isoleucyl-transfer ribonucleate synthetase
Valine, leucine and isoleucine biosynthesis
Zinc-dependent tRNA binding by a peptide element within a tRNA synthetase.
Valyl-tRNA, isoleucyl-tRNA and tyrosyl-tRNA synthetase from baker's yeast. Substrate specificity with regard to ATP analogs and mechanism of the aminoacylation reaction.
A stereochemical and positional isotope exchange study of the mechanism of activation of isoleucine by isoleucyl-tRNA synthetase from Escherichia coli.
NMR analyses of the conformations of L-isoleucine and L-valine bound to Escherichia coli isoleucyl-tRNA synthetase.
Evidence from cassette mutagenesis for a structure-function motif in a protein of unknown structure.
Nonprotein amino acid furanomycin, unlike isoleucine in chemical structure, is charged to isoleucine tRNA by isoleucyl-tRNA synthetase and incorporated into protein.
Understanding structural relationships in proteins of unsolved three-dimensional structure.
Nuclear overhauser effect studies of the conformations of Mg(alpha, beta-methylene)ATP bound to E. coli isoleucyl-tRNA synthetase.
Isoleucyl-tRNA synthetase from the ciliated protozoan Tetrahymena thermophila. DNA sequence, gene regulation, and leucine zipper motifs.
A 15N-1H nuclear magnetic resonance study on the interaction between isoleucine tRNA and isoleucyl-tRNA synthetase from Escherichia coli.
Thiol ligation of two zinc atoms to a class I tRNA synthetase: evidence for unshared thiols and role in amino acid binding and utilization.
Probing the metal binding sites of Escherichia coli isoleucyl-tRNA synthetase.
Residues in a class I tRNA synthetase which determine selectivity of amino acid recognition in the context of tRNA.
C-terminal zinc-containing peptide required for RNA recognition by a class I tRNA synthetase.
Mutational analysis suggests the same design for editing activities of two tRNA synthetases.
Proofreading in trans by an aminoacyl-tRNA synthetase: a model for single site editing by isoleucyl-tRNA synthetase.
Characterization of isoleucyl-tRNA synthetase from Staphylococcus aureus. I: Kinetic mechanism of the substrate activation reaction studied by transient and steady-state techniques.
Enzyme structure with two catalytic sites for double-sieve selection of substrate.
Autonomous folding of a C-terminal inhibitory fragment of Escherichia coli isoleucine-tRNA synthetase.
Insights into editing from an ile-tRNA synthetase structure with tRNAile and mupirocin.
Rational design of femtomolar inhibitors of isoleucyl tRNA synthetase from a binding model for pseudomonic acid-A.
Errors from selective disruption of the editing center in a tRNA synthetase.
The fidelity of the translation of the genetic code.
Editing by a tRNA synthetase: DNA aptamer-induced translocation and hydrolysis of a misactivated amino acid.
Active site of an aminoacyl-tRNA synthetase dissected by energy-transfer-dependent fluorescence.
Structural basis for the recognition of isoleucyl-adenylate and an antibiotic, mupirocin, by isoleucyl-tRNA synthetase.
Mutational separation of two pathways for editing by a class I tRNA synthetase.
Blocking site-to-site translocation of a misactivated amino acid by mutation of a class I tRNA synthetase.
Interstice mutations that block site-to-site translocation of a misactivated amino acid bound to a class I tRNA synthetase.
Crystal structures of the CP1 domain from Thermus thermophilus isoleucyl-tRNA synthetase and its complex with L-valine.
Although this enzyme binds zinc ions, the binding sites are not conserved, away from active sites, suggesting that zinc ions are not involved in catalysis. The detailed catalytic mechanism has not been elucidated yet. However, this enzyme catalyzes two successive transfer reactions. (A) Transfer of the adenylate from ATP (the first substrate) to the carboxylate of the second substrate, isoleucine: This reaction results in the formation of leucinyl-adenylate (intermediate) and the release of the inorganic pyrophosphate. (B) Transfer of the acyl group from the intermediate to the 3'-end of tRNA(Ile).