Results 191 to 200 of about 31,890 (243)
Phenylalanine Ammonia-Lyase - An Update On Its Kinetics
, 1989 Khan, Nayeem Ullah +2 more
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Fungal and Plant Phenylalanine Ammonia-lyase [PDF]
Mycobiology, 2011 L-Phenylalanine is one of the essential amino acids that cannot be synthesized in mammals in adequate amounts to meet the requirements for protein synthesis. Fungi and plants are able to synthesize phenylalanine via the shikimic acid pathway. L-Phenylalanine, derived from the shikimic acid pathway, is used directly for protein synthesis in plants or ...
Min Woo Hyun +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
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
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 ...
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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