The characteristics of adenosinetriphosphatase (ATPase) and inorganic pyrophosphatase (PPase) in the tonoplasts isolated from leaf mesophyll homogenates of Ananas comosus (pineapple), a hexose-utilizing species with high PPi-PFK activities, and Kalancho(j pinnata and K daigremontiana, starch-utilizing species with high ATP-PFK activities, were investigated. The ATPase and nitrate-sensitive ATPase (L1N0 3 --ATPase) activities were higher than the PPase activity of pineapple, but the reverse was the case in the two Kalancho£:' species. The optimum pH for L1N0 3 --ATPase in pineapple, K. daigremontiana and K pinnata was 7 .0,....,_.8.25, 7 .5,....,_.8.25 and 7 .5,....,_.8.25, respectively, and that for PPase was 6.5...._,7.5 in all species. The Km of L1N0 3 --ATPase for Na 2 -ATP for pineapple, K daigremontiana and K pinnata was 0.47, 0.48 and 0.43 mM, respectively, and V max was 52.6, 27.0 and 40.0 ,umol Pi mg-1 protein h-1 , respectively.The optimum MgS0 4 and Na 4 PP 1 concentrations for the PPase activity of the three CAM species were approximately 2 mM and 0.16 mM, respectively. The optimum temperature for the L1N0 3 --ATPase in pineapple, K daigremontiana and K. pinnata was 35----43, 35,...,.,.,40 and 37°C, respectively, and that for PPase was 46,....,_.49°C. In addition, at a high temperature, the decrement of tonoplast L1N0 3 --ATPase and PPase activities in pineapple was less than that in the two Kalanchoe· species. Thus, pineapple obviously maintained high tonoplast L1N0 3 --ATPase and PPase activities at high temperatures.