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. 2011 Aug 3;39(21):9306–9315. doi: 10.1093/nar/gkr619

Table 1.

Kinetic constants of GluRS2 for tRNAGln glutamylation and of GatCAB for Glu-tRNAGln transamidation in the absence or in the presence of the second protein

KM (µM) kcat (s−1)
GluRS2 0.87 ± 0.13 0.094 ± 0.004
GluRS2 + GatCAB 1.86 ± 0.19 0.24 ± 0.009
GluRS2 + GatCAB 0.69 ± 0.15 0.23 ± 0.015
GatCAB 0.42 ± 0.11 0.21 ± 0.011
GatCAB + GluRS2 1.34 ± 0.38 0.21 ± 0.014
GatCAB + GluRS2 0.97 ± 0.30 0.23 ± 0.019

Constants were measured using the assay for the first enzyme indicated. When present as the second enzyme, GatCAB and GluRS2 were in equimolar amounts (normal font), or in excess 330- and 440-fold, respectively (in bold). Reported KM values are for tRNAGln in all experiments except GatCAB alone and with an excess of GluRS2, in which they were for Glu-tRNAGln. Errors shown are the standard errors for non-linear curve-fitting of data obtained from at least two experiments.