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The effects of sunflower l-phenylalanine ammonia-lyase inactivating factor on Rhodotorula glutinis l-phenylalanine ammonia-lyase

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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Phenylalanine-dependent de novo synthesis of phenylalanine ammonia-lyase from Rhodotorula glutinis

Archives of Biochemistry and Biophysics, 1982
Abstract A synthetic medium was developed in which the presence of phenylalanine ammonialyase (PAL) in the yeast Rhodotorula glutinis was dependent on the addition of l -phenylalanine. The appearance of PAL activity occurred during mid- to late log phase regardless of the time of l -phenylalanine introduction into the medium.
J F, Wick, J E, Willis
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[Phenylalanine ammonia-lyase of pigmented yeasts].

Mikrobiologiia, 1980
116 pigmented yeast cultures were tested for the presence of L-phenylalanine-ammonia lyase transforming L-phenylalanine into trans-cinnamic acid. The enzyme was found in 54 strains. Most of these strains belonged to the genera Rhodotorula and Sporobolomyces.
N Iu, Mushi   +3 more
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The phenylalanine ammonia-lyase gene family in Arabidopsis thaliana

Plant Molecular Biology, 1995
Phenylpropanoid derivatives are a complex class of secondary metabolites that have many important roles in plants during normal growth and in responses to environmental stress. Phenylalanine ammonialyase (PAL) catalyzes the first step in the biosynthesis of phenylpropanoids, and is usually encoded by a multi-gene family.
L A, Wanner   +4 more
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Phenylalanine Ammonia-Lyase and the Phenylalanine Ammonia-Lyase Inactivating System: Effects of Light, Temperature and Mineral Deficiencies

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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Activity of l-phenylalanine ammonia-lyase in organic solvents

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1997
L-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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Tissue and method specificities of phenylalanine ammonia-lyase assay

Journal of Plant Physiology, 2012
A 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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Phenylalanine ammonia lyase gene expression during abscission in citrus

Physiologia Plantarum, 2002
Phenylalanine ammonia lyase (PAL) gene expression was examined in fruit and leaf abscission zones of Valencia orange for periods up to 72 h after induction of abscission with Ethrel® (CEPA) or the citrus mature fruit‐specific abscission material 5‐chloro‐3‐methyl‐4‐nitro‐1H‐pyrazole (CMN‐P).
Igor A, Kostenyuk   +2 more
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[72a] l-phenylalanine ammonia-lyase (potato tubers)

1970
Publisher Summary This chapter presents the assay, purification, and properties of L-phenylalanine ammonia-lyase from potato tubers. The initial rate of cinnamate formation is followed with a spectrophotometer. Under the standard assay conditions, 1 micromole of trans-cinnamate in 3 ml has an absorbancy of 3.0 at 290 m μ and 6.1 at 270 m μ .
Evelyn A. Havir, Kenneth R. Hanson
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[72b] l-phenylalanine ammonia-lyase (Ustilago bordei)

1970
Publisher Summary This chapter describes the assay, purification, and properties of L-phenylalanine ammonia-lyase. The enzyme may be assayed by measuring the appearance of trans-cinnamic acid in two ways—namely, by measuring the optical density at 268 m μ or by determining the radioactivity.
P.V. Subba Rao, G.H.N. Towers
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