Plant and Cell Physiology · 1983 · 18 citations · 0 references
Life SciencesBiochemistryMicrobiologyCellular MetabolismEnzymologyMetabolismAmino Acid Biosynthesis InhibitionAmino Acid MetabolismEnzyme CharacterizationEnzyme InhibitionEnzyme KineticsEnzyme RegulationAutotrophic GrowthBiosynthetic Enzyme CharacterizationDecarboxylase EnzymesIonic StrengthIonic Strength EffectsOptimal Ph DeterminationPh Effects On Enzyme ActivityPolyamine Biosynthesis
In a Chlorella culture grown asynchronously under autotrophic conditions, two biosynthetic enzymes of putrescine—ornithine decarboxylase (ODC) and arginine decarboxylase (ADC)—were detected. Both enzymes require pyridoxal phosphate and dithiothreitol for their activity but differ in their optimal pH, the ionic strength of their buffer, temperature of inactivation, and Km. In addition, L-canaline was found to inhibit the activity of ODC but not that of ADC. During the logarithmic phase of growth, ODC activity increased sharply, then decreased before the onset of the stationary phase. ADC activity changed only slightly during growth.