Results 201 to 210 of about 31,890 (243)
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Redesign of a Phenylalanine Aminomutase into a Phenylalanine Ammonia Lyase
ChemCatChem, 2013AbstractAn aminomutase, naturally catalyzing the interconversion of (S)‐α‐phenylalanine and (R)‐β‐phenylalanine, was converted into an ammonia lyase catalyzing the nonoxidative deamination of phenylalanine to cinnamic acid by a rational single‐point mutation.
Sebastian Bartsch +6 more
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Phenylalanine ammonia-lyase gene organization and structure
Plant Molecular Biology, 1989Phenylalanine ammonia-lyase (PAL; EC 4.3.1.5) genomic sequences were isolated from bean (Phaseolus vulgaris L.) genomic libraries using elicitor-induced bean PAL cDNA sequences as a probe. Southern blot hybridization of genomic DNA fragments revealed three divergent classes of PAL genes in the bean genome.
C L, Cramer +8 more
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Biosynthesis of 15NL-phenylalanine by phenylalanine ammonia-lyase from Rhodotorula glutinis
Amino Acids, 2008Catalyzed by phenylalanine ammonia-lyase from Rhodotorula glutinis, 2% trans-cinnamic acid and 0.5 mol/l (15NH4)2SO4 was bioconverted to 15NL-phenylalanine. The yield and the purity of 15NL-phenylalanine reached 71 and 99.3%, respectively. The results showed that 96% of 15N was labeled on the L-phenylalanine and 88% of (15NH4)2SO4 was recovered.
Wenya, Wang +3 more
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Properties of yeast l-phenylalanine ammonia-lyase
Archives of Biochemistry and Biophysics, 1972Abstract l -Phenylalanine ammonia-lyase from the yeast Rhodotorula glutinis is inhibited by the halide anions iodide, bromide, and chloride. Iodide acts as a competitive inhibitor of phenylalanine deamination. The enzyme is deactivated by reagents attacking either amino or sulfhydryl functional groups and contains approximately two catalytically ...
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Activity of l-phenylalanine ammonia-lyase in organic solvents
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1997L-Phenylalanine ammonia-lyase (EC 4.3.1.5), (PAL) was shown to be active in a monophasic non-aqueous medium for the first time. Ultraviolet absorbance spectra of trans-cinnamic acid were shown to be similar in both water and n-octanol. High catalytic rates were observed only when the enzyme was placed in solvents containing high concentrations of water.
D G, Rees, D H, Jones
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Further observations on phenylalanine ammonia-lyase in fungi
Phytochemistry, 1975Abstract Phenylalanine ammonia-lyase (PAL) has been detected in an Ascomycete, Nectria cinnabarina. Growth in light increases levels of PAL in some but not all Basidiomycetes.
G H N Towers
exaly +2 more sources
Tissue and method specificities of phenylalanine ammonia-lyase assay
Journal of Plant Physiology, 2012A large number of studies have estimated phenylalanine ammonia-lyase (PAL) activity because it strongly reacts to various stimuli. Activity of this enzyme has been assayed mainly by means of spectrophotometry, but the precision of this method is poorly known.
Jozef, Kováčik, Bořivoj, Klejdus
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Australian Journal of Plant Physiology, 1980
In constant light, whole apples (cv. Red Spy) that received alternating 6/25°C treatment accumulated more phenylalanine ammonia-lyase (PAL) and anthocyanin than those receiving constant 25° throughout the course of experiment. The stimulatory effect of low temperature (6°) on the activity of PAL and synthesis of anthocyanin was also observed in the ...
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In constant light, whole apples (cv. Red Spy) that received alternating 6/25°C treatment accumulated more phenylalanine ammonia-lyase (PAL) and anthocyanin than those receiving constant 25° throughout the course of experiment. The stimulatory effect of low temperature (6°) on the activity of PAL and synthesis of anthocyanin was also observed in the ...
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Phytochemistry, 1991
Abstract Phenylalanine ammonia-lyase inactivating factor (IF) prepared from chloroplasts isolated from sunflower leaves was utilized to study its inactivating effects on l -phenylalanine ammonia-lyase from Rhodotorula glutinis in vitro. The effects of inactivation by inactivating factor were compared with those caused by chemicals such as sodium ...
Subhash C. Gupta, Leroy L. Creasy
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Abstract Phenylalanine ammonia-lyase inactivating factor (IF) prepared from chloroplasts isolated from sunflower leaves was utilized to study its inactivating effects on l -phenylalanine ammonia-lyase from Rhodotorula glutinis in vitro. The effects of inactivation by inactivating factor were compared with those caused by chemicals such as sodium ...
Subhash C. Gupta, Leroy L. Creasy
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Protection of phenylalanine ammonia-lyase from proteolytic attack
Biochemical and Biophysical Research Communications, 1985Phenylalanine ammonia-lyase contained within permeabilized cells of Rhodosporidium toruloides was protected from proteolytic attack by trypsin, chymotrypsin and duodenal juice. The inactivation by the proteases was biphasic. The enzyme contained within the yeast cells had a similar Km for phenylalanine and Ki for cinnamic acid to the protein in free ...
H J, Gilbert, M, Tully
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