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pmid: 789364
The role of cations (polyamines and Mg2+) in isoleucyl-tRNA formation catalyzed by purified isolecuyl-tRNA synthetase [EC 6.1.1.5] from Escherichia coli was studied. It was found that spermine, spermidine, and Mg2+ bind to tRNA and that when bound to these cations, tRNA acts as substrate of aminoacylation without requiring further cations. These findings suggest that the primary function of cations in aminoacyl-tRNA formation is to bind to tRNA to stabilize its structure, not to bind to the enzyme to activate it.
Isoleucine-tRNA Ligase, Binding Sites, Spermidine, RNA, Transfer, Escherichia coli, Polyamines, Magnesium, Spermine, Transfer RNA Aminoacylation, Isoleucine
Isoleucine-tRNA Ligase, Binding Sites, Spermidine, RNA, Transfer, Escherichia coli, Polyamines, Magnesium, Spermine, Transfer RNA Aminoacylation, Isoleucine
citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 9 | |
popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Average | |
influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Average | |
impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Average |