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. 2009 Nov 30;285(5):3064–3075. doi: 10.1074/jbc.M109.000810

TABLE 1.

Steady-state catalytic activities of nNOS and the Lys842 mutants

Rates were measured at 25 °C as described under “Experimental Procedures.” Values represent the mean ± S.D. of three independent measurements with two preparations of each enzyme. ND, not detected.

Enzyme CaM NO synthesis NADPH Oxidation Cytochrome c reduction K3Fe(CN)6 reductase
min1 min1 min1 min1
nNOS WT + 42 ± 2.9 168 ± 2.2 4941 ± 100 10486 ± 796
ND 4.6 ± 0.1 511 ± 13 7825 ± 252
K842A + 32 ± 2.2 114 ± 2.1 3417 ± 12 9098 ± 314
ND 18 ± 0.2 754 ± 38 7294 ± 209
K842E + 40 ± 1.5 186 ± 0.5 4547 ± 220 10087 ± 283
ND 23 ± 0.2 1471 ± 81 7104 ± 265