[Adenosine-3':5'-monophosphate phosphodiesterase from Rhizobium].
The phosphodiesterase (PDE) activity of adenosine-3':5'-monophosphate was detected in the cells of tubercular bacteria of Rhizobium lupini and Rhizobium japonicum. The specific activity of three Rhizobium forms, e.g. bacteroids from lupine root tubercles, free-nitrogen-fixing culture and vegetative cells grown on a mannitol--yeast agar, were compared. In the bacteroids PDE is represented both by soluble and membrane-bound forms. The optimal enzyme activity is revealed in an alkaline medium, whereas the curve of PDE activity dependence on pH has a broad maximum. PDE is inhibited by methylxanthines, the inhibiting effect being stronger than that of theophylline.
D015105:3',5'-Cyclic-AMP Phosphodiesterases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009586:Nitrogen Fixation; D012231:Rhizobium / Q000201:enzymology*; D013045:Species Specificity
D015105:3',5'-Cyclic-AMP Phosphodiesterases
Fosfodiésteraza adenozin-3':5'-monofosfata u Rhizobium.