Role of lysine‐195 in the KMSKS sequence of E. coli tryptophanyl‐tRNA synthetase
- 17 April 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 363 (1-2), 33-36
- https://doi.org/10.1016/0014-5793(95)00274-d
Abstract
Lysine 195 in the K195 MSKS sequence of E. coli tryptophanyl-tRNA synthetase (TrpRS) was replaced with alanine. The resulting K195A mutant TrpRS had essentially unchanged Km values for ATP and Trp, but a 1500-fold decreased kcat in a pyrophosphate-ATP exchange reaction. This large decrease in kcat reduces the rate of aminoacyladenylate formation (step 1) to a rate comparable to the rate of aminoacylation of tRNATTrp (step 2) by the K195A mutant enzyme. Both the TIGN and KMSKS sequences are important for step 1 of class I aminoacyl-tRNA synthetase reactionsKeywords
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