Results 241 to 250 of about 32,058 (267)
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Phytochemistry, 1973
Abstract The literature concerning the physiology and biochemistry of the enzyme phenylalanine ammonia lyase (PAL) (E.C. 4.1.1.5) from different organisms has been reviewed. Levels of the enzyme are affected by age, light, phytochrome, wounding, infection and growth modifiers. The possibility that PAL is involved in the control of phenolic metabolism
Edith L. Camm, G.H.Neil Towers
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Abstract The literature concerning the physiology and biochemistry of the enzyme phenylalanine ammonia lyase (PAL) (E.C. 4.1.1.5) from different organisms has been reviewed. Levels of the enzyme are affected by age, light, phytochrome, wounding, infection and growth modifiers. The possibility that PAL is involved in the control of phenolic metabolism
Edith L. Camm, G.H.Neil Towers
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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 entrapped in fibers
Biochimie, 1980Phenylalanine ammonia-lyase extracted form Rhodotorula rubra (IFO 1101) was immobilized into cellulose triacetate fibers made hemocompatible by physical blend with a platelet anti-aggregating agent. The entrapped enzyme could operate at physiological values of phenylalanine and tyrosine reducing their level to traces within a few hours.
W. Marconi +4 more
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A modern view of phenylalanine ammonia lyase
Biochemistry and Cell Biology, 2007Phenylalanine ammonia lyase (PAL; E.C.4.3.1.5), which catalyses the biotransformation of l-phenylalanine to trans-cinnamic acid and ammonia, was first described in 1961 by Koukol and Conn. Since its discovery, much knowledge has been gathered with reference to the enzyme’s catabolic role in microorganisms and its importance in the phenyl propanoid ...
M. Jason MacDonaldM.J. MacDonald +1 more
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Artificial Cell-Microencapsulated Phenylalanine Ammonia-Lyase
Applied Biochemistry and Biotechnology, 1984Phenylalanine ammonia-lyase (PAL) is immobilized in collodion artificial cells. Once technical problems associated with the encapsulation of this enzyme were solved, the enzyme kinetics were compared to PAL in free solution. Microencapsulated PAL has an apparent enzyme activity that is 20% of the activity of enzyme in free solution.
Thomas Ming Swi Chang, L. Bourget
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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.
K. Edwards +9 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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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.
C.P. Vance +2 more
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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 +2 more
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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 +2 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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