. Author manuscript; available in PMC: 2010 Jul 16.

Published in final edited form as: Biochemistry. 2008 Mar 26;47(16):4808–4816. doi: 10.1021/bi702494q

Table 1.

Apparent Kinetic Parameters for Aminoacylation^a

Deletion mutants	K_M(µM)	k_cat (s⁻¹)	k_cat/K_M (µM¹ s⁻¹)	Relative k_cat/K_M
Wild type	1.2 ± 0.2	14.3 ± 0.3	11.9	1
N-terminal β-strand
ΔS₂₂₇E₂₂₈	ND^b	ND^b	ND^b	-
ΔS₂₂₇	ND^b	ND^b	ND^b	-
ΔE₂₂₈	ND^b	ND^b	ND^b	-
ΔG₂₂₉V₂₃₀	0.94 ± 0.4	9.2 ± 2.7	9.7	0.8
ΔE₂₃₁I₂₃₂	1 ± 0.1	10.2 ± 4	10.2	0.9
ΔT₂₃₃F₂₃₄	2.3 ± 0.5	39.1 ± 3.3	17	1.4
C-terminal β-strand
ΔG₄₀₇V₄₀₈	0.9 ± 0.2	12.5 ± 1	13.8	1.2
ΔG₄₀₉E₄₁₀	0.6 ± 0.1	6.9 ± 1.2	11.5	1
ΔR₄₁₁K₄₁₂	2.1 ± 0.5	35.2 ± 3.5	16.7	1.4
ΔV₄₁₃N₄₁₄	1.7 ± 0.6	4.5 ± 0.3	2.7	0.2
ΔV₄₁₃	0.7 ± 0.2	0.2 ± 0.05	0.3	0.02
ΔN₄₁₄	2.8 ± 0.5	0.6 ± 0.3	0.2	0.02

The kinetic parameters that are reported are apparent values.

ND – Not determined because of low activity.