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. 2010 Jan 20;285(12):8995–9007. doi: 10.1074/jbc.M109.069203

TABLE 1.

Km and Vmax values of ACER2 for different substrates

Δypc1Δydc1ACER2 microsomes (40 μg of proteins per reaction) were measured for ceramidase activity at pH 9.0 using different concentrations of various ceramides as substrates in the presence of Triton X-100 (0.15%, v/v) and CaCl2 (1 mm). The apparent Km and Vmax values were computed according to nonlinear regression by GraphPad Prism software. Data represent mean ± S.D. of three independent experiments.

Substrates Km Vmax Vmax/Km
μm/mol % pmol/min/mg μm
C6:0-Cer 224.16 ± 37.51/8.45 ± 1.41 5.04 ± 0.72 0.02 ± 0.00
C12:0-Cer 133.83 ± 17.88/5.05 ± 0.67 10.67 ± 1.54 0.08 ± 0.02
C14:0-Cer 114.61 ± 13.28/4.32 ± 0.50 11.37 ± 1.41 0.10 ± 0.03
C16:0-Cer 98.52 ± 11.79/3.71 ± 0.44 23.70 ± 3.18 0.24 ± 0.03
C18:0-Cer 94.81 ± 10.06/3.57 ± 0.38 26.11 ± 3.47 0.28 ± 0.05
C18:1-Cer 77.31 ± 8.43/2.91 ± 0.32 35.42 ± 5.10 0.46 ± 0.07
C20:0-Cer 91.47 ± 9.79/3.45 ± 0.37 28.94 ± 3.61 0.32 ± 0.04
C20:1-Cer 72.11 ± 8.52/2.71 ± 0.32 38.16 ± 4.74 0.53 ± 0.08
C24:0-Cer 143.2 ± 18.16/5.39 ± 0.68 6.74 ± 0.87 0.05 ± 0.00
C24:1-Cer 81.40 ± 10.21/3.06 ± 0.38 27.07 ± 3.78 0.33 ± 0.06