Table 1

Kinetic data for mouse acetylcholinesterase (AChE) [22]

No

Mutation

kon TFK+ (1011 M-1min-1)

kcat/Km ATCh (108 M-1min-1)

Km ATCh (μM)


00

WT

9.8 ± 0.6

30

46 ± 3

01*

D74N

0.39 ± 0.01

0.65

1300 ± 140

02*

E450Q

1.2 ± 0.1

0.24

140 ± 10

03*

E202Q

7.9 ± 0.4

4.3

200 ± 40

04*

D74N/E202Q/E450Q

-

0.0022

18000 ± 2500

05

D280V

8.2 ± 2.0

16

73 ± 4

06

D280V/D283N

7.6 ± 0.3

23

60 ± 9

07

E84Q/E91Q/D280V/D283N/D372N

2.3 ± 0.1

5.1

162 ± 6

08

E84Q/E91Q/D280V/D283N/E292Q/D372N

1.8 ± 0.1

2.3

230 ± 32

09

E84Q/E91Q/D280V/D283N

4.3 ± 0.8

4.6

240 ± 52

10*

D74N/E202Q

0.14 ± 0.01

0.34

700 ± 29

11*

D74N/D280V/D283N

0.31 ± 0.02 #

0.23

1600 ± 320


The data are for wild-type and 11 mutant AChEs interacting with the inhibitor TFK+ and the substrate ATCh. Active site mutants are marked by an asterisk; mutant no. 11 has a combination of active site and surface residue mutations.

#The value published in reference [22] for this parameter is 10 times larger due to a typographical error [Z. Radic, personal communication].

Gabdoulline et al. BMC Bioinformatics 2007 8:373   doi:10.1186/1471-2105-8-373

Open Data