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. Author manuscript; available in PMC: 2008 Aug 17.
Published in final edited form as: Biochemistry. 2006 Jun 20;45(24):7463–7473. doi: 10.1021/bi0602314

Table 2.

Kinetic parameters with respect to AdoMet in the methyl transferase reaction

kcat (min-1) Km(μM) kcat/Km (μM-1min-1) Relative kcat/Km
Wild-type Trm5 0.73 ± 0.01 1.0 ± 0.1 0.7 ± 0.1 1.0
P267A 0.006 ± 0.001 0.5 ± 0.04 0.01 ± 0.003 0.02

Kinetics of the wild-type Trm5 and P267A mutant was assayed with 0.2 μM enzyme, 6 μM tRNACys, and AdoMet ranging in 0.5-15 μM. The kcat and Km values are the average of at least 3 independent measurements.