Table 4Apparent destabilization of the initial complex(ΔΔGs) and of the transition state complex (ΔΔGT) for the charging of Eco-tRNATyr by Bst-TyrRSa

MutationΔΔGS ΔΔGT
T17A-0
N146A++++0
K151Nb 0++++
E152Ac --
W196Ad +++++
R207Qnag +++
K208Nna+++
F323Ae ++++++
R368Qf na++++
R371Qna+++
R407Qna+++
R408Qna+++
R410Nna+++
K411Nna+++

a The values are deduced from steady state kinetics.25-27,29 Notations, in kcal·mol-1: - = -1.0 to -0.5; 0 = -0.5 to +0.5; + = 0.5 to 1.0; ++ = 1.0 to 1.5; +++ = 1.5 to 2.0; ++++ = > 2.0.

b Mutations K151A and K151Q suggested that K151N induces a conformational change.26

c Mutations E152D and E152Q had similar effects to those of E152A.27

d Mutation W196Q had a mild effect and W196F had no effect.26

e Mutations F323L, -Y and -W showed that the hydrophobic character of Phe323 was essential.29

f Mutation S356A in TyrRS from Acidithiobacillus ferrooxidans (equivalent to S366A in Bst-TyrRS) induces a variation ΔΔGS = 1.2 kcal·mol-1 (ref. 134).

g na, not available.

From: Tyrosyl-tRNA Synthetases

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