qPIPSA: Relating enzymatic kinetic parameters and interaction fields

BMC Bioinformatics

Table 1 Kinetic data for mouse acetylcholinesterase (AChE) [22]

No	Mutation	k_on TFK+ (10¹¹ M^-1min^-1)	k_cat/K_m ATCh (10⁸ M^-1min^-1)	K_m 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].

ISSN: 1471-2105