期刊论文详细信息
FEBS Letters | |
Phenylalanyl‐tRNA synthetase from Thermus thermophilus can attach two molecules of phenylalanine to tRNAPhe | |
Lavrik, Ol'ga I.1  Moor, Nina A.1  Ankilova, Valentina N.1  Stepanov, Victor G.1  | |
[1] Novosibirsk Institute of Bioorganic Chemistry, Siberian Division of the Russian Academy of Sciences, Lavrentiev Prospect 8, 630090, Novosibirsk, Russia | |
关键词: Phenylalanyl-tRNA synthetase; tRNAPhe; tRNA aminoacylation; PheRSase; phenylalanyl-tRNA synthetase (EC 6.1.1.20); hyper-Phe∼tRNA; tRNA phenylalanylated above 100%; Phe∼tRNA; normally phenylalanylated tRNA; RNase A; ribonuclease A; | |
DOI : 10.1016/0014-5793(92)81099-8 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Phenylalanyl-tRNA synthetase from the extreme thermophilic bacterium Thermus thermophilus can incorporate more than one molecule of phenylalanine into the tRNAPhe. It is shown that the ‘hyperaminoncylated’ tRNAPPhe is the bis-2′,3′-O-phenylalanyl-tRNAPhe, and its formation is typical for the thermophilic enzyme but does not occur for E. coli phenylalanyl-tRNA synthetase under the same conditions.
【 授权许可】
Unknown
【 预 览 】
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