The amino acid sequence of the tyrosyl-tRNA synthetase from Bacillus stearothermophilus.
The amino acid sequence of the tyrosyl-tRNA synthetase from Bacillus stearothermophilus.
复制标题
嗜热脂肪芽孢杆菌酪氨酰-tRNA 合成酶的氨基酸序列。
DOI:
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发表时间:
1983
期刊:
影响因子:
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通讯作者:
David G. Barker
中科院分区:
文献类型:
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作者:
Greg Winter;Gordon L. E. Koch;Brian S. Hartley;David G. Barker
The primary structure of the tyrosyl-tRNA synthetase (TyrTS) of Bacillus stearothermophilus has been deduced from the nucleotide sequence of the cloned gene and from the amino acid sequence of peptides isolated from the purified enzyme. TyrTS (B. stearothermophilus) has a molecular weight of 47316 and the sequence is 56% homologous with that of TyrTS (Escherichia coli). The binding domain for the substrate intermediate tyrosyl adenylate is located in the N-terminal portion of the polypeptide and is highly conserved in both enzymes. Several lysine residues, which are shielded from acetylation in the TyrTS-tRNATyr complex, are also located in a stretch of highly conserved sequence.
DOI:
10.1126/science.7025207
发表时间:
1981
期刊:
Science (New York, N.Y.)
影响因子:
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作者:
Putney,SD;Royal,NJ;NeumandeVegvar,H;Herlihy,WC;Biemann,K;Schimmel,P
通讯作者:
Schimmel,P