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. Author manuscript; available in PMC: 2005 Oct 5.
Published in final edited form as: J Biol Chem. 2005 May 24;280(28):26099–26104. doi: 10.1074/jbc.M503539200

Table IV.

Steady-state aminoacylation kinetics of M. thermautotrophicus LeuRS

Enzymea Additionsb kcat/Km Leu kcat/Km tRNALeu
s1 μm1
LeuRS BSA 0.35 ± 0.07 0.75 ± 0.08
LeuRS ProRS, BSA 0.37 ± 0.09 0.75 ± 0.03
a

Enzymes were added at a final concentration of 40 nm.

b

Other components at 400 nm each. Due to the high Km compared to practical tRNA concentrations ([S] ≪ Km), kcat/Km was directly estimated from the equation v = kcat / Km ([E] [S]).