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. 2010 May 10;38(17):5774–5783. doi: 10.1093/nar/gkq336

Table 2.

Kinetic data for glutamylation activity of M. thermautotrophicus ND-GluRS for tRNAGln

Enzyme KM (µM) kcat (min−1) kcat/KM (min−1/µM)
GluRS 2.1 ± 0.4 0.7 ± 0.1 0.3 ± 0.1
GluRS + GatDEa 2.4 ± 0.6 0.6 ± 0.1 0.3 ± 0.1
GluRS + BSAb 2.4 ± 0.5 0.6 ± <0.1 0.3 ± 0.1

Measurements were from three to four separate experiments. Standard deviations are reported. Reactions with M. thermautotrophicus ND-GluRS (50 nM) were carried out as described in the ‘Materials and Methods’ section at 37°C in the presence of excess ATP (4 mM), Glu (1 mM) and Asn (2 mM). The concentration of tRNAGln varied from 0.31 µM up to 15 µM.

aGatDE (2.0 µM) or bBSA (2.0 µM) was added to the reaction mix.