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. Author manuscript; available in PMC: 2009 Oct 14.
Published in final edited form as: Biochemistry. 2008 Sep 20;47(41):10933–10939. doi: 10.1021/bi8008278

Table 2.

Steady state kinetic constants measured for TMEGF45 mutants

Protein KD, (nM)1 TMEGF45 KM,TM(nM) TMEGF45 KM,PC(∝M) TMEGF45 kcat(s-1) TMEGF45
wild type 68 140±12 0.32±0.1 5.0±0.1
D349N 43 440±38 0.77±0.2 0.69±0.01
E357Q 55 149±29 1.0±0.2 0.36±0.06
E357D ND 542±41 0.62±0.26 0.22±0.02
Y358A ND 623±100 1.3±0.3 0.08±0.003
Y358H ND 163±16 1.6±0.16 0.2±0.02
Y358W ND 61±9 0.8±0.5 5.6±1.6
F376W ND 208±19 0.9±0.14 15±4
M388L 57 140±40 0.38±0.1 7.8±0.5
D400N ND 616±131 0.7±0.04 0.04±0.001
D400E 49 237±16 1.36±0.1 0.17±0.01
1

Kd was determined by Scatchard analysis of the fluorescein-EGR-chloromethylketone-labeled thrombin binding data.