Determination of tryptophan tRNA recognition sites for tryptophanyl-tRNA synthetase from hyperthermophilic archaeon, Aeropyrum pernix K1.
Article Details
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Tsuchiya W, Umehara T, Kuno A, Hasegawa T
Determination of tryptophan tRNA recognition sites for tryptophanyl-tRNA synthetase from hyperthermophilic archaeon, Aeropyrum pernix K1.
Nucleic Acids Symp Ser (Oxf). 2004;(48):185-6.
- PubMed ID
- 17150540 [ View in PubMed]
- Abstract
To investigate the recognition mechanism of tryptophan tRNA by tryptophanyl-tRNA synthetase from extreme hyperthermophilic and aerobic archaeon, Aeropyrum pernix K1, tryptophanylation activities were examined by using mutant tryptophan tRNA transcripts prepared by in vitro transcription system. Their transcripts were aminoacylated with tryptophan by overexpressed A. pernix tryptophanyl-tRNA synthetase. The results indicated that anticodon nucleotides C34, C35 and A36, discriminator base A73, G1-C72 and G2-C71 base pairs of acceptor stem were base-specifically recognized by A. pernix tryptophanyl-tRNA synthetase.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Tryptophan Tryptophan--tRNA ligase Protein Geobacillus stearothermophilus UnknownInhibitorDetails Tryptophan Tryptophan--tRNA ligase, cytoplasmic Protein Humans UnknownInhibitorDetails - Drug Enzymes
Drug Enzyme Kind Organism Pharmacological Action Actions Tryptophan Tryptophan--tRNA ligase Protein Geobacillus stearothermophilus UnknownSubstrateInhibitorDetails Tryptophan Tryptophan--tRNA ligase, cytoplasmic Protein Humans UnknownSubstrateInhibitorDetails