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. Author manuscript; available in PMC: 2009 Dec 25.
Published in final edited form as: J Phys Chem B. 2008 Dec 25;112(51):16741–16751. doi: 10.1021/jp807067g

Table 1.

Numerical values for the thermodynamic and kinetic parameters obtained from fits of the activity data to eq. 12 together with eq. 19 and 20.

phospholipid
g1RT
(a)
KM0/10−6 (Mm−2)(b) KM00/10−7 (Mm−2)(c) KS0 (mM)(d) k3 (μmol/min/mg)
DLPC (11.3±5.4) 1.34±0.14 5.12±0.19 0.92±0.23 4797±964
DMPC (12.8±1.6) 2.55±0.03 3.18±0.12 1.28±0.03 3333±80
DPPC (17.1±0.6) 7.50±0.91 8.53±0.94 1.24±0.03 3723±590
(a)

g1 is the coefficient of the free energy of activation for lipid-enzyme binding as defined by eq. 17 and Fig. 4b.

(b)

KM0=k3k20 (eq. 19 and 18)

(c)

KM00=k20k20 (eq. 19 and 18)

(d)

KS0=k1k1 (eq. 20)