Results 161 to 170 of about 3,523 (218)
Some of the next articles are maybe not open access.
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
openaire +2 more sources
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
openaire +1 more source
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
openaire +1 more source
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
[149a] Histidine ammonia-lyase (Pseudomonas)
1971Publisher Summary This chapter focuses on Histidine Ammonia-Lyas (Pseudomonas). Histidine ammonia-lyase is assayed spectrophotometrically. At 277 mμ, urocanate has an extinction coefficient of 1.88 × l0 4 M -1 cm -1 . The enzymatic conversion of L -histidine to urocanate has been considered irreversible— 15 NH 3 added to the reaction mixture does
Matthew M. Reghler, Herbert Tabor
openaire +1 more source
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 ...
openaire +2 more sources