Table 2 Kinetic Parameters for ATP11-CDC50A Complexes.

From: Proteomic Analysis and Functional Characterization of P4-ATPase Phospholipid Flippases from Murine Tissues

Substrate

ATP11A

ATP11B

ATP11C

ATP8A2‡

ATP8A1§

PS

  KA (µM)

87 ± 23

178 ± 19

69 ± 13

38 ± 1

39 ± 4

  Vmax

15.1 ± 1.1

17.3 ± 0.6

34.9 ± 1.7

160 ± 6#

38.7 ± 1

PE

  KA (µM)

240 ± 40

5470 ± 1200

2650 ± 1120

371 ± 13

887 ± 111

  Vmax

12.2 ± 0.6

25.2 ± 4.4

48.4 ± 13.7

67 ± 3

26.8 ± 1.5

ATP

  Km (µM)

200 ± 50

730 ± 190

1440 ± 110

704 ± 7

267 ± 5

  Vmax

9.6 ± 0.4

9.5 ± 0.7

48.3 ± 1.5

57 ± 2

37.6 ± 2

  1. Data is the mean ± SEM. Vmax is in µmoles ATP hydrolyzed per min per mg protein.
  2. ‡Data from ref.19,33.
  3. #Vmax for PS activation of ATP8A2 varies from 80–160 µmoles ATPase hydrolyzed per min per mg protein.
  4. §Data from ref.34.
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