. Author manuscript; available in PMC: 2018 Nov 29.

Published in final edited form as: Methods Enzymol. 2018 Jun 1;606:485–522. doi: 10.1016/bs.mie.2018.04.014

Table 1.

Steady-State Kinetic Parameters of MoaA and MoaC From Different Organisms (Hover et al., 2013, 2015)

Enzyme	Organism	Tag	Substrate	K_m (μM)	K_cat (min⁻¹)
MoaA	S. aureus	His-tagged	GTP	1.4 ± 0.2	0.045 ± 0.003
			SAM	4.1 ± 1.3	0.043 ± 0.004
MoaC	S. aureus	His-tagged	3′,8-cH₂GTP	<0.060	0.17 ± 0.026
	E. coli	His-tagged	3′,8-cH₂GTP	0.21 ± 0.058	0.56 ± 0.027
		Nontagged	3′,8-cH₂GTP	0.25 ± 0.040	0.53 ± 0.061
MOCS1B	Homo sapiens	His-tagged	3′,8-cH₂GTP	0.79 ± 0.24	0.092 ± 0.020