlorophyll-a and OD680nm for tested cyanobacteria; (2) the toxicity of the tested herbicides with the order from high to low was: photosynthesis-inhibiting > ACCase inhibitor > protox inhibiting herbicides; (3) the ...
متن کاملOptimized condition for enhanced soluble-expression of recombinant mutant anabaena variabilis phenylalanine ammonia lyase.
PURPOSE Recently discovered Anabaena variabilis phenylalanine ammonia lyase (AvPAL) proved to be a good candidate for enzyme replacement therapy of phenylketonuria. Outstanding stability properties of a mutant version of this enzyme, produced already in our laboratory, have led us to the idea of culture conditions optimization for soluble expression of this therapeutically valuable enzyme in E....
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ژورنال
عنوان ژورنال: Journal of Microbiology and Biotechnology
سال: 2020
ISSN: 1017-7825,1738-8872
DOI: 10.4014/jmb.1908.08009