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. | |
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【 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 】
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