| Literature DB >> 6840095 |
G Winter, G L Koch, B S Hartley, D G Barker.
Abstract
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.Entities:
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Year: 1983 PMID： 6840095 DOI： 10.1111/j.1432-1033.1983.tb07374.x
Source DB: PubMed Journal: Eur J Biochem ISSN： 0014-2956