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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.
J Hordern, and
R H Johnson, and
B D McLennan
January 1972,
Journal of medicine,
J Hordern, and
R H Johnson, and
B D McLennan
December 1974,
Canadian journal of biochemistry,
J Hordern, and
R H Johnson, and
B D McLennan
July 1975,
Biochemical and biophysical research communications,
J Hordern, and
R H Johnson, and
B D McLennan
January 1968,
Biochemistry,
J Hordern, and
R H Johnson, and
B D McLennan
January 1972,
Biochemical pharmacology,
J Hordern, and
R H Johnson, and
B D McLennan
March 1977,
Plant physiology,
J Hordern, and
R H Johnson, and
B D McLennan
August 2008,
Plant cell reports,
J Hordern, and
R H Johnson, and
B D McLennan
December 1971,
Plant physiology,
J Hordern, and
R H Johnson, and
B D McLennan
November 1981,
The Journal of biological chemistry,
J Hordern, and
R H Johnson, and
B D McLennan
November 1971,
Analytical biochemistry,
