N-6-(delta-2-isopentenyl) adenosine: hydrolysis by a mucleosidase isolated from Lactobacillus acidophilus cells.
A nucleosidase activity has been isolated from Lactobacillus acidophilus which rapidly hydrolyses N-6 (delta-2-isopentenyl) adenosine to its corresponding base, N-6(delta-2-isopentenyl) adenine. The activity can be distinguished from the spleen exzyme (EC. 2.4.2.1), a purine nucleoside transferase, on the basis of its substrate specificity, electrophoretic behavior, and nondependence on phosphate. The bacterial enzyme hydrolyzes both inosine and isopentenyl adenosine, giving Km values of 63.3muM and 177 muM respectively. The presence of this enzyme in bacteria counts for the rapid conversion of the parent nucleoside to isopentenyl adenine, which has been observed in these cells. The enzyme thus assumes importance as one of the catabolic activities available to the cell for metabolizing the cytokinin, N-6-(delta-2-isopentenyl) adenosine.
D000241:Adenosine / Q000031:analogs & derivatives*; D006863:Hydrogen-Ion Concentration; D007541:Isopentenyladenosine / Q000378:metabolism*; D007700:Kinetics; D007779:Lactobacillus acidophilus / Q000201:enzymology*; D008970:Molecular Weight; D009699:N-Glycosyl Hydrolases / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism
D007541:Isopentenyladenosine; D009699:N-Glycosyl Hydrolases; D000241:Adenosine