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. Author manuscript; available in PMC: 2010 Aug 2.

Published in final edited form as: Biochemistry. 2006 Aug 1;45(30):9074–9084. doi: 10.1021/bi060567d

Table 2.

Kinetics of mant-ATP binding to PKR.

Enzyme Form	Association Kinetics			Dissociation Kinetics^a
	k_obs, ₁ : Slope (μM⁻¹·s⁻¹)^b	k_obs, ₁ :Intercept (s⁻¹)^c	k_obs, ₂: Average (s⁻¹)^d	k_obs, ₁ (s⁻¹)	k_obs, ₂ (s⁻¹)
Unphosphorylated	6.25 ± 0.35	206 ± 11	48.9 ± 9.9	175 ± 2	43.1 ± 5.5
Phosphorylated	4.75 ± 0.40	239 ± 14	43.2 ± 4.9	214 ± 5	56.0 ± 0.8
K296R	5.56 ± 0.38	91 ± 13	39.7 ± 5.7	134 ± 4	18.6 ± 0.1
Unphos. + 40mer dsRNA	5.36 ± 0.50	232 ± 16	36.5 ± 8.1	175 ± 1	23.2 ± 5.5

^a

Dissociation kinetics measured upon addition of 2 mM unlabeled ATP.

^b

Slope from linear fit of _kobs,1 vs. [mant-ATP].

^c

Y-intercept from linear fit of _kobs,1 vs. [mant-ATP].

^d

Average value of _kobs,2 over the entire range of [mant-ATP].