Regulation of L-phenylalanine ammonia-lyase by L-phenylalanine and nitrogen in Neurospora crassa
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l-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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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 کاملPhenylalanine-Tyrosine Biosynthesis in NEUROSPORA CRASSA.
IOCHEMICAL investigations of the phenylalanine-tyrosine specific portion of the aromatic pathmway reveal a reaction sequence depicted in Figure 1. Although the organisms studied use similar intermediates to accomplish phenylalanine and tyrosine synthesis, some important functional differences exist. Aerobacter aerogenes and Escherichia coli W possess two molecular forms of chorismate mutase sep...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1982
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.150.3.1287-1291.1982