PMID:2009959
| Citation |
Anselme, J and Härtlein, M (1991) Tyr-426 of the Escherichia coli asparaginyl-tRNA synthetase, an amino acid in a C-terminal conserved motif, is involved in ATP binding. FEBS Lett. 280:163-6 |
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| Abstract |
Sequence comparisons of the E. coli asparaginyl-tRNA synthetase (NRSEC) with aminocyl-tRNA synthetase sequences of class II enzymes show significant homologies with aspartyl- and lysyl-tRNA synthetases. Three conserved regions were found, one of which is located in the C-terminal part of the NRSEC sequence. Site-directed mutagenesis was performed in this conserved region. A single point mutation Tyr-426----Ser results in a 15-fold increase in the Km for ATP, while all the other kinetic parameters remain unchanged. The replacement of this Tyr-426 by a Phe does not affect the kinetic behaviour of the enzyme. These data indicate that Tyr-426 is part of the ATP binding site. |
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| Keywords |
Adenosine Triphosphate/metabolism; Amino Acid Sequence; Amino Acyl-tRNA Synthetases/genetics; Amino Acyl-tRNA Synthetases/metabolism; Aspartate-tRNA Ligase; Base Sequence; Cloning, Molecular; Escherichia coli/enzymology; Escherichia coli/genetics; Genes, Bacterial; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; RNA, Transfer, Amino Acyl; Sequence Homology, Nucleic Acid; Substrate Specificity; Tyrosine/chemistry; Tyrosine/metabolism |
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