. 2014 Jul 21;53(31):5150–5161. doi: 10.1021/bi5007404

Table 3. P5CDH Kinetic and NAD⁺ Binding Parameters.

BjPutA	k_cat (s^–1)^a	K_m (mM)^a	k_cat/K_m (M^–1 s^–1)	K_d (μM, NAD⁺)^b
wild-type	3.4 ± 0.1	0.42 ± 0.04	8095 ± 822	0.60 ± 0.04
T348Y	4.2 ± 0.2	0.42 ± 0.04	10000 ± 1017	0.75 ± 0.06
S607Y	4.5 ± 0.2	0.48 ± 0.03	9375 ± 664	1.00 ± 0.04
D778Y	3.8 ± 0.1	0.38 ± 0.02	10000 ± 567	0.67 ± 0.04
D779A	5.0 ± 0.1	0.38 ± 0.03	13157 ± 1102	0.64 ± 0.05
D779Y	0.02 ± 0.01	0.20 ± 0.03	100 ± 16	0.65 ± 0.04
D779W	0.003 ± 0.001	0.35 ± 0.15	8.6 ± 4	0.78 ± 0.05

Mixture of 0.01–6 mM L-P5C, 0.2 mM NAD⁺, 0.25 μM enzyme, and 50 mM potassium phosphate (pH 7.5, 600 mM NaCl).

From fluorescence quenching with 0.1–25 μM NAD⁺, 0.25 μM enzyme, and 50 mM potassium phosphate (pH 7.5).

Table 3. P5CDH Kinetic and NAD+ Binding Parameters.