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. Author manuscript; available in PMC: 2018 Oct 5.
Published in final edited form as: Chembiochem. 2017 Aug 15;18(19):1928–1934. doi: 10.1002/cbic.201700343

Table 2.

Kinetic parameters for tRNATyr aminoacylation by TyrRS and its variants.

kcat [s−1] KM,tRNA [μM] kcat/KM,tRNA [s−1μM−1]
wild-type 1.32 ± 0.23 0.37 ± 0.04 3.51
85AcK 0.15 ± 0.06 0.45 ± 0.05 0.33
144AcK 1.17 ± 0.37 0.42 ± 0.07 2.78
235AcK n.d.[a] n.d. n.d.
238AcK n.d. n.d. n.d.
355AcK 1.09 ± 0.29 0.48 ± 0.14 2.27
[a]

n.d.: not determined due to undetectable activities of TyrRS-235AcK and -238AcK. Mean values and standard deviations were calculated based on three replicates.