منابع مشابه
l-Phenylalanine Ammonia-lyase (Maize): Partial Purification and Response to Gibberellic Acid and Cycloheximide of l-Phenylalanine and l-Tyrosine Ammonia-lyase Activities.
Extracts of maize leaf sheath tissue deaminate both l-phenylalanine and l-tyrosine. The activities with both substrates are enhanced by treating the plant with gibberellic acid. Both activities decrease rapidly at the same rate when tissue is incubated in a moist atmosphere, and this decrease can be slowed by treatment with cycloheximide. The ratio of the activities was constant throughout a se...
متن کاملl-Phenylalanine Ammonia-Lyase (Maize): Evidence for a Common Catalytic Site for l-Phenylalanine and l-Tyrosine.
l-Phenylalanine ammonia-lyase (E.C. 4.3.1.5) from maize is active with l-tyrosine and l-phenylalanine and exhibits atypical Michaelis-Menten kinetics with both substrates. With phenylalanine as a substrate, the pH optimum is 8.7 and with tyrosine, 7.7. The estimated Km at high substrate concentrations is 0.27 mm for phenylalanine and 0.029 mm for tyrosine. However, the V(max) with phenylalanine...
متن کاملYeast Phenylalanine Ammonia-lyase
I?henyialanine ammonia-lyase from the yeast Rhodotorula gluiinis was purified by salt fractionations and Sephadex chromatography. Density gradient centrifugation and Sephadex chromatography indicated its molecular weight to be about 275,000. Enzymatic deamination of several ring-substituted phenylalanine analogues and n-phenylalanine was studied. While cinnamic acid, a product of deamination, a...
متن کاملEnzymes in Metabolism of Amino Acids. VII.* Phenylalanine Ammonia-Lyase in Maize {Zea mays L.)
We have isolated an enzyme, phenylalanine ammonia-lyase (EC 4.3.1.5.), from the rootlets of Zea mays var. СЕ-IV. After partial purification by fractional salting out with ammonium sulfate and gel chromatography on Sephadex G-100, we obtained a preparation of a 40-fold greater specific activity than that of the crude homogenate. We hbve determined the ap parent Michaelis constant and the activa...
متن کاملl-Phenylalanine Ammonia-Lyase Activity During Germination of Phaseolus vulgaris.
l-Phenylalanine ammonia-lyase (PAL) activity develops in excised bean axes after approximately 5 hours of incubation and reaches a maximum level after 14 hours of incubation. Light does not affect the development of activity, but puromycin, cycloheximide, actinomycin D, and 5-fluorouracil inhibit.During this period of incubation both d- and l-p-fluorophenylalanine stimulate fresh weight increas...
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ژورنال
عنوان ژورنال: Plant Physiology
سال: 1972
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.50.4.480