Conformational activation of the yeast phenylalanyl-tRNA synthetase catalytic site induced by tRNAPhe interaction: triggering of adenosine or CpCpA trinucleoside diphosphate aminoacylation upon binding of tRNAPhe lacking these residues.
Adenosine or CpCpA trinucleoside diphosphate can be aminoacylated by phenylalanyl-tRNA synthetase [L-phenylalanine:tRNAPhe ligase (AMP forming), EC 6.1.1.20] when the reaction takes place in the presence of tRNAPhe deprived of its 3' adenosine or pCpCpA terminus. This shows that, upon interaction with tRNA, a structural alteration of the enzyme's active site is achieved. This process may be a determining step in the specificity of the aminoacylation reaction.
D000241:Adenosine; D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D001665:Binding Sites; D009841:Oligonucleotides; D010652:Phenylalanine-tRNA Ligase / Q000378:metabolism*; D011485:Protein Binding; D012343:RNA, Transfer / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013379:Substrate Specificity
D009841:Oligonucleotides; C029986:cytidylyl-cytidylyl-adenosine; D012343:RNA, Transfer; D000604:Amino Acyl-tRNA Synthetases; D010652:Phenylalanine-tRNA Ligase; D000241:Adenosine