Catabolism of adenine nucleotides in suspension-cultured plant cells.
Profiles of the catabolism of adenine nucleotides in cultured plant cells were investigated. Adenine nucleotides, prelabelled by incubation of suspension-cultured Catharantus roseus cells with [8-14C]adenosine, were catabolized rapidly and most of the radioactivity appeared in 14CO2. Allantoin and allantoic acid, intermediates of the oxidative catabolic pathway of purines, were temporarily labelled. When the cells, prelabelled with [8-14C]adenosine, were incubated with high concentrations of adenosine, the rate of catabolism of adenine nucleotides increased. The results suggest that the relative rate of catabolism of adenine nucleotides is strongly dependent on the concentration of adenine nucleotides in the cells. Studies using allopurinol, coformycin and tiazofurin, inhibitors of enzymes involved in purine metabolism, suggest that participation of AMP deaminase and xanthine oxidoreductase in the catabolism of adenine nucleotides in plant cells. AMP deaminase was found in extracts from C. roseus cells and its activity increased significantly in the presence of ATP. In contrast, no adenosine deaminase or adenine deaminase activity was detected. Qualitative differences in the catabolic activity of AMP were observed between suspension-cultured cells from different species of plants.
Yabuki
N
N
Department of Biology, Faculty of Science, Ochanomizu University, Tokyo, Japan.
Ashihara
H
H
D000659:AMP Deaminase / Q000378:metabolism; D000227:Adenine Nucleotides / Q000378:metabolism*; D000241:Adenosine / Q000378:metabolism; D000243:Adenosine Deaminase / Q000378:metabolism; D000619:Aminohydrolases / Q000378:metabolism; D002478:Cells, Cultured; D010944:Plants / Q000378:metabolism*
D000227:Adenine Nucleotides; D000619:Aminohydrolases; C018774:adenine deaminase; D000243:Adenosine Deaminase; D000659:AMP Deaminase; D000241:Adenosine