‘Half-site’ affinity modification of tryptophanyl-tRNA synthetase leads to ‘freezing’ of the free subunit
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(81)80277-3/fullpdf
Reference21 articles.
1. AMINOACYL-tRNA SYNTHETASES: APPROACHES TO THE STRUCTURE AND FUNCTION OF THE ACTIVE CENTERS
2. [18] Tryptophanyl-tRNA synthetase from beef pancreas
3. Affinity labelling of tryptophanyl-transfer RNA synthetase
Cited by 10 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Part-of-the-sites binding and reactivity in the homooligomeric enzymes – facts and artifacts;Archives of Biochemistry and Biophysics;2018-03
2. Kinetic Anticooperativity in Pre-Steady-State Formation of Tryptophanyl Adenylate by Tryptophanyl-tRNA Synthetase from Beef Pancreas;European Journal of Biochemistry;2005-03-03
3. Kinetic evidence for half-of-the-sites reactivity in tRNATrp aminoacylation by tryptophanyl-tRNA synthetase from beef pancreas;Biochemistry;1986-11-04
4. Pyrophosphate-caused inhibition of the aminoacylation of tRNA by the leucyl-tRNA synthetase from Neurospora crassa;European Journal of Biochemistry;1986-10
5. Substrate depletion analysis as an approach to the pre-steady-state anticooperative kinetics of aminoacyl adenylate formation by tryptophanyl-tRNA synthetase from beef pancreas;Biochemistry;1984-04-10
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