. Author manuscript; available in PMC: 2016 Sep 1.

Published in final edited form as: Hum Mutat. 2015 Jul 24;36(9):881–893. doi: 10.1002/humu.22823

Table 4.

ChAT Kinetic parameters of wild type and mutant ChAT enzymes^a

	k_cat, s⁻¹	$K_{m}^{A c C o A}$ μM	$K_{m}^{c h o l i n e}$ μM	k_cat/ $K_{m}^{A c C o A}$	k_cat/ $K_{m}^{A c C o A}$ · $K_{m}^{c h o l i n e}$
Wild-type	281.9 ± 3.5	22.7 ± 1.8	396 ± 24	1.00	1.00
p.Val136Met	223.0 ± 2.6	27.4 ± 1.3	432 ± 31	0.65	0.71
p.Arg186Trp	1 3.7 ± 1.1	7.3 ± 1.3	224 ± 27	0.15	0.10
p.Val194Leu	608.2 ± 16	88 ± 7.4	565.8 ± 32	0.55	0.79
p.Arg207His	0.80 ± 0.05	4.53 ± 8.7	442 ± 21	0.02	0.03
p.Pro211Ala	488.7 ± 12.4	96.1 ± 5.3	425 ± 11	0.41	0.44
p.Arg566Cys	103.7 ± 6.9	37.1 ± 5.7	721 ± 23	0.23	0.45
p.Ser694Cys	135.8 ± 9.5	31.0 ± 2.3	831 ± 18	0.35	0.73

Values indicate estimate ± standard error. Catalytic efficiency (k_cat/ $K_{m}^{A c C o A}$ ) is normalized with respect to wild type. The overall catalytic efficiency [k_cat/ $K_{m}^{A c C o A}$ · $K_{m}^{c h o l i n e}$ ] is normalized with respect to wild type.