期刊论文详细信息
FEBS Letters
Role of lysine‐195 in the KMSKS sequence of E. coli tryptophanyl‐tRNA synthetase
Koeppe, Roger E.1  Chan, Kim W.1 
[1] Department of Chemistry and Biochemistry, 103 Chemistry Building, University of Arkansas, Fayetteville, AR 72701, USA
关键词: Aminoacyl-tRNA synthetase;    Mononucleotide binding fold;    KMSKS sequence;    Kinetics;    Overexpression;    Mutagenesis;    aaRS;    aminoacyl-tRNA synthetase(s);    TrpRS;    tryptophanyl-tRNA synthetase;    TrpRS;    tyrosyl-tRNA synthetase;    HIGH;    His-Ile-Gly-His sequence;    TIGN;    Thr-Ile-Gly-Asn sequence;    KMSKS;    Lys-Met-Ser-Lys-Ser sequence;    KFGKT;    Lys-Phe-Gly-Lys-Thr sequence;   
DOI  :  10.1016/0014-5793(95)00274-D
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
PDF
【 摘 要 】

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 k cat in a pyrophosphate-ATP exchange reaction. This large decrease in k cat 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 reactions.

【 授权许可】

Unknown   

【 预 览 】
附件列表
Files Size Format View
RO201912020300942ZK.pdf 472KB PDF download
  文献评价指标  
  下载次数:9次 浏览次数:9次