Table 1.

Kinetic constants for steady-state cleavage of pGln and pGlnCCA by E. coli M1 RNA, Synechocystis RNase P RNA wild type, and Synechocystis RNase P RNA CCA332

Enzyme	Substrate	Km, M × 106	kcat, min−1	kcat/Km, min−1⋅M−1 × 109
E. coli	pGln	3.0  ±  0.27	0.039  ±  0.0020	13.0
	pGlnCCA	0.13  ±  0.05	0.003  ±  0.0002	23.1
Synechocystis wild type	pGln	2.9  ±  0.25	0.008  ±  0.002	2.8
	pGlnCCA	350.6  ±  2.10	0.812  ±  0.012	2.3
Synechocystis CCA332	pGln	2.7  ±  0.45	0.004  ±  0.002	1.5
	pGlnCCA	126.5  ±  1.60	0.060  ±  0.005	0.5

K_m and k_cat were determined as described in Materials and Methods.