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. 2002 Nov 12;99(24):15339–15344. doi: 10.1073/pnas.242604099

Table 1.

Summary of the rate constants and extents for the interaction of nucleotides with wild-type and salt-bridge mutant HMMs

Measurements Parameters Wild-type R247A R247E E470A E470R R247E/E470R
MantATP binding Fast, % 100 82 93 87 58 91
K1k+2 (s−1⋅M−1) 3.5 × 105 0.49 × 105 0.28 × 105 4.5 × 105 5.7 × 105 2.2 × 105
Slow, % 33
kslow, s−1 0.0001
Trp fluorescence Increase, % 19 1.8 1.1 16 4 (6.7) 15
K1k+2 (s−1⋅M−1) 2.5 × 105 0.33 × 105 0.23 × 105 3.1 × 105 4.5 × 105 1.6 × 105
kmax, s−1 166  92 172
K0.5, μM 650 330 980
Phosphate burst Mole per mole of HMM head 0.68 0 0   0 0   0
MantATP release k+3 or k+3k+4/(k+3 + k−3), s−1 0.009 0.003 0.0011 0.00014 0.000036 0.001
MantADP release k+5, s−1 1.3 0.027 0.0036 0.28 0.34 0.031
Steady-state ATPase kcat, s−1 0.005 0.002 0.0005 0.00008 0.00003 0.0004
Actin-activated ATPase kmax, s−1 1.9 0 0 0 0 0
Kactin, μM 120
*

Conditions: 0.45 M KCl, 3 mM MgCl2, 1 mM EDTA, 20 mM Tris⋅HCl (pH 7.5) at 20°C.

The estimated increase for E470R of which sites are vacant.

Conditions: 200 μM F-actin, 0.04 mM KCl, 2 mM MgCl2, 20 mM Tris⋅HCl (pH 7.5) at 25°C.