نتایج جستجو برای: lyase enzyme activity pal
تعداد نتایج: 1289672 فیلتر نتایج به سال:
The recombinant plasmid pAL-A3 bears a (poly ManA) alginate lyase-encoding gene that originates from the marine bacterium ATCC 433367 (Brown et al., Appl. Environ. Microbiol. (1991) 57, 1870-1872). The alginate lyase produced by Escherichia coli TC4 harbouring pAL-A3 was purified to protein homogeneity and the corresponding gene sequenced, giving access to the first known primary structure of a...
Enzyme substitution therapy with the phenylalanine ammonia lyase (PAL) is a new approach to the treatment of patients with phenylketonuria (PKU). This enzyme is responsible for the conversion of phenylalanine to trans-cinnamic acid. We assessed the PAL enzyme of the endemic plant Cyathobasis fruticulosa (Bunge) Aellen. for its possible role in the dietary treatment of PKU. The enzyme was found ...
Plants develop a plethora of defense strategies during their acclimation and interactions with various environmental stresses. Secondary metabolites play pivotal role in the processes stress acclimation, therefore deciphering relevant responses exchange interpretation underlying molecular mechanisms that may contribute to improved adaptability efficacy. In current study, tomato plants were expo...
Phenylalanine ammonia-lyase (PAL) is the first enzyme involved in the phenylpropanoid pathway and plays important roles in the secondary metabolisms, development and defense of plants. To study the molecular function of PAL in anthocyanin synthesis of Coleus (Solenostemon scutellarioides (L.) Codd), a Coleus PAL gene designated as SsPAL1 was cloned and characterized using a degenerate oligonucl...
Flavonoids are valuable natural products derived from the phenylpropanoid pathway. The objective of this study was to create a host for the biosynthesis of naringenin, the central precursor of many flavonoids. This was accomplished by introducing the phenylpropanoid pathway with the genes for phenylalanine ammonia lyase (PAL) from Rhodosporidium toruloides, 4-coumarate:coenzyme A (CoA) ligase (...
Excising plant tissues has been found to increase the activity of phenylalanine ammonia-lyase (EC 4.1.3.5) (1, 4, 11, 12). This increase is probably due to de novo synthesis of this enzyme, since inhibitors of protein synthesis block the rise of PAL' activity (4, 11, 12). We suggested earlier (4) that the increase of PAL in gherkin hypocotyl segments was due to the release into the medium of re...
Pseudomonas aeruginosa is an opportunistic pathogen that causes a variety of infections in compromised patients. The ability of Pseudomonas aeruginosa to produce chronic infection is based in part on its ability to biosynthesis of biofilm, and alginate is the major polysaccharide in the synthesized biofilm. So alginate degradation is very essential in the dispersion of Pseudomonas aeruginosa bi...
This study was conducted to investigate certain characteristics of the purified Phenylalanine ammonia lyase (PAL). The results revealed that molecular weight 180 kDa by gel filtration and Native-PAGE. optimal pH temperature for enzyme activity were 7 40 °C respectively. stable against values range 6-8. retained 79% its total after incubation one hour at 50 7% (lost 93%) 70 °C. entire completely...
l-Phenylalanine ammonia-lyase (PAL) activity is low in the external layers (flavedo) of intact mature grapefruit peel. Flavedo discs evince upon incubation increasing PAL activity and ethylene production. Light has no effect in enhancing PAL activity in discs. Exogenous ethylene stimulates PAL activity in the flavedo of intact mature grapefruits (half maximum stimulation at 15 ppm); such activi...
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