Results 191 to 200 of about 3,572 (239)
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Structure and Function of Amino Acid Ammonia-lyases
Biocatalysis and Biotransformation, 2004Histidine ammonia-lyase (HAL) and methylaspartate ammonia-lyase (MAL) belong to the family of carbon-nitrogen lyases (EC 4.3.1). The enzymes catalyze the α,β-elimination of ammonia from (S)-His to yield urocanic acid, and (S)-threo-(2S,3S)-3-methylaspartic acid to mesaconic acid, respectively.
Yasuhisa Asano +2 more
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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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Plant Phenylalanine/Tyrosine Ammonia-lyases
Trends in Plant Science, 2020Aromatic amino acid deaminases are key enzymes mediating carbon flux from primary to secondary metabolism in plants. Recent studies have uncovered a tyrosine ammonia-lyase that contributes to the typical characteristics of grass cell walls and contributes to about 50% of the total lignin synthesized by the plant.
Jaime, Barros, Richard A, Dixon
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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, MacDonald, Godwin B, D'Cunha
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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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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.
L, Bourget, T M, Chang
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Journal of Plant Physiology, 2003
Phenylalanine ammonia-lyase (PAL, EC 4.3.1.5) and tyrosine ammonia-lyase (TAL, 4.3.1.), the key enzymes of the phenylpropanoid pathway, are inducible in response to biotic (such as chitin from fungal cell walls) and abiotic cues. Application of chitin and chitosan to soybean leaf tissues caused increased activity of PAL and TAL enzymes.
Wajahatullah, Khan +2 more
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Phenylalanine ammonia-lyase (PAL, EC 4.3.1.5) and tyrosine ammonia-lyase (TAL, 4.3.1.), the key enzymes of the phenylpropanoid pathway, are inducible in response to biotic (such as chitin from fungal cell walls) and abiotic cues. Application of chitin and chitosan to soybean leaf tissues caused increased activity of PAL and TAL enzymes.
Wajahatullah, Khan +2 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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Crop Science, 1993
The relation between the activities of lignification enzymes and deposition of cell‐wall components during progressive stages of development has not been demonstrated. In this study, phenylalanine ammonialyase (PAL), tyrosine ammonia‐lyase (TALI, and cinnamyl alcohohNADPH dehydrogenase (CAD) activities were determined in maize (Zea maize L.) internodes
T. A. Morrison, D. R. Buxton
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The relation between the activities of lignification enzymes and deposition of cell‐wall components during progressive stages of development has not been demonstrated. In this study, phenylalanine ammonialyase (PAL), tyrosine ammonia‐lyase (TALI, and cinnamyl alcohohNADPH dehydrogenase (CAD) activities were determined in maize (Zea maize L.) internodes
T. A. Morrison, D. R. Buxton
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Histidine ammonia-lyase from Streptomyces griseus
Gene, 1992Histidine ammonia-lyase (histidase; HutH) has been purified to homogeneity from Streptomyces griseus and the N-terminal amino acid (aa) sequence used to clone the histidase-encoding structural gene, hutH. The purified enzyme shows typical saturation kinetics and is inhibited competitively by D-histidine and histidinol phosphate.
P C, Wu +3 more
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