Aminoacyl-tRNA synthetases: affinity labeling of the ATP binding site by 2', 3' -ribose oxidized ATP.
نویسندگان
چکیده
منابع مشابه
Aminoacyl-tRNA synthetases: affinity labeling of the ATP binding site by 2', 3' -ribose oxidized ATP.
Homogeneous Escherichia coli methionyl-, isoleucyl-, tryptophanyl-, and phenylalanyl-tRNA synthetases and Bacillus stearothermophilus methionyl- and tyrosyl-tRNA synthetases are irreversibly inactivated by reaction of their active ATP sites with the 2',3'-dialdehyde derivative of ATP obtained by periodate oxidation. In each case, the amount of 14C-labeled dialdehyde derivative incorporated per ...
متن کاملAminoacyl-tRNA synthetases database
Aminoacyl-tRNA synthetases (AARSs) are at the center of the question of the origin of life. They constitute a family of enzymes integrating the two levels of cellular organization: nucleic acids and proteins. AARSs arose early in evolution and are believed to be a group of ancient proteins. They are responsible for attaching amino acid residues to their cognate tRNA molecules, which is the firs...
متن کاملRegulation of Angiogenesis by Aminoacyl-tRNA Synthetases
In addition to their canonical roles in translation the aminoacyl-tRNA synthetases (ARSs) have developed secondary functions over the course of evolution. Many of these activities are associated with cellular survival and nutritional stress responses essential for homeostatic processes in higher eukaryotes. In particular, six ARSs and one associated factor have documented functions in angiogene...
متن کاملAminoacyl-tRNA synthetases catalyze AMP----ADP----ATP exchange reactions, indicating labile covalent enzyme-amino-acid intermediates.
Aminoacyl-tRNA synthetases (amino acid-tRNA ligases, EC 6.1.1.-) catalyze the aminoacylation of specific amino acids onto their cognate tRNAs with extraordinary accuracy. Recent reports, however, indicate that this class of enzymes may play other roles in cellular metabolism. Several aminoacyl-tRNA synthetases are herein shown to catalyze the AMP----ADP and ADP----ATP exchange reactions (in the...
متن کاملAcetylation regulates aminoacyl-tRNA synthetases
Previous proteomic analyses have shown that aminoacyl-tRNA synthetases (aaRSs) in many organisms can be modified by acetylation of lysine (Lys). In this present study, leucyl-tRNA synthetase and arginyl-tRNA synthetase from Escherichia coli (EcLeuRS and EcArgRS) were overexpressed and purified, and found to be acetylated on Lys residues by mass spectrometry (MS). Glutamine (Gln) scanning mutage...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1978
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.75.5.2088