
doi: 10.1007/bf02877044
pmid: 283
FDP aldolase was found to be present in the cell-free extracts of Rhizobium leguminosarum, Rhizobium phaseoli, Rhizobium trifolii, Rhizobium meliloti, Rhizobium lupini, Rhizobium japonicum and Rhizobium species from Arachis hypogaea and Sesbania cannabina. The enzyme in 3 representative species has optimal activity at pH 8.4 in 0.2M veronal buffer. The enzyme activity was completely lost by treatment at 60 degrees C for 15 min. The Km values were in the range from 2.38 to 4.55 X 10(-6)M FDP. Metal chelating agents inhibited enzyme activity, but monovalent or bivalent metal ions failed to stimulate the activity. Bivalent metal ions in general were rather inhibitory.
Hot Temperature, Cell-Free System, Species Specificity, Metals, Fructose-Bisphosphate Aldolase, Cysteine, Hydrogen-Ion Concentration, Chelating Agents, Rhizobium
Hot Temperature, Cell-Free System, Species Specificity, Metals, Fructose-Bisphosphate Aldolase, Cysteine, Hydrogen-Ion Concentration, Chelating Agents, Rhizobium
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