. 2022 Nov 22;61(23):2766–2775. doi: 10.1021/acs.biochem.2c00531

Table 2. Third-Order Rate Constants (Scheme 4) for EA Activation of RAdK- and HAdK1-Catalyzed Phosphoryl Transfer from ATP to Dianions^a.

enzyme	dianion substrate	(k_cat)_XP·Act/K_XPK_Act (M^–2 s^–1)
Rabbit Muscle (k_cat/K_m)_AMP = 1.2 × 10⁶ M^–1 s^–1^b	HPO₃^2–^d	220 ± 10
Rabbit Muscle (k_cat/K_m)_AMP = 1.2 × 10⁶ M^–1 s^–1^b	FPO₃^2–^e	55 ± 3
Human (k_cat/K_m)_AMP = 7.0 × 10⁶ M^–1 s^–1^c	HPO₃^2–^c	260 ± 7
	FPO₃^2–^f	47 ± 0.5
	HOPO₃^2–^g	9.6 ± 1.0

Determined at pH 7.5 and 25 °C in 25 mM TEA buffer at I = 0.15 (NaCl). The uncertainty in the kinetic parameters is the standard error from the least-squares fits of the kinetic data to eq 3.

Table 1.

Published data.²³

Determined for data from Figure 2.

Determined for data from Figure S3A,B.

Determined for data from Figure 3A,B.

Determined for data from Figure 4A,B.

Table 2. Third-Order Rate Constants (Scheme 4) for EA Activation of RAdK- and HAdK1-Catalyzed Phosphoryl Transfer from ATP to Dianionsa.

Table 2. Third-Order Rate Constants (Scheme 4) for EA Activation of RAdK- and HAdK1-Catalyzed Phosphoryl Transfer from ATP to Dianions^a.