Table 1 Kinetic constants for macromolecular or peptidyl substrate cleavage and prothrombinase assembly

From: Engineered factor Xa variants retain procoagulant activity independent of direct factor Xa inhibitors

 

Prothrombina

Prothrombina

Cofactor Vaa

S2765a

S2765a

S2765b

S2765b

 

K m (µM)

k cat (min−1)

K d, app (nM)

K m (µM)

k cat (s−1)

K m (µM)

k cat (s−1)

pd-FXa

0.31 ± 0.07

1880 ± 136

0.41 ± 0.05

59 ± 19

47 ± 4

 29 ± 8

36 ± 3

wt-FXa

0.41 ± 0.08

1243 ± 89

1.44 ± 0.41

33 ± 7

27 ± 2

 26 ± 8

 21 ± 2

FXa-A

0.14 ± 0.04

 122 ± 8

0.81 ± 0.26

39 ± 7

 9 ± 1

243 ± 50

  11 ± 1

FXa-B

0.25 ± 0.07

 239 ± 20

0.85 ± 0.28

49 ± 8

10 ± 1

249 ± 29

 15 ± 1

FXa-C

0.22 ± 0.04

 370 ± 19

0.57 ± 0.06

60 ± 11

17 ± 1

 216 ± 28

 21 ± 1

  1. The kinetic constants for the enzyme aprothrombinase or bFXa were obtained as described in ‘Methods’. Fitted values ± 1 standard deviation of the induced fit are representative of two to three independent experiments
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