. Author manuscript; available in PMC: 2015 Apr 15.

Published in final edited form as: Biochemistry. 2008 Mar 13;47(14):4228–4236. doi: 10.1021/bi800023a

Table 4.

Kinetic Parameters for the Reduction of DDsaACP by Wild Type and Mutant FabIs

Enzyme	k_cat (min⁻¹)	NADPH		DDsaACP
Enzyme	k_cat (min⁻¹)	K_m (μM)^a	k_cat/K_m (min⁻¹ μM⁻¹)^a	K_m (μM^b	k_cat/K_m (min⁻¹ μM⁻¹)^b
WT	130.2 ± 9.1	70.8 ± 6.0	1.8 ± 0.3	4.5 ± 0.5	29.5 ± 5.0
A95V	18.4 ± 0.1	269.4 ± 29.2	0.007 ± 0.001	11.4 ± 1.6	1.7 ± 0.2
I193S	-	> 1000	0.13 ± 0.02	-	5.1 ± 0.4
F204S	157.3 ± 7.2	429.6 ± 45.0	0.17 ± 0.02	18.4 ± 1.3	7.8 ± 0.7

Reactions were carried out with 20 μM DDsaACP;

reactions were carried out with 300 μM NADPH.