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Table 1 Kinetic analysis of in vitro lipid kinase activity of p110 αEEWT/p85 α, p110 αEEE545K/p85 α and p110 αEEH1047R/p85 α

From: Autophosphorylation of serine 608 in the p85 regulatory subunit of wild type or cancer-associated mutants of phosphoinositide 3-kinase does not affect its lipid kinase activity

 

Wild type

E545K

H1047R

PI kinase activity a

V max b

35 ± 13c

118 ± 12

150 ± 13

 

K m (μM)

23 ± 3

22 ± 6

14 ± 7

PI-(4,5)-P 2 kinase activity

V max

35 ± 8

117 ± 13

146 ± 15

 

K m (μM)

22 ± 5

19 ± 6

9 ± 3

  1. aPI or PI-(4,5)-P2 were used as substrates to generate PI-3-P or PI-(3,4,5)-P3.
  2. bMichaelis-Menten kinetic parameters (substrate affinity (Km) and maximum reaction velocity (Vmax)) for the production of PI-3-P or PI-(3,4,5)-P3 were calculated from assays in which the concentration of ATP was varied.
  3. cKm and Vmax are shown as mean ± SEM, n = 4.