. Author manuscript; available in PMC: 2018 May 18.

Published in final edited form as: Biochemistry. 2017 Jul 7;56(28):3539–3548. doi: 10.1021/acs.biochem.7b00450

Table 2.

Comparison of PRMT3 and PRMT8 kinetic parameters for arginine methylation.

Enzyme	Substrate	k_cat (min⁻¹)	K_0.5 (μM)	n	k_cat/K_0.5 (min⁻¹ μM⁻¹)
PRMT3	Ac-H4(1-20)	0.21 ± 0.0050	1.0 ± 0.049	2.0 ± 0.16	0.21
	Ac-H4(1-20)K5_me	0.63 ± 0.029	0.76 ± 0.070	3.0 ± 0.68	0.83
	Ac-H4(1-20)K5_ac	0.14 ± 0.0056	2.3 ± 0.15	1.8 ± 0.14	0.061
PRMT8	Ac-H4(1-20)	0.21 ± 0.0070	1.2 ± 0.10	1.6 ± 0.17	0.18
	Ac-H4(1-20)K5_me	0.21 ± 0.0032	0.42 ± 0.010	2.7 ± 0.18	0.50
	Ac-H4(1-20)K5_ac	0.12 ± 0.015	4.5 ± 1.2	1.1 ± 0.16	0.027

35 min reactions with 0.05 μM [E] and 15 μM [¹⁴C]-SAM