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. Author manuscript; available in PMC: 2022 Nov 21.
Published in final edited form as: Biochemistry. 2017 Jul 7;56(28):3619–3631. doi: 10.1021/acs.biochem.7b00114

Table 1.

Steady state aminoacylation kinetics of tRNAHis by human and bacterial histidyl-tRNA synthetases


Variable Substrate

tRNA histidine

Enzyme Km (μM) kcat (s−1) kcat/Km (μM−1 s−1) Km (μM) kcat (s−1) kcat/Km (μM−1 s−1) References
WT HARS 1.2 ± 0.5 3.9 ± 0.6 3.2 ± 1.0 8.0 ± 4.0 4.1 ± 0.4a 0.5 ± 0.4 This work
Y454S HARS 0.9 ± 0.2 4.4 ± 0.3 5.1 ± 1.0 4.7 ± 2.5 5.9 ± 0.5a 1.2 ± 0.4 This work
E. coli HisRS 0.34 ± 0.05 1.71 ± 0.06 5.0 35 ± 4b 133 ± 2b 3.8b 16

Values reported are the mean ± standard error of three independent experiments.

a

Significantly different (extra sum-of-squares F test) p<0.05.

b

Data are for histidine in the pyrophosphate exchange reaction.