. 2009 Sep 4;37(19):6503–6514. doi: 10.1093/nar/gkp711

Table 1.

ATPase activities of DbpA with 32-mer RNA with and without the 2′-O-methyl at U2552

	k_max (min⁻¹)	K_app,RNA(nM)
32-mer	45 ± 3.6	220 ± 32
2′-O-methyl 32-mer	43 ± 2.6	230 ± 31

The K_app,RNA and k_max values were measured in the presence of saturating (5 mM) ATP, 60 nM DbpA and 0–2 μM RNA in buffer (50 mM Hepes pH 7.5, 10 mM MgCl₂, 50 mM KC1, 100 μM DTT, 200 μM NADH, 1 mM phospho(enol)pyruvate and 10 mM phosphate kinase/lactate dehydrogenase) at 24°C. Lines were fit to the Michaelis–Menten equation.