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. 2014 Feb 4;289(11):7691–7701. doi: 10.1074/jbc.M113.535567

TABLE 1.

Kinetic parameters of Rickettsial methyltransferases

The steady state kinetics was monitored by the incorporation of radioactive [methyl-3H] from [methyl-3H]AdoMet into OmpB(AN) as described under “Materials and Methods.” The final concentration of methyltransferase was 0.26 μm.

Methyltransferase KmAN kcat kcat/Km
μm s1 m1·s1
RT0101 0.48 ± 0.057 0.83 × 10−3 1.74 × 103
RP027-028a 10.1 ± 1.63 0.16 × 10−3 0.015 × 103
RP789 0.29 ± 0.093 5.98 × 10−3 20.6 × 103
RP789ΔN 1.13 ± 0.17 3.32 × 10−3 2.93 × 103
RT0776 1.71 ± 0.182 2.20 × 10−3 1.28 × 103
RT0776ΔN 3.07 ± 1.55 4.45 × 10−3 1.45 × 103

a RP027-028-catalyzed methylation was analyzed at 2 μm RP027-028 and 2–20 μm OmpB(AN) because of the low enzyme efficiency.